Proteinuria: Changes and Mechanisms in Toxic Nephropathies

References

• Misra R. P., Berman L. B. The molecular basis of proteinuria. JAMA 1979; 242: 757
   PubMedGoogle Scholar
• Ludwig C. Beitrage zur Lehre vom Mechanismus der Harnsecretion. Elwert, Marburg 1843; 1
   Google Scholar
• Bright R. Original Papers of Richard Bright on Renal Disease, Osman. Oxford University Press, London 1937; 78
   Google Scholar
• Wearn J. T., Richards A. N. Observations on the composition of giomerular urine, with particular reference to the problem of reabsorption in the renal tubule. Am. J. Physiol. 1924; 71: 209
   Google Scholar
• Walker A. M. Comparison of total molecular concentration of giomerular urine and blood plasma from the frog and necturus. J. Biol. Chem. 1930; 87: 499
   Google Scholar
• Walker A. M., Blott A. P., Oliver J., MacDonald M. C. The collection and analysis of fluid from single nephrons of the mammalian kidney. Am. J. Physiol. 1941; 134: 580
   Google Scholar
• Harris C. A., Bauer P. G., Chirito E., Dirkes J. H. Composition of mammalian giomerular filtrate. Am. J. Physiol. 1974; 227: 971
   Google Scholar
• Mondorf A. W., Scherberich J. E., Stefanescu T., Mitron P. S., Schoeppe W. Elimination of brush border membrane protein in urine caused by toxic alterations of the tubular cell. Contrib. Nephrol. 1981; 24: 99
   PubMedGoogle Scholar
• Thompson R. E., Piper D. J., Galberg C., Chan T. H., Tolkoff-Rubin N. E., Rubin R. H. Adenosine deaminase binding protein, a new diagnostic marker for kidney disease. Clin. Chem. 1985; 31: 679
   PubMed Web of Science ®Google Scholar
• Feinfeld D. A., Bourgoignie J. J., Fleischner G., Goldstein E. J., Biempica L., Arias I. M. Ligandinuria in nephrotqxic acute tubular necrosis. Kidney int. 1977; 12: 387
   PubMed Web of Science ®Google Scholar
• Taniguchi N., Tanaka M., Kishihara C., Ohno H., Rondo T., Matsuda I., Fujiiio T., Harada M. Determination of carbonic anhydrase C and bta2-microglobulin by radioimmunoassay in urine of heavy-metal-exposed subjects and patients with renal tubular acidosis. Environ. Res. 1979; 20: 154
   PubMed Web of Science ®Google Scholar
• Falkenberg F. W., Mai U., Puppe C., Risse P., Hermann G., Kicking E., Bremer K., Mondorf A., Shapira Z. Kidney derived urinary antigens assayed with monoclonal antibodies for the detection of renal damage. Clin. Chim. Acta 1986; 160: 171
   PubMedGoogle Scholar
• Mutti A., Lucertini S., Valcavi P. P., Neri T. M., Fornarni M., Alinovi V., Franchini I. Urinary excretion of brush-border antigens: early indicator of toxic nephropathy. Lancet 1985; ii: 914
   Google Scholar
• Hoyer J. H., Sisson S. P., Vernier M. D. Tamm-Horsfall glycoprotein ultrastructural immunoperoxidase localization in rat kidney. Lab. Invest. 1979; 41: 168
   PubMedGoogle Scholar
• Ravnskov U. Low molecular weight proteinuria in association with paroxysmal myoglobinuria. Clin. Nephrol. 1975; 3: 65
   PubMedGoogle Scholar
• Durst A., Dishon R., Rosenmann E. Excretion of liver antigens in experimental hepatitis. Lab. Invest. 1971; 25: 35
   PubMedGoogle Scholar
• Hall R. R., Lawrence D. J. P., Duray D., Stevens U., James R., Roberts S., Manzo Neville S. Carcino-embryonic antigen in the urine of patients with urothelial carcinomas. Br. Med. J. 1972; 3: 609
   PubMed Web of Science ®Google Scholar
• Lillehof E. P., Poulik M. D. Normal and abnormal aspects of proteinuria. I. Mechanisms, characteristics and analyses of urinary protein. Exp. Pathol. 1986; 29: 1
   PubMedGoogle Scholar
• Henry R. J., Sobel C., Segolove M. Turbidimetric determination of proteins with sulfosalicylic and trichloroacetic acids. Proc. Soc. Exp. Biol. 1956; 92: 748
   PubMed Web of Science ®Google Scholar
• Iwata J., Nishikadze O. New micro-rurbidimetric methods for determination of protein in cerebrospinal fluid and urine. Clin. Chem. 1979; 25: 1317
   PubMed Web of Science ®Google Scholar
• Miller A., Greif R., Beckntann W. Determination of protein in the urine by the Biuret method. J. Biol. Chem. 1948; 176: 1421
   PubMedGoogle Scholar
• Saifer A., Gerstenfeld S. Photometric determination of urinary proteins. Clin. Chem. 1964; 10: 321
   PubMedGoogle Scholar
• McLntosch J. C. Application of a dye-binding method to the determination of protein in urine and cerebrospinal fluid. Clin. Chem. 1977; 23: 1939
   PubMedGoogle Scholar
• Meola J. M., Vargas M. A., Brown H. H. Simple procedure for measuring total protein in urine. Clin. Chem. 1977; 23: 975
   PubMedGoogle Scholar
• Yatzidis H. New colorimetric method for quantitative determination of protein in urine. Clin. Chem. 1977; 23: 811
   PubMed Web of Science ®Google Scholar
• Doetsch K., Gadsden R. H. Determination of total urinary protein, combining Lowry sensitivity and Biuret specificity. Clin. Chem. 1973; 19: 1170
   PubMedGoogle Scholar
• McElderry C. A., Tarbit I. F., Cassells-Smith A. J. Six methods for urinary protein compared. Clin. Chem. 1982; 28: 356
   PubMed Web of Science ®Google Scholar
• Uena D B.A., Penberthy L. A., Fraser G. C. Six methods for determining urinary protein compared. Clin. Chem. 1983; 29: 553
   PubMedGoogle Scholar
• Anderson N. C., Anderson N. L., Tollaksen S. L., Hahn H., Cicre F., Edwards J. Analytical techniques for cell fractions. XXV. Concentration and 2-D electrophoretic analysis of urinary proteins. Anal. Biochem. 1979; 95: 48
   PubMed Web of Science ®Google Scholar
• Piscator M. Proteinuria in chronic cadmium poisoning. III. Electrophoretic and immunoelectrophoretic studies on urinary proteins for cadmium workers with special reference to the excretion of low molecular weight proteins. Arch. Environ. Health 1966; 12: 335
   PubMedGoogle Scholar
• Lauwerys R., Buchet J. P., Reels H. Epidemiological survey of workers exposed to cadmium. Arch. Environ. Health 1974; 28: 145
   PubMed Web of Science ®Google Scholar
• Bernard A., Reels H., Hubermont G., Buchet J. P., Masson P. L., Lauwerys R. Characterization of the proteinuria in cadmium exposed workers. Int. Arch. Occup. Environ. Health 1976; 38: 19
   PubMed Web of Science ®Google Scholar
• Fafck F. Y., Keren D. F., Fine L. J., Smith R. G., McClatchey K. D., England B., Annesley T. Protein excretion patterns in cadmium-exposed individuals: high resolution electrophoresis. Arch. Environ. Health 1984; 39: 69
   PubMedGoogle Scholar
• Foa V., Caimi L., Amanti L., Antonini C., Gattinoni A., Tettamanti G., Lombardo A., Giulani A. Patterns of some lysosomal enzymes in the plasma and of proteins in urine of workers exposed to inorganic mercury. Int. Arch. Occup. Environ. Health 1976; 37: 115
   PubMed Web of Science ®Google Scholar
• Bernard A., Goret A., Buchet J. P., Roels H., Lauwerys R. Comparison of sodium dodecyl sulfate polyacrylamide gel electrophoresis with quantitative methods for the analysis of cadmiuminduced proteinuria. Int. Arch. Occup. Environ. Health 1979; 44: 139
   PubMed Web of Science ®Google Scholar
• Stonard M. D., Chater B. V., Duffield D. P., Nevitt A. L., O'Sullivan J. J., Steel G. T. An evaluation of renal function in workers occupationally exposed to mercury vapour. Int. Arch. Occup. Environ. Health 1983; 52: 177
   PubMed Web of Science ®Google Scholar
• Fleming J. J. Comparison of tubular proteinuria using sodium dodecyl sulphate polyacrylamide gel electrophoresis in patients during methotrexate of aminoglycoside treatment or with cadmium of Balkan nephropathy. Clin. Chim. Acta 1984; 140: 267
   PubMedGoogle Scholar
• Vesterberg O., Nise G., Hansen L. Urinary proteins in occupational exposure to chemicals and in diseases. J. Occup. Med. 1976; 18: 473
   PubMedGoogle Scholar
• Anderson N. C., Anderson N. L., Tollaksen S. L. Proteins of human urine. I. Concentration and analysis by two-dimensional electrophoresis. Clin. Chem. 1979; 25: 1999
   Google Scholar
• Lindblom H., Axio-Fredriksson U. B., Cooper E. H., Turner R. Separation of urine proteins on the anion-exchange resin Mono Q. J. Chromatogr. 1983; 273: 13
   Google Scholar
• Turpeinen U., Koivanen E., Stenman U. H. Liquid chromatographic determination of btarmicroglobulin, alphai-acid glycoprotein and albumin in urine. Clin. Chem. 1987; 33: 1756
   PubMedGoogle Scholar
• Evrin P. E., Peterson P. A., Wide L., Berggård I. Ra-dioimmunoassay of btai-microglobulin in human biological fluids. Scand. J. Clin. Lab. Invest. 1971; 28: 439
   PubMed Web of Science ®Google Scholar
• Ferrna B., Vincent C., Revillard J. P. A sandwich method of enzyme immunoassay. HI. Assay for human bta2-microglobulin compared with radioimmunoassay. J. Immunol. Methods 1980; 36: 149
   PubMedGoogle Scholar
• Playford R. J., Dawnay A., Cattell W. R., Landon J. The development of a fluoroimmunoassay for bta2-microglobulin in serum. Ann. Clin. Biochem. 1985; 22: 166
   PubMed Web of Science ®Google Scholar
• Bernard A., Lauwerys R. Continuous flow-system for the automation of latex immunoassay by particle counting. Clin. Chem. 1983; 29: 1007
   PubMed Web of Science ®Google Scholar
• Bernard A., Vyskocil P., Lauwerys R. Determination of bta2-microglobulin in human urine and serum by latex immunoassay. Clin. Chem. 1981; 27: 382
   Google Scholar
• Vesterberg O. Protein quantification with zone immunoelectro-phoresis assay (ZIA). Modern Methods in Protein Chemistry. Walter de Gruyter, Berlin 1983; 187
   Google Scholar
• Tanun I., Horsfall F. L., Jr. Characterization and separation of an inhibitor of viral hemogglutination present in urine. Proc. Soc. Exp. Biol. Med. 1950; 74: 108
   Google Scholar
• Pennies D., Khor W. J., Kuang W. J., Glaister D., Aggarwal B. B., Chen E. Y., Goeddel D. V. Identification of human uromodulin as the Tamm-Horsfall urinary glycoprotein. Science 1987; 236: 83
   PubMedGoogle Scholar
• Thonüey G., Dawnay A., Cattell W. R. Human Tamm-Horsfall glycoprotein: urinary and plasma levels in normal subjects and patients with renal disease determined by a fully validated radioimmunoassay. Clin. Sci. 1985; 68: 529
   Google Scholar
• Elving L. O., Bakkeren J. A. J. M., Jansen M. J. H., de Kat Angelino C. M., de Nobel E., van Monster P. J. J. Screening for microalbuminuria in patients with diabetes mellitus: frozen storage of urine samples decreases their albumin content. Clin. Chem. 1989; 35: 308
   PubMed Web of Science ®Google Scholar
• Mogensen C. E., Soiling K. Studies of renal tubular protein absorption: partial and near complete inhibition by certain amino acids. Scand. J. Clin. Lab. Invest. 1977; 37: 477
   PubMed Web of Science ®Google Scholar
• Trivin F., Giraudet P. “Microalbuminuria” or “Paucialbuminuria”. Clin. Chem. 1988; 34: 209
   PubMedGoogle Scholar
• Mogensen C. E. Microalbuminuria as a predictor of clinical diabetic nephropathy. Kidney Int. 1987; 31: 673
   PubMed Web of Science ®Google Scholar
• Peterson P. A., Evrin P. E., Berggård I. Differentiation of glomerular, tubular and normal proteinuria: determinations of urinary excretion of bta2-microglobulin, albumin and total protein. J. Clin. Invest. 1969; 48: 1189
   PubMed Web of Science ®Google Scholar
• Bernard A., Viau C., Ouled A., Lauwerys R. Competition between low and high molecular weight proteins for renal tubular uptake. Nephron 1987; 47: 115
   Google Scholar
• Bernard A., Ouled A., Viau C., Lauwerys R. The renal uptake of proteins: a nonselective process as evidenced by com-petition experiments in conscious rats. Kidney Int. 1988; 34: 175
   PubMed Web of Science ®Google Scholar
• Ghiggeri G. M., Candiano G., Delflno G., Bianchini F., Queirolo C. Glycosylated albumin and diabetic microalbuminuria: demonstration of an altered renal handling. Kidney Int. 1984; 25: 565
   PubMed Web of Science ®Google Scholar
• Deen W. M., Sitvat B. Determinants of the glomerular filtration of proteins. Am. J. Physiol. 1981; 241: F162
   PubMedGoogle Scholar
• Coimbray T. M., Lachat J. J. Analysis of urinary albumin excretion in gentamicin treated rats. Nephron 1988; 40: 154
   Google Scholar
• Bernard A., Ouled-Amor A., Goemare-Vanneste J., Antoine J. L., Lauwerys R. R., Lambert A., Vandeleene B. Microtransferrinuria: a more sensitive indicator of early glomerular damage in diabetes than microalbuminuria. Clin. Chem. 1988; 34: 1220
   Google Scholar
• Bernard A., Ouled-Amor A., Goemare-Vanneste J., Antoine J. L., Lauwerys R., Colin L, Vandeleene B., Lambert A. Urinary proteins and red blood cell membrane negative charges in diabetes mellitus. Clin. Chim. Acta 1990; 190: 249
   PubMedGoogle Scholar
• Cheung C. K., Cockran J. S., Yeung V. T. F., Swaminothan R. Urinary excretion of transferrin by non-insulin dependent diabetics, a marker for early complications. Clin. Chem. 1989; 35: 1672
   PubMed Web of Science ®Google Scholar
• McConnick C. P., Konen J. C., Shihabi Z. K. Microtransferrinuria and microalbuminuria. I. In the diabetic human. Clin. Physiol. Biochem. 1990; 8: 53
   PubMedGoogle Scholar
• Bernard A., Roels H., Cardenas A., Lauwerys R. Assessment of urinary protein 1 and transferrin as early markers of cadmium nephrotoxicity. Br. J. Ind. Med. 1990; 47: 559
   PubMedGoogle Scholar
• Bernard A., Lauwerys R., Chia K. S. Latex immunoassay of urinary transferrin, submitted
   Google Scholar
• Pedersen E. B., Mogensen C. E., Selling K., Andersen A., Darling S. Urinary excretion of albumin, bta2-microglobulin and free light chains during lithium treatment. Scand. J. Clin. Lab. Invest. 1978; 38: 269
   PubMedGoogle Scholar
• Deen W. M., Bridges C. R., Brenner B. M., Myers B. D. Heteroporous model of glomerular size selectivity, application to normal and nephrotic humans. Am. J. Physiol. 1985; 249: 374
   PubMedGoogle Scholar
• Nakamura Y., Myers B. P. Charge selectivity of proteinuria in diabetic nephropathy. Diabetes 1988; 37: 1202
   PubMed Web of Science ®Google Scholar
• Deckert T., Feldt-Rasmussen B., Djurup R., Deckert M. Glomerular size and charge selectivity in insulin-dependent diabetes mellitus. Kidney Int. 1988; 33: 100
   PubMed Web of Science ®Google Scholar
• Berggård I., Beam A. G. Isolation and properties of a low molecular weight bta2-globulin occurring in human biological fluids. J, Biol. Chem. 1968; 243: 4095
   PubMed Web of Science ®Google Scholar
• Bernard A., Vyskocil A., Mahieu P., Lauwerys R. Assessment of urinary retinal-binding protein as index of tubular damage. Clin. Chem. 1987; 33: 775
   PubMed Web of Science ®Google Scholar
• Evrin P. E., Wibell L. The serum levels and urinary excretion of béta2-microglobulin in apparently healthy subjects. Scand. J. Clin. Lab. Invest. 1972; 29: 69
   PubMed Web of Science ®Google Scholar
• Wibell L., Evrin P. E. The urinary excretion of bta2-microglobulin in renal disorders. Protides Biol. Fluids 1973; 21: 519
   Google Scholar
• Kanai M., Raz A., Goodman O. S. Retinol-binding protein: the transport protein for vitamin A in human plasma. J. Clin. Invest. 1968; 47: 2029
   Google Scholar
• Peterson P. A., Berggård I. Isolation and properties of a human retinol-transporting protein. J. Biol. Chem. 1971; 246: 25
   PubMed Web of Science ®Google Scholar
• Goodman D. S. Biosynthesis, absorption and hepatic metabolism of retinoi. The Retinoids, M. B. Spom, A. B. Roberts, D. S. Goodman. Academic Press, Orlando, FL 1984; Vol. 2: 40
   Google Scholar
• Bernard A., Vyskocil A., Mahieu P., Lauwerys R. Effect of renal insufficiency in the concentration of free retinol-binding protein in urine and serum. Clin. Chim, Acta 1987; 85: 171
   Google Scholar
• Bernard A., Lauwerys R. Retinoi binding protein in urine: a more practical index than urinary β2-microglobulin for the routine screening of renal tubular function. Clin. Chem. 1986; 21: 1781
   Google Scholar
• Topping M., Forster H. W., Dolman C., Luczynska C., Bernard A. Measurement of urinary retinol-binding protein by enzyme linked immuno-sorbent assay and its application to detection of tubular proteinuria. Clin. Chem. 1986; 32: 1863
   PubMedGoogle Scholar
• Bernard A., Moreau D., Lauwerys R. Latex immunoassay of retinol-binding protein. Clin. Chem. 1982; 28: 1167
   PubMedGoogle Scholar
• Beetham R., Dawnay A., London J., Cattell W. R. A radioimmunoassay for retinol-binding protein in serum and urine. Clin. Chem. 1985; 31: 1364
   PubMed Web of Science ®Google Scholar
• Ekström B., Peterson P. A., Berggård L. A urinary and plasma glycoprotein of low molecular weight: isolation and some properties. Biochem. Biophys. Res. Commun. 1975; 65: 1427
   PubMedGoogle Scholar
• Yu H., Yanagisawa Y., Forbes M. A., Cooper E. H., Crock-Son R. A., MacLennan I. C. M. Alpha l-microglobulin: an indicator for renal tubular function. J. Clin. Pathol. 1983; 36: 253
   PubMed Web of Science ®Google Scholar
• Donaldson M. D. C., Chambers R. E., Woolridge M. W., Whicher J. T. Stability of alfa,-microglobulin, bta2-microglobulin, retinol-binding protein in urine. Clin. Chim. Acta 1989; 179: 73
   PubMed Web of Science ®Google Scholar
• Osserman E. F. Lysozymuria in renal and non-renal diseases, part IV. Proteins in Normal and Pathological Urine, Y. Manuel, J. P. Revillard, H. Betuel. University Park Press, Baltimore 1970; 180
   Google Scholar
• Litwack G. Photometric determination of lysozyme activity. Proc. Soc. Exp. Biol. Med. 1955; 89: 401
   PubMed Web of Science ®Google Scholar
• Brouwer J., van Leeuwen-Herberts, van de Ruit O. Determination of lysozyme in serum, urine, cerebrospinal fluid and feces by enzyme immunoassay. Clin. Chim. Acta 1984; 142: 21
   PubMed Web of Science ®Google Scholar
• Bernard A., Lauwerys R., Noel A., Vendeleene B., Lambert A. Urine protein 1: a sex dependent marker of tubular or glomerular dysfunction. Clin. Chem. 1989; 35: 2141
   PubMed Web of Science ®Google Scholar
• Bernard A., Lauwerys R., Noel A., Vandeleene B., Lam-Bert A. E. Determination by latex immunoassay of protein 1 in normal and pathological urine, submitted
   Google Scholar
• Clausen J. Proteins in normal cerebrospinal fluid rat found in serum. Proc. Soc. Exp. Biol. Med. 1961; 107: 170
   PubMed Web of Science ®Google Scholar
• Butler E. A., Flynn F. V. The occurrence of post-gamma globulin protein in urine: a new protein abnormality. J. Clin. Pathol. 1961; 14: 172
   PubMed Web of Science ®Google Scholar
• Poulik M. D., Perry D. J., Voka E., Sekine T. Post-gamma globulin. II. Radioimmunoassay determination of levels of post-gamma globulin and bta2-microglobulin. Clin. Chim. Acta 1983; 128: 249
   PubMed Web of Science ®Google Scholar
• Gauthier F., Pagano M., Esnard F., Mouray H., Engler R. A heat stable low molecular weight inhibitor of lysosomal cystein proteinases in human serum. Biochem. Biophys. Res. Commun. 1983; 110: 449
   PubMedGoogle Scholar
• Whitsed M., Penny R. Beta-trace protein purification and urinary excretion studies in selected diseases. Clin. Chim. Acta 1974; 50: 111
   PubMedGoogle Scholar
• Aderka D., Tene M., Graff E., Levo Y. Amylase-creatinine clearance ratio. A simple test to predict gentamycin nephrotoxicity. Arch. Intern. Med. 1988; 148: 1093
   PubMedGoogle Scholar
• Soelling K., Mogensen Ch., Vittinghus E., Brock A. The renal handling of amylase in normal man. Nephron 1979; 23: 282
   PubMedGoogle Scholar
• Mohos S. C., Skoza L. Histochemical demonstration and localization of sialoproteins in the glomerulus. Exp. Med. Pathol. 1970; 12: 316
   PubMedGoogle Scholar
• Rodewald R., Karnovsky M. J. Porous substructure of the glomerular slit diaphragm in the rat and mouse. J. Cell Biol. 1974; 60: 423
   PubMed Web of Science ®Google Scholar
• Kanwar Y. S. Biology of disease. Biophysiology of glomerular filtration and proteinuria. Lab. Invest. 1984; 51: 1
   PubMedGoogle Scholar
• Abrahamson D. R. Recent studies on the structure and pathology of basement membranes. J. Pathol. 1986; 149: 257
   PubMed Web of Science ®Google Scholar
• Kanwar Y. S., Farquhar M. G. Isolation and glycosaminoglycans (heparan sulfate) from glomerular basement membranes. Proc. Nail. Acad. Sci. U.S.A. 1979; 76: 4493
   PubMed Web of Science ®Google Scholar
• Caulfield J. P., Farquhar M. G. Distribution of anionic sites in glomerular basement membranes: their possible role in filtration and attachment. Proc. Natl. Acad. Sci. U.S.A. 1976; 73: 1646
   PubMedGoogle Scholar
• Kanwar Y. S., Farquhar M. G. Anionic sites in the glomerular basement membrane:in vivo andin vitro localization to the lamina rarae by cationic probes. J. Cell Biol. 1979; 81: 137
   PubMed Web of Science ®Google Scholar
• Kanwar Y. S., Rosenzweig L. J. Clogging of the glomerular basement membrane. J. Cell Biol. 1982; 93: 489
   PubMedGoogle Scholar
• Ota Z., Makivo H., Miyoshi A., Hiramatsu M., Takahashi K., Ofuji T. Molecular sieve in glomerular basement as revealed by electron microscopy. J. Electron. Microsc. 1978; 28: 20
   Google Scholar
• Latta H., Johnston W. H., Stanley T. M., Sykes E. Sialoglycoproteins and filtration barrier in the glomerular capillary wall. J. Vltrastruc. Res. 1975; 51: 354
   PubMedGoogle Scholar
• Kerjaschki D., Sharkey D. J., Farquhar M. G. Identification and characterization of podocalyxin, the major sialoprotein of the renal glomerular epithelial cell. J. Cell Biol. 1984; 98: 1591
   PubMed Web of Science ®Google Scholar
• Seiler M. W., Rennke H. G., Venkatachalam M. A., Cotran R. S. Pathogenesis of polycation-induced alterations (“fusion”) of glomerular epithelium. Lab. Invest. 1977; 36: 48
   PubMed Web of Science ®Google Scholar
• Maack T., Johnson V., Kau S., Figueirido J., Siguelin D. Renal filtration, transport and metabolism of low molecular weight proteins. A review. Kidney Int. 1979; 16: 251
   PubMed Web of Science ®Google Scholar
• Brewer D. B. Renal clearances of dextran of varying molecular weight. Proc. R. Soc. Med. 1951; 44: 561
   PubMedGoogle Scholar
• Pappenheimer J. R. Passage of molecules through capillary walls. Physiol. Rev. 1953; 33: 387
   PubMed Web of Science ®Google Scholar
• Walenius G. Renal clearance of dextran as a measure of glomerular permeability. Acta Soc. Meet. Ups. Suppl. 1954; 4: 1
   Google Scholar
• Hardwicke J., Hulme B., Jones J. H., Ricketts C. R. Measurement of glomerular permeability to polydisperse radioactivity-labelled macromolecules in normal rabbits. Clin. Sci. 1968; 34: 505
   PubMed Web of Science ®Google Scholar
• Arturson G., Groth T., Grotte G. Human glomerular membrane porosity and filtration pressure: dextran clearance data analyzed by theoretical models. Clin. Sci. 1971; 40: 137
   PubMed Web of Science ®Google Scholar
• Renkin E. M., Robinson R. R. Glomerular filtration. N. Engl. J. Med. 1974; 299: 785
   Google Scholar
• Chang R. L. S., Robertson C. R., Deen W. M., Brenner B. M. Permselectivity of the glomerular capillary wall to macro-molecules. I. Theoretical considerations. Biophys. J. 1975; 15: 861
   PubMedGoogle Scholar
• Brenner B. M., Bohrer M. P., Baylis C., Deen W. M. Determinants of glomerular permselectivity: insights derived from observations in vivo. Kidney Int. 1977; 12: 229
   PubMed Web of Science ®Google Scholar
• Deen W. M., Bohrer M. D., Robertson C. R., Brenner B. M. Determinations of the transglomerular passage of macro-molecules. Fed. Proc. 1977; 36: 2614
   PubMedGoogle Scholar
• Laurent T. C., Killander J. A theory of gel filtration and its experimental verification. J. Chromatogr. 1964; 14: 317
   Web of Science ®Google Scholar
• Lambert P. P., Du Bois R., de Coodt P., Verniory A. Determination of glomerular intracapillary and transcapillary pressure gradients from sieving data. II. A physiological study in the normal dog. Pflugers Arch. 1975; 359: 1
   PubMedGoogle Scholar
• Reakin E. M. Filtration, diffusion and molecular sieving through porous cellulose membranes. J. Gen. Physiol. 1954; 38: 225
   PubMedGoogle Scholar
• Lambert P. P., Gassée J. P., Askenasi R. Physiological basis of protein excretion. Proteins in Normal and Pathological urine. S. Karger, Basel 1970; 67
   Google Scholar
• Verniory A., Du Bois R., de Coodt P., Cassée J. P., Lambert P. P. Measurement of the permeability of biological membranes. Application to the glomerular wall. J. Gen. Physiol. 1973; 62: 489
   PubMed Web of Science ®Google Scholar
• Brenner B. M., Baylis C., Deen W. M. Transport of molecules across renal glomerular capillaries. Physiol. Rev. 1976; 56: 502
   PubMedGoogle Scholar
• Rennke H. G., Venkatachalam M. A., Patel Y. Glomerular permeability of macromolecules. Effect of molecular configuration on the fractional clearance of uncharged dextran and neutral horseradish peroxidase in the rat. J. Clin. Invest. 1979; 63: 713
   PubMed Web of Science ®Google Scholar
• Ogston A. G., Preston B. N., Wells J. D. The transport of compact particles through solutions of chain polymers. Proc. R. Soc. London Biol. Sci. 1973; A333: 297
   Google Scholar
• Michael A. F., Blau E., Vernier R. L. Glomerular polyanion: alteration in aminonucleoside nephrosis. Lab. invest. 1970; 23: 649
   PubMed Web of Science ®Google Scholar
• Chang R. L. S., Deen W. M., Robertson C. R., Brenner B. M. Permselectivity of the glomerular capillary wall. III. Restricted transport of polyanions. Kidney Int. 1975; 8: 212
   PubMed Web of Science ®Google Scholar
• Rennke H. G., Cotran R. S., Vankatachalam M. A. Role of molecular charge in glomerular permeability: tracer studies with cationized ferritins. J. Cell Biol. 1975; 67: 638
   PubMed Web of Science ®Google Scholar
• Bohrer M. P., Baylis C., Hermes H. P., Glassock R. J., Robertson C. R., Brenner B. M. Permselectivity of the glomerular capillary wall: facilitated filtration of circulating polycations. J. Clin. Invest. 1978; 61: 72
   PubMedGoogle Scholar
• Rennke H. G., Patel Y., Venkatachalam M. A. Effect of molecular charge on the glomerular permeability to proteins in the rat. Clearance studies using neutral, anionic and cationic horseradish peroxidase. Kidney Int. 1978; 13: 278
   PubMedGoogle Scholar
• Purtell J. N., Pesce A. J., Clyne D. H., Miller W. C., Pollack V. E. Isoelectric point of albumin: effect on renal handling of albumin. Kidney Int. 1979; 16: 366
   PubMed Web of Science ®Google Scholar
• Graham R. C., Karnovsky M. J. Glomerular permeability: ultrastructure cytochemical studies using peroxidases as protein tracers. J. Exp. Med. 1966; 124: 1123
   PubMed Web of Science ®Google Scholar
• Caulfield J. P., Farquhar M. G. The permeability of glomerular capillaries to graded dextrans. Identification of the basement membrane as the primary filtration barrier. J. Cell Biol. 1974; 63: 883
   PubMed Web of Science ®Google Scholar
• Laliberte F., Sapin C., Belair M. F., Dniet P., Bariety J. The localization of the filtration barrier in normal rats glomeruli by ultrastructural immunoperoxidase techniques. Biol. Cell 1978; 31: 15
   Google Scholar
• Rosenzweigh L. J., Kanwar Y. S. Removal of sulfated (heparan sulfate) nonsulfated (hyaluronic acid) glycosaminoglycans results in increased permeability of the glomerular basement mem-brane to125I bovine serum albumin. Lab. Invest. 1982; 47: 177
   PubMedGoogle Scholar
• Kanwar Y. S., Linker A., Farquhar M. G. Increased permeability of the glomerular basement membrane to ferritin after removal of glycosaminoglycans (heparan sulfate) by enzyme digestion. J. Cell Biol. 1980; 86: 688
   PubMed Web of Science ®Google Scholar
• Hunsicker L. G., Shearer T. P., Shaffer S. J. Acute reversible proteinuria induced by infusion of the polycation hexadi-methrine. Kidney Int. 1981; 20: 7
   PubMedGoogle Scholar
• Vehaskari V. M., Root E. R., Germuth F. G., Robson A. M. Glomerular charge and urinary protein excretion: effects of systemic and intrarenal polycation infusion in the rat. Kidney Int. 1982; 22: 127
   PubMed Web of Science ®Google Scholar
• Barnes J. C., Radnick R. A., Gilchrist E. P., Venkatachalam M. A. Size and charge selective permeability defects induced in glomerular basement membrane by a polycation. Kidney Int. 1984; 25: 11
   PubMed Web of Science ®Google Scholar
• Kelley V. E., Cavallo T. Glomerular permeability: transfer of native ferritin in glomeruli with decreased anionic sites. Lab. Invest. 1978; 391: 547
   Google Scholar
• Bertolatus J. A., Hunsicker L. G. Polycation binding to glomerular basement membrane. Effect of biochemical modification. Lab. Invest. 1987; 56: 170
   PubMedGoogle Scholar
• Orikasa M., Matsui K., Oite T., Shimizu F. Massive proteinuria induced in rats by a single intravenous injection of a monoclonal antibodies. J. Immunol. 1988; 141: 807
   PubMedGoogle Scholar
• Park C. H., Maack T. Albumin absorption and catabolism by isolated perfused proximal convoluted tubules of the rabbit. J. Clin. Invest. 1984; 73: 767
   PubMed Web of Science ®Google Scholar
• Waller K. V., Ward K. M., Mahan J. P., Wismalt D. K. Current concepts of proteinuria. Clin. Chem. 1989; 35: 755
   PubMed Web of Science ®Google Scholar
• Cameron J. S., Blandford G. The simple assessment of selectivity in heavy proteinuria. Lancet 1966; ii: 242
   Google Scholar
• MacLean P. R., Robson J. S. A simple method for determining selectivity of proteinuria. Lancet 1967; ii: 539
   Google Scholar
• Brancaccio D., Rivolta E., Grazioni G., Pizzolato M. Albumin and alfa2-macroglobulin clearance: a new approaching method for studying selectivity of proteinuria in unconcentrated urine. Nephron 1974; 12: 150
   PubMedGoogle Scholar
• Myers B. D., Okarma T. B., Friedman S., Bridges C., Ross J., Asseff S., Deen W. Mechanisms of proteinuria in human glomerulonephritis. J. Clin. Invest. 1982; 70: 732
   PubMedGoogle Scholar
• Shemesh O., Ross J. C., Deen W. M., Grant G. W., Myers B. D. Nature of the glomerular capillary injury in human membranous nephropathy. J. Clin. Invest. 1986; 77: 868
   PubMedGoogle Scholar
• Bonsib S. M. Glomerular basement membrane discontinuities. Scanning electron microscopic study of acellular glomeruli. Am. J. Pathol. 1985; 119: 357
   PubMed Web of Science ®Google Scholar
• Ryan G. B. The glomerular sieve and the mechanisms of proteinuria. Aust. N.Z. J. Med. 1981; 11: 197
   PubMedGoogle Scholar
• Ryan G. B., Karnovsky M. J. An ultrastructural study of mechanism of proteinuria in aminonucleoside nephrosis. Kidney Int. 1975; 8: 219
   PubMedGoogle Scholar
• Olson J. L., Rennke H. G., Venkatachalam M. A. Alterations in the charge and size selectivity barrier of the glomerular filter in aminonucleoside nephrosis in rats. Lab. Invest. 1981; 44: 270
   Google Scholar
• Kühn K., Ryan G. B., Hein S. J., Galaske R. G., Karnovsky M. J. An ultrastructural study of the mechanisms of proteinuria in rat nephrotoxic nephritis. Lab. Invest. 1977; 36: 375
   PubMedGoogle Scholar
• Olson J. L., Hosteller T. H., Rennke H. G., Brenner B. M., Venkatachalam M. A. Altered glomerular permselectivity and progressive sclerosis following extreme ablation of renal mass. Kidney Int. 1982; 227: 112
   Google Scholar
• Weening J. J., Rennke H. G. Glomerular permeability and polyanion in adryamicin nephrosis in the rat. Kidney Int. 1983; 24: 152
   PubMed Web of Science ®Google Scholar
• Bennett C. M., Glassock R. J., Chang R. L. S., Deen W. M., Robertson C. R., Brenner B. M. Permselectivity of the glomerular capillary wall: studies of experimental glomerulonephritis in the rat using dextran sulfate. J. Clin. Invest. 1976; 57: 1287
   PubMedGoogle Scholar
• Kreisberg J. I., Karnovsky M. J. Rapid and focal loss of negative charge following administration of nephrotoxic serum in rats. Kidney Int. 1979; 16: 290
   PubMedGoogle Scholar
• Michael A. F., Blau E., Vernier R. L. Glomerular polyanion: alteration in aminonucleoside nephrosis. Lab. Invest. 1970; 23: 649
   PubMed Web of Science ®Google Scholar
• Blau E. B., Michael A. F. Rat glomerular glycoprotein composition and metabolism in aminonucleoside nephrosis. Proc. Soc. Exp. Biol. Med. 1972; 141: 164
   PubMedGoogle Scholar
• Caulfield J. P., Parquhar M. G. Loss of anionic sites from the glomerular basement membrane in aminonucleoside nephrosis. Lab. Invest. 1978; 39: 505
   PubMed Web of Science ®Google Scholar
• Caulfield J. P. Alterations in the distribution of alcian blue-staining fibrillar anionic sites in the glomerular basement membrane in aminonucleoside nephrosis. Lab. Invest. 1979; 40: 503
   PubMedGoogle Scholar
• Blau E. B., Haas O. E. Glomerular sialic acid and proteinuria in human renal disease. Lab. Invest. 1973; 28: 477
   PubMedGoogle Scholar
• Hirsh H. Z., Ains worth S. K., Spicer S. S., Kurtz E. H., Brissie R. M. Ultrastructural assessment by colloidal iron of the distribution and localization of anionic sites in human glomerulonephritides, Am. J. Pathol. 1982; 102: 99
   Google Scholar
• Okada K., Kawakami K., Miyao M., Oite T. Ultrastructural alterations of glomerular anionic sites in idiopathic membranous glomerulonephritis. Clin. Nephrol. 1986; 26: 7
   PubMed Web of Science ®Google Scholar
• Carrie B. J., Salver W. R., Myers B. D. Minimal change nephropathy: an electrochemical disorder of the glomerular membrane. Am. J. Med. 1981; 70: 262
   PubMed Web of Science ®Google Scholar
• De Bats A., Gordon A. H., Rhodes E. L. Variation in glomerular sialic acid content in diabetes and as the result of aging. Clin. Sci. Mol. Med. 1974; 47: 93
   PubMedGoogle Scholar
• Westberg N. G., Michael A. F. Human glomerular basement membrane chemical composition in diabetes mellitus. Acia Med. Scand. 1973; 194: 39
   Google Scholar
• Vernier R. L., Kkta D. J., Sisson S. P., Mahan J. D., Oegema T. R., Brown D. M. Heparan sulfate-rich anionic sites in the human glomerular basement membrane. Decreased concentration in congenital nephrotic syndrome. New Engl. J. Med. 1983; 309: 1001
   PubMed Web of Science ®Google Scholar
• Mynderse L. A., Hassell J. R., Kleinman H. K., Martin G. R., Marinez-Hernadez A. Loss of heparan sulfate proteoglycan from glomerular basement membrane of nephrotic rats. Lab. invest. 1983; 48: 292
   PubMed Web of Science ®Google Scholar
• Rohrbach D. H., Hassell J. R., Kleinman H. K., Martin G. R. Alterations in the basement membrane (heparan sulfate) proteoglycan in diabetic mice. Diabetes 1982; 31: 185
   PubMed Web of Science ®Google Scholar
• Wahl P., Deppermann D., Hasslacher C. Biochemistry of glomerular basement membrane of the normal and diabetic human. Kidney Int. 1982; 21: 744
   PubMedGoogle Scholar
• Schleicher E., Wieland E. Changes of human glomerular basement membrane in diabetes mellitus. J. Clin. Chem. Clin. Biochem. 1984; 22: 223
   PubMedGoogle Scholar
• Shimomura H., Spiro R. G. Studies on macromolecular components of human glomerular basement membrane and alteration in diabetes. Decreased levels of heparan sulfate pioteoglycan and laminin. Diabetes 1987; 36: 374
   PubMedGoogle Scholar
• Groggei G. C., Horvingh P., Border W. A., Linker A. Changes in glomerular heparan sulfate in puromycin aminonucleoside nephrosis. Am. J. Pathol. 1987; 128: 521
   PubMedGoogle Scholar
• Lelongt B., Makino H., Kanwar Y. S. Status of glomerular proteoglycans in aminonucleoside nephrosis. Kidney Int. 1987; 31: 1299
   PubMedGoogle Scholar
• Groggei G. C., Stevenson J., Horvingh P., Linker A., Border W. A. Changes in heparan sulfate correlate with increased glomerular permeability. Kidney Int. 1988; 33: 517
   PubMedGoogle Scholar
• Kerjaschki D., Vernillo A. T., Farquhar M. G. Reduced sialylation of podocalyxin, the major sialoprotein of rat kidney glomerulus in aminonucleoside nephrosis. Am. J. Pathol. 1985; 118: 343
   PubMedGoogle Scholar
• Quatacker J. Alterations in the sialic acid content of the rat glomerular filter in aminonucleoside nephrosis. Virchows Arch. 1986; 50: 237
   Google Scholar
• Bernard A., Ouled Amor A., Lauwerys R. Loss of glomerular polyanion correlated with albuminuria in chronic cadmium poisoning, submitted
   Google Scholar
• Olson J. L., Rennke H. G., Venkatachalam M. A. Alterations in the charge and size selectivity barrier of the glomerular filter in aminonucleoside nephrosis in rats. Lab. Invest. 1981; 44: 270
   Google Scholar
• Bertolatus J. A., Forster S. J., Hunsicker L. G. Stainable glomerular basement membrane polyanions and renal hemodynamics during hexadimethrine-induced proteinuria. J. Lab. Clin. Med. 1984; 103: 632
   PubMedGoogle Scholar
• Feldman J. E., Fisher E. R. Renal lesions of aminonucleoside nephrosis as revealed by electron microscopy. Lab. Invest. 1959; 8: 371
   PubMedGoogle Scholar
• Vernier R. L., Papermaster B. W., Good R. A. Aminonucieoside nephrosis. I. Electron microscopic study of the renal lesion in rats. J. Exp. Med. 1959; 109: 115
   PubMed Web of Science ®Google Scholar
• Sonnenburg-Hatzopoulos C., Assel E., Schurek H. J., Stolte H. Glomerular albumin leakage and morphology after neutralization of polyanions. H. Discrepancy of protamine induced albuminuria and fine structure of the glomerular filtration barrier. J. Submicrosc. Cytol. 1984; 16: 741
   PubMedGoogle Scholar
• Assel E., Neumann K. H., Schurek H. J., Sonnenburg C. H., Stolte H. Glomerular albumin leakage and morphology after neutralization of polyanions. I. Albumin clearance and sieving coefficient in the isolated perfused rat kidney. Renal Physiol. 1985; 1: 357
   Google Scholar
• Robinson R. R. Isolated proteinuria. Contrib. Nephrol. 1981; 24: 53
   PubMedGoogle Scholar
• Poortmans J. Proteinuria after muscular work. Proteins in Normat and Pathological Urine, Y. Manuel, J. P. Revillard, H. Betuel. S. Karger, Basel 1970; 229
   Google Scholar
• Vittinghus E., Mogensen C. E. Albumin excretion and renal haemodynamic response to physical exercise in normal and diabetic man. Scand. J. Clin. Lab. Invest. 1981; 41: 627
   PubMed Web of Science ®Google Scholar
• Mogensen C. E., Christensen C. K., Christensen N. J., Gundersen H. J. G., Jacobsen F. K., Pedersen E. B., Vittinghus E. Renal protein handling in normal, hypertensive and diabetic man. Contrib. Nephrol. 1981; 24: 139
   PubMedGoogle Scholar
• Carrie B. J., Huberman M., Schroeder J. S., Myers B. D. Albuminuria and the permselective properties of the glomerulus in cardiac failure. Kidney Int. 1980; 17: 507
   PubMedGoogle Scholar
• Feld L. G., Van Liew J. B., Galaske R. G., Boylan J. W. Selectivity of renal injury and proteinuria in the spontaneously hypertensive rat. Kidney Int. 1977; 12: 332
   PubMed Web of Science ®Google Scholar
• Addis T., Barrett E., Boyd R. I., Ureen H. J. Renin proteinuria in the rat. I. the relation between the proteinuria and the pressor effect of renin. J. Exp. Med. 1949; 89: 131
   PubMed Web of Science ®Google Scholar
• Deodhar S. D., Cappage F. E., Sableman E. Studies on the mechanism of experimental proteinuria induced by renin. J. Exp. Med. 1964; 120: 677
   PubMed Web of Science ®Google Scholar
• Bobrer M. P., Deen W. M., Robertson C. R., Brenner B. M. Mechanism of angiotensin H-induced proteinuria in the rat. Am. J. Physiol. 1977; 233: 1321
   Google Scholar
• Bauman J. W. Corticoid effects on angiotensinand norepinephrine-induced proteinuria in rats. Am. J. Physiol. 1979; 237: 133
   Google Scholar
• Schor N., Ichikawa I., Brenner B. M. Mechanisms of action of various hormones and vasoactive substances on glomerular ultraflltration in the rat. Kidney Int. 1981; 20: 442
   PubMed Web of Science ®Google Scholar
• Pessina A. C., Peart W. S. Renin-induced proteinuria and the effects of adrenalectomy. I. Hemodynamic changes in relation to function. Proc. R. Soc. London Biol. 1982; 180: 61
   Google Scholar
• Eisenbach G. M., Van Liew J. B., Boylan J. W., Manz N., Muir P. Effect of angiotensin on the filtration of protein in the rat kidney: a micropuncture study. Kidney Int. 1975; 8: 80
   PubMed Web of Science ®Google Scholar
• Olivetti G., Kithier K., Giacomelli F., Wiener J. Glomerular permeability to endogenous proteins in the rat. Lab. Invest. 1981; 44: 127
   PubMedGoogle Scholar
• Deen W. M., Maddox D. A., Robertson C. R., Brenner B. M. Dynamics of glomerular ultrafiltration in the rat. VII. Response to reduced renal mass. Am. J. Physiol. 1974; 227: 556
   PubMedGoogle Scholar
• Kaufman J. M., Siegel N. J., Hayslett J. P. Functional and hemodynamic adaptation to progressive renal ablation. Circ. Res. 1975; 36: 286
   PubMed Web of Science ®Google Scholar
• Hostetter T. H., Olson J. L., Rennke H. G., Venkatachalam M. A., Brenner B. M. Hyperfiltration in remnant nephrons: a potentially adverse response to renal ablation. Am. J. Physiol. 1981; 241: F85
   PubMed Web of Science ®Google Scholar
• Robson A. M., Mor J., Root E. R., Jager B. V., Shankel S. W., Ingelflnger J. R., Kienstra R. A., Bricker N. S. Mechanism of proteinuria in nonglomerular renal disease. Kidney Int. 1979; 16: 416
   PubMedGoogle Scholar
• Shea S. M., Raskova J., Morrison A. B. Ultrastructure of the glomerular basement membrane of rats with proteinuria due to subtotal nephrectomy. Am. J. Pathol. 1980; 100: 513
   PubMedGoogle Scholar
• Shimamura T., Morreson A. B. A progressive glomerulosclerosis occurring in partial five-sixths nephrectomized rats. Am. J. Pathol. 1975; 79: 95
   PubMed Web of Science ®Google Scholar
• Mogensen C. E., Vittinghus E. Urinary albumin excretion during exercise in juvenile diabetes. A provocation test for early abnormalities. Scand. J. Clin. Lab. Invest. 1975; 35: 295
   PubMed Web of Science ®Google Scholar
• Viberti G. C., Jarrett R. J., McCortney M., Keen H. Increased glomerular permeability to albumin induced by exercise in diabetic subjects. Diabetologia 1978; 14: 293
   PubMed Web of Science ®Google Scholar
• Pedersen E. B., Mogensen C. E., Lassen J. S. Effects of exercise on urinary excretion of albumin and beta2-microglobulin in young patients with mild essential hypertension without treatment and during long-term propranolol treatment. Scand. J. Clin. Lab. Invest. 1981; 41: 493
   PubMed Web of Science ®Google Scholar
• Ghiggeri G. M., Candiano G., Ginevri F., Gusmano R., Ciardi M. R., Perfume F., Delfino G., Cuniberti C., Gueirolo C. Renal selectivity properties towards endogenous albumin in minimal change nephropathy. Kidney Int. 1987; 32: 69
   PubMedGoogle Scholar
• Williams S. K., Siegal R. K. Preferential transport of nonenzymatically glycosylated ferritin across the kidney glomerulus. Kidney Int. 1985; 28: 146
   PubMedGoogle Scholar
• Ghiggeri G. M., Candiano G., Delfino G., Gueirolo C. Electrical charge of serum and urinary albumin in normal and diabetic humans. Kidney Int. 1985; 28: 168
   PubMedGoogle Scholar
• Layton G. J., Jerums G. Effect of glycation of albumin on its renal clearance in normal and diabetic rats. Kidney Int. 1988; 33: 673
   PubMed Web of Science ®Google Scholar
• Hayashi Y., Merikawa A., Makino M. Heterogeneity of urinary albumin from diabetic patients. Clin. Chim. Acta 1990; 190: 93
   PubMedGoogle Scholar
• Waldmann T. A., Strober W., Mogielnicki R. P. The renal handling of low molecular weight proteins. J. Clin. Invest. 1972; 51: 2162
   PubMed Web of Science ®Google Scholar
• Strober W., Waldmann T. A. The role of the kidney in the metabolism of plasma proteins. Nephron 1974; 13: 35
   PubMed Web of Science ®Google Scholar
• Maack T. Renal handling of low molecular weight proteins. Am. J. Med. 1975; 58: 57
   PubMed Web of Science ®Google Scholar
• Carone F. A. Renal handling of proteins and peptides. Ann. Clin. Lab. Med. 1978; 8: 287
   Google Scholar
• Kult J., Lammelein C., Röckel A., Heideland A. Beta2-microglobulin in serum—a parameter of glomerular filtrate. Dtsch. Med. Wochenschr. 1974; 99: 1686
   PubMedGoogle Scholar
• Graham R. C., Karnovsky M. J. Glomerular permeability: ultrastructure cytochemical studies using peroxidases as protein tracers. J. Exp. Med. 1966; 124: 1123
   PubMed Web of Science ®Google Scholar
• Strauss W. Colorimetric analysis with N, N-dimethyl-p-phenile-nediamine of the uptake of intravenously injected horseradish peroxidase by various tissues of the rat. J. Biophys. Biochem. Cytol. 1958; 4: 541
   PubMedGoogle Scholar
• Strauss W. Occurrence of phagosomes and phago-lysosomes in different segments of the nephron in relation to the reabsorption, transport, digestion and extrusion of intravenously injected horse-radish peroxidase. J. Cell. Biol. 1964; 21: 295
   PubMedGoogle Scholar
• Strauss W. Cytochemical observations on the relationship between lysosomes and phagosomes in kidney and liver by combined staining for acid phosphatase and intravenously injected horseradish peroxidase. J. Cell. Biol. 1964; 20: 497
   PubMedGoogle Scholar
• Bourdeau J. E., Carone F. A., Ganote C. E. Serum albumin uptake in isolated perfused renal tubules. J. Cell. Biol. 1972; 54: 382
   PubMed Web of Science ®Google Scholar
• Maunsbach A. B. Absorption of125l-homologous albumin by rat kidney proximal tubular cells. J. Ultrastruct. Res. 1966; 15: 197
   PubMedGoogle Scholar
• Lathem W., Davis B. B., Zweig P. H., Dew R. The demonstration and localization of renal tubular reabsorption by stop flow analysis. J. Clin. Invest. 1960; 39: 840
   PubMed Web of Science ®Google Scholar
• Ericsson J. L. E. Transport and digestion of hemoglobin in the proximal tubule, n. Electron microscopy. Lab. Invest. 1965; 14: 16
   PubMed Web of Science ®Google Scholar
• Miller F., Palade G. E. Lytic activities in renal protein absorption droplets. An electron microscopical cytochemical study. J. Cell Biol. 1964; 23: 519
   PubMedGoogle Scholar
• Neustein H. B. Hemoglobin absorption in the proximal tubules of the kidney in the rabbit. J. Ultrastruct. Res. 1967; 17: 565
   PubMedGoogle Scholar
• Maunsbach A. B., Neustein H. B. Autoradiographic demonstration of hemoglobin in lysosomes of rabbit proximal tubule cells during experimental hemoglobinemia. J. Ultrastruct. Res. 1968; 25: 183
   PubMedGoogle Scholar
• Karnovsky M. J., Rice D. F. Exogenous cytochrome C as an ultrastructural tracer. J. Histochem. Cytochem. 1969; 17: 751
   PubMed Web of Science ®Google Scholar
• Christensen E. L. Rapid protein uptake and digestion in proximal tubule lysosomes. Kidney Int. 1976; 10: 301
   PubMed Web of Science ®Google Scholar
• Maunsbach A. B. Absorption of ferritin by rat kidney proximal tubular cells. Electron microscopic observations of the initial uptake phase in cells of microperfused single proximal tubules. J. Ultrasiruct. Res. 1966; 16: 1
   PubMedGoogle Scholar
• Johnson V., Maack T. Renal extraction, filtration, absorption and catabolism of growth hormone. Am. J. Physiol. 1977; 233: F185
   PubMed Web of Science ®Google Scholar
• Stacy B. D., Wallace A. L. C., Gemmel R. T., Wilson B. W. Absorption of125I-labelled sheep growth hormone in single proximal tubules of the rat kidney. J. Endochnol. 1976; 68: 21
   PubMedGoogle Scholar
• Oliver D., Essner E. Protein transport in mouse kidney utilizing tyrosinase as an ultrastructural tracer. J. Exp. Med. 1972; 136: 291
   PubMedGoogle Scholar
• Maack T. Changes in the activity of acid hydrolases during renal reabsorption of lysozyme. J. Cell. Biol. 1967; 35: 268
   PubMedGoogle Scholar
• Maack T., Mackensie D. D. S., Kinter W. B. Intracellular pathways of renal reabsorption of lysozyme. Am. J. Physiol. 1971; 221: 1609
   PubMedGoogle Scholar
• Wochner R. D., Strober W., Waldmann T. A. The role of the kidney in the catabolism of Bence-Jones proteins and immunoglobulin fragments. J. Exp. Med. 1967; 126: 207
   PubMed Web of Science ®Google Scholar
• Gauthier C., Nguyen-Simonnet H., Vincent C., Revillard J. P., Pellet M. V. Renal tubular absorption of beta2-microglobulin. Kidney Int. 1984; 26: 170
   PubMed Web of Science ®Google Scholar
• Farboody G., Tattrie B., Rippstein P. U., Robin E. Z. The renal handling of human urinary ribonuclease by rat kidneys. Can. J. Physiol. Pharmacol. 1985; 63: 619
   PubMedGoogle Scholar
• Bourdeau J. E., Cohen E. R. Y., Carone F. A. Insulin uptake in the renal proximal tubule. Am. J. Physiol. 1973; 225: 1399
   PubMedGoogle Scholar
• Kau S. T., Maack T. Transport and catabolism of parathyroid hormone in isolated rat kidney. Am. J. Physiol. 1977; 233: F444
   Google Scholar
• Norquist R. E., Pahnieri G. M. A. Intracellular localization of parathyroid hormone in the kidney. Endocrinology 1974; 95: 229
   PubMedGoogle Scholar
• Wall D. A., Maack T. Endocytotic uptake, transport and catabolism of proteins by epithelial ceils. Am. J. Physiol. 1985; 248: 12
   Google Scholar
• Christensen E. I., Carone F. A., Rennke H. G. Effect of molecular charge on endocytic uptake of ferritin in renal proximal tubule cells. Lab. invest. 1981; 44: 351
   PubMed Web of Science ®Google Scholar
• Christensen E. I., Rennke H. G., Carone F. A. Renal uptake of protein: effect of molecular charge. Am. J. Physiol. 1983; 244: F436
   PubMed Web of Science ®Google Scholar
• Christensen E. I., Bjorke T. Renal uptake of protein: effect of pH. Renal Physiol. 1986; 9: 160
   PubMedGoogle Scholar
• Cojocel C., Franzen-Sieveking M., Beckman G., Bauman K. Inhibition of renal accumulation of lysozyme (basic low molecular weight protein) by basic proteins and other basic substances. Pflugers Arch. 1981; 390: 211
   PubMedGoogle Scholar
• Bernard A., Ouled Amor A., Lauwerys R. Charge-dependent renal uptake of beta₂-microglobulin in conscious rats, submitted
   Google Scholar
• Bernard A., Lauwerys R. Experimental evidence that the L-aspartate microproteinuria actually results from a tubular “Washout,”. Nephron, in press
   Google Scholar
• Ødum L., Hansen-Nord G., Nielsen C. A. Reversible microproteinuria induced by L-aspartate infusion. Nephron 1990; 56: 40
   PubMedGoogle Scholar
• Nomiyama K., Foulkes E. C. Reabsorption of filtered cadmium-metallothionein in the rabbit kidney. Proc. Soc. Exp. Biol. Med. 1977; 156: 97
   PubMed Web of Science ®Google Scholar
• Rabkin R., Petersen J., Mamelock R. Binding and degradation of insulin by isolated renal brush border membranes. Diabetes 1982; 31: 618
   PubMed Web of Science ®Google Scholar
• Beck L. V., Fedynsky J. N. Evidence from combined immunoassay and radioautography procedures that intact insulin123I molecules are concentrated by mouse kidney proximal tubule cells. Endocrinology 1967; 81: 475
   PubMed Web of Science ®Google Scholar
• De Kretser D. M., Martin T. J., Mellick R. A. The autoradiographic localization of 'I-labelled bovine parathyroid hormone. J. Endocrinol. 1970; 46: 507
   PubMedGoogle Scholar
• Bourdeau J. E., Carone F. A. Contraluminal serum albumin uptake in isolated perfused renal tubules. Am. J. Physiol. 1973; 224: 399
   PubMedGoogle Scholar
• Cho J., Galaske R. G., Arbesman H., Van Liew J. B. Renal albumin reabsorption in normal and sodium maleate-treated rats. Renal Physiol. 1985; 8: 8
   PubMedGoogle Scholar
• Galaske R. G., Baldamus C. A., Stolte H. Plasma protein handling in the rat kidney: micropuncture experiments in the acute heterologous phase of anti-GMB nephritis. Pflugers Arch. 1978; 375: 269
   PubMedGoogle Scholar
• Galaske R. G., Van Liew J. B., Feld L. G. Filtration and reabsorption of endogenous LMW protein in the rat kidney. Kidney Int. 1979; 16: 394
   PubMed Web of Science ®Google Scholar
• Cortney M., Sawin L., Weiss D. Renal tubular protein absorption in the rat. J. Clin. Invest. 1970; 49: 1
   PubMed Web of Science ®Google Scholar
• Madsen K. M., Harris R. H., Tester C. C. Influence of charge on ferritin uptake in the nephron (Abstr.). Kidney Int. 1981; 19: 248
   Google Scholar
• Madsen K. M., Harris R. H., Tisher C. C. Uptake and intracellular distribution of ferritin in the rat distal convoluted tubule. Kidney Int. 1982; 2: 354
   Google Scholar
• Sumpio B. E., Maack T. Kinetics, competition and selectivity of tubular absorption of proteins. Am. J. Physiol. 1982; 243: F379
   PubMedGoogle Scholar
• Clapp W. L., Park H. G., Madsen K. M., Tisher C. G. Axial heterogeneity in the handling of albumin by the rat kidney proximal tubule. Lab. Invest. 1988; 58: 549
   PubMed Web of Science ®Google Scholar
• Viau C., Bernard A., Gueret F., Maldague P., Gengoux P., Lauwerys R. Isoparaffinic solvent-induced nephrotoxicity in the rat. Toxicology 1986; 38: 227
   PubMedGoogle Scholar
• Stonard M. D., Phillips P. G. N., Foster J. R., Simpson M. G., Lock E. A. Alphaau-globulin: measurements in rat kidney following administration of 2,2,4-trimethylpentane. Toxicology 1986; 41: 161
   PubMedGoogle Scholar
• Maack T., Kinter W. B. Transport of protein by flounder kidney tubules during long term incubation. Am. J. Physiol. 1969; 216: 1034
   PubMedGoogle Scholar
• Christensen E. I., Maunsbach A. B. Intralysosomal digestion of lysozyme in renal proximal tubular cells. Kidney Int. 1974; 6: 396
   PubMedGoogle Scholar
• Ottosen P. D., Maunsbach A. B. Transport of peroxidase in flounder kidney tubules studied by electron microscope histochemistry. Kidney Int. 1973; 3: 315
   PubMed Web of Science ®Google Scholar
• Ottosen P. D., Bode F., Madsen K. M., Maunsbach A. B. Renal handling of lysozyme in the rat. Kidney Int. 1979; 15: 246
   PubMedGoogle Scholar
• Falconer-Smith J. F., Van Began R. I., Esnouff M. P., Ross B. D. Characteristics of renal handling of human immunoglobulin light chain by the perfused rat kidney. Clin. Sci. 1979; 57: 113
   Google Scholar
• Chamberlain M. J., Stimmler L. The renal handling of insulin. J. Clin. Invest. 1967; 46: 911
   PubMed Web of Science ®Google Scholar
• Rubinstein A. H., Spitz I. Role of the kidney in insulin metabolism and excretion. Diabetes 1968; 17: 161
   PubMedGoogle Scholar
• Rabbin R., Colwell J. A. The renal uptake and excretion of insulin in the dog. J. Lab. Clin. Med. 1969; 73: 893
   PubMedGoogle Scholar
• Ravnskov U., Johansson B. G., Gothlin J. Renal extraction of betarmicroglobulin. Scand. J. Clin. Lab. Invest. 1972; 30: 71
   PubMed Web of Science ®Google Scholar
• Katz A. I., Rubenstein A. H. Metabolism of proinsulin, insulin and C-peptide in the rat. J. Clin. Invest. 1973; 52: 1113
   PubMed Web of Science ®Google Scholar
• Hall P. W., Chung Park M., Vacca C. V., London M., Crowley A. Q. The renal handling of betaa-microglobulin in the dog. Kidney Int. 1982; 22: 156
   PubMed Web of Science ®Google Scholar
• Bernier G. M., Conrad M. E. Catabolism of human beta2-microglobulin by the rat kidney. Am. J. Physiol. 1969; 217: 1359
   PubMed Web of Science ®Google Scholar
• Frederiksson A. Renal handling of beta2-microglobulin in experimental renal disease. Scand. J. Clin. Lab. Invest. 1975; 35: 591
   PubMed Web of Science ®Google Scholar
• Martin K., Hruska K. A., Lewis J., Anderson C., Slatopolski E. The renal handling of parathyroid hormone in the dog: the role of peritubular uptake and glomerular filtration. J. Clin. Invest. 1977; 60: 808
   PubMed Web of Science ®Google Scholar
• Novakovic L., Hall P. W., Persky L. Renal protein metabolism in osbtructive uropathy. J. Urol. 1975; 113: 389
   PubMedGoogle Scholar
• Karlsson F. A., Groth T., Sege K., Wibell L., Peterson P. A. Turnover in humans of beta2-microglobulin: the constant chain of HLA antigens. Ear. J. Clin. Invest. 1980; 10: 293
   PubMed Web of Science ®Google Scholar
• Welling L. W., Grantham J. J. Physical properties of isolated perfused renal tubules and tubular basement membranes. J. Clin. Invest. 1972; 51: 1063
   PubMed Web of Science ®Google Scholar
• Katz A., Emmanouel D. Metabolism of polypeptide hormones by the normal kidney and in uremia. Nephron 1978; 22: 69
   PubMedGoogle Scholar
• Talor Z., Emmanouel D. S., Katz A. I. Glucagon (GLU) degradation by luminal and basolateral renal tubular membranes (Abstr.). Clin. Res. 1981; 29: 779A
   Google Scholar
• Carone F. A., Pullman T. N., Oparil S., Nakamura S. Micropuncture evidence of rapid hydrolysis of bradykinin by rat proximal tubule. Am. J. Physiol. 1976; 230: 1420
   PubMed Web of Science ®Google Scholar
• Carone F. A., Peterson D. R., Oparil S., Pullman T. N. Renal tubular transport and catabolism of proteins and peptides. Kidney Int. 1979; 16: 271
   PubMed Web of Science ®Google Scholar
• Camargo M. J. F., Sumpio B. E., Maack T. Renal hydrolysis of absorbed protein: influence of load and lysosomal pH. Am. J. Physiol. 1984; 247: F656
   PubMedGoogle Scholar
• Baumann K., Cojocel C., Franzen-Sieveking M. Inhibition of endocytotic lysozyme uptake by cationic proteins in perfused proximal tubules of rat kidney. Pflugers Arch. 1979; 379(Suppl.)R12
   Google Scholar
• Foulkes E. C. Apparent competition between myoglobin and metallothionein for renal reabsorption. Proc. Soc. Exp. Biol. Med. 1978; 159: 321
   PubMedGoogle Scholar
• Hardwicke J., Squire J. R. The relationship between plasma albumin concentration and protein excretion in patients with proteinuria. Clin. Sci. 1955; 14: 50
   Google Scholar
• Harrison J. F., Barnes A. D. The urinary excretion of lysozyme in dogs. Clin. Sci. 1970; 38: 533
   PubMed Web of Science ®Google Scholar
• Harrison J. R., Blainey J. D. Low molecular weight proteins in chronic renal disease. Clin. Sci. 1967; 33: 381
   PubMed Web of Science ®Google Scholar
• Alt J. M., Hacke M., Von der Heyde D., Jänig H., Junge P. M., Olbrech Ch., Schurek H. J., Stolte H. Urinary protein excretion in interstitial and tubular kidney diseases as characterized by gradient electrophoresis. Klin. Wochenschr. 1983; 61: 641
   PubMedGoogle Scholar
• Neuhaus O. W. Renal absorption of low molecular weight proteins in adult male rats: alpha2u-globulin. Proc. Soc. Exp. Bio. Med. 1986; 182: 531
   PubMed Web of Science ®Google Scholar
• Simonnet H., Gauthier C., Vincent C., Revillard J. R. The binding of beta2-microblogulin to renal brush-border membrane: affinity measurement, inhibition by serum albumin. Biophys. Biochim. Acta 1988; 940: 247
   PubMedGoogle Scholar
• Friberg L. Proteinuria and kidney injury among workmen exposed to cadmium and nickel dust. Preliminary report. J. Ind. Hyg. Toxicol. 1948; 30: 32
   PubMedGoogle Scholar
• Friberg L. Health hazards in the manufacture of alkaline accumulators with special reference to chronic cadmium poisoning. Acta Med. Scand. 1950; 138(Suppl. 240)1
   PubMed Web of Science ®Google Scholar
• Kekwick R. A. Physico-chemical examination of the serum and urine proteins in some cases of cadmium poisoning. Br. J. Ind. Med. 1955; 12: 196
   PubMedGoogle Scholar
• Butler E. A., Flynn F. V. The proteinuria of renal tubular disorders. Lancet 1958; ii: 978
   Google Scholar
• Butler E. A., Flynn F. V., Harris H., Robson E. B. A study of urine proteins by two dimensional electrophoresis with special reference to the proteinuria of renal tubular disorders. Clin. Chim. Acta 1962; 7: 34
   PubMed Web of Science ®Google Scholar
• Piscator M. Proteinuria in chronic cadmium poisoning. I. an electrophoretic and chemical study of urinary and serum proteins from workers with chronic cadmium poisoning. Arch. Environ. Health 1962; 4: 607
   PubMed Web of Science ®Google Scholar
• Piscator M. Proteinuria in chronic cadmium poisoning. IV. Gel filtration and ion exchange chromatography of urinary proteins from cadmium workers. Arch. Environ. Health 1966; 12: 345
   PubMed Web of Science ®Google Scholar
• Walravens Ph., Laterre E. C., Heremans J. F. Studies on tubular proteinuria. Clin. Chim. Acta 1968; 19: 107
   Google Scholar
• Flynn F. V., Platt H. S. The origin of the proteins excreted in tubular proteinuria. Clin. Chim. Acta 1968; 21: 377
   PubMed Web of Science ®Google Scholar
• Schultze H. E., Heremans J. F. Molecular Biology of Human Proteins with Special Reference to Plasma Proteins. Elsevier, Amsterdam 1966
   Google Scholar
• Oken D. E., Cotes S. C., Mende C. W. Micropuncture study of tubular transport of albumin in rats with aminonucleosis nephrosis. Kidney Int. 1972; 1: 3
   PubMedGoogle Scholar
• Wallenkamp G., Vree T. B., Guelen P. J., Jongman-Nix B. Interaction between the renal excretion rates of btai-microglobulin and gentamicin in man. Clin. Chim. Acta 1983; 127: 229
   PubMedGoogle Scholar
• Bernard A., Viau C., Ouled A., Tulkens P., Lauwerys R. Effects of gentamicin on the renal uptake of endogenous and exogenous proteins in conscious rats. Toxicol. Appl. Pharmacol. 1986; 84: 431
   PubMed Web of Science ®Google Scholar
• Buchet J. P., Roels H., Bernard A., Lauwerys R. Assessment of renal function of workers exposed to inorganic lead, cadmium or mercury vapour. J. Occup. Med. 1980; 22: 741
   PubMedGoogle Scholar
• Bernard A., Roels H., Buchet J. P., Lauwerys R. Comparison by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of urinary proteins excreted by workers exposed to cadmium, mercury or lead. Toxicol. Lett. 1980; 5: 219
   PubMedGoogle Scholar
• Hammond P. B., Lerner S. L, Gartside P. S., Hanenson I. B., Roda S. B., Foulkes E. C., Johnson D. R., Pesce A. J. The relationship of biological indices of lead exposure to the health status of workers in a secondary lead smelter. J. Occup. Med. 1980; 22: 475
   PubMedGoogle Scholar
• Verschoor M., Wibowo A., Herber R., Van Hemmen J., Zielhuis R. Influence of occupational low-level lead exposure on renal parameters. Am. J. Ind. Med. 1987; 12: 341
   PubMed Web of Science ®Google Scholar
• Huang J., He F., Wu Y., Zhang S. Observations on renal function in workers exposed to lead. Sci. Total Environ. 1988; 71: 535
   PubMedGoogle Scholar
• Rods H., Gennart Ph. J., Lauwerys R., Buchet J. P., Malchaire J., Bernard A. Surveillance of workers exposed to mercury vapour validation of a previously proposed biological threshold limit value of mercury concentration in urine. Am. J. Ind. Med. 1985; 1: 45
   Google Scholar
• Iesato K., Wakashin M., Wakashin Y., Tojo S. Renal tubular dysfunction in Minamata disease. Ann. Intern. Med. 1977; 86: 731
   PubMed Web of Science ®Google Scholar
• OW G., Yamamoto S., Fujino T., Itai Y., Ueno K., Saito H., Inoba Y., Nakajima K., Shiroishi K. Urinary bta2-microglobulin does not serve as diagnostic tool for Minamata disease. Arch. Environ. Health 1982; 37: 336
   PubMedGoogle Scholar
• Stewart W. K., Guirais H. A., Sanderson J., Taylor W. Urinary mercury excretion and proteinuria in pathology laboratory staff. Br J. Med. 1977; 34: 26
   Google Scholar
• Pesce A. J., Hanenson I., Seth K. Bta2-microglobulinuria in a patient with nephrotoxicity secondary to mercuric chloride ingestion. Clin. Toxicol. 1977; 11: 309
   PubMed Web of Science ®Google Scholar
• Mutti A., Cavatorta A., Pedroni C., Borghi A., Giaroli C., Franchini I. The role of chromium accumulation in the relationship between airborne and urinary chromium in welders. Int. Arch. Occup. Environ. Health 1979; 43: 123
   PubMed Web of Science ®Google Scholar
• Lindberg E., Vesterberg O. Urinary excretion of proteins in chromeplaters, ex-chromeplaters and referents. Scand. J. Work Environ. Health 1983; 9: 505
   PubMed Web of Science ®Google Scholar
• Saner G., Yuzbasiyan V., Cigdem S. Hair chromium concentration and excretion in tannery workers. Br. J. Ind. Med. 1984; 41: 263
   PubMedGoogle Scholar
• Uttorin M., Welinder H., Hultberg B. Kidney function in stainless steel workers. Int. Arch. Occup. Environ. Health 1984; 53: 279
   PubMedGoogle Scholar
• Verschoor M. A., Bragt P. C., Herber R. F. M., Zielhuis R. L., Zwennis W. C. M. Renal function of chrome plating workers and welders. Inc. Arch. Occup. Environ. Health 1988; 60: 67
   PubMed Web of Science ®Google Scholar
• Franchini I., Mutti A. Selected lexicological aspects of chromium compounds, Sci. Total Environ. 1988; 71: 379
   PubMed Web of Science ®Google Scholar
• Gompertz D., Fletcher J. G., Perkins J., Smith N. Y., Chettle D. R., Mason H., Scott M. C., Topping M. D. Renal dysfunction in cadmium smelters: relation toin vivo liver and kidney cadmium concentration. Lancet 1983; i: 1185
   Google Scholar
• Elinder C. G., Edling C., Lindberg E., Bertil K., Vesterberg O. Bta2-microglobulinuria among workers previously exposed to cadmium: follow-up and dose-response analyses. Am. J. Ind. Med. 1985; 8: 553
   PubMed Web of Science ®Google Scholar
• Saito H., Shiofi R., Harukawa Y., Nagui K., Arikawa T., Saito T., Sasaki Y., Furuyama T., Yoshinaga K. Cadmium-induced proximal tubular dysfunction in a cadmium polluted area. Contr. Nephrol. 1977; 6: 1
   PubMedGoogle Scholar
• Thun M. J., Osorio A. M., Schober S., Hannon W. A., Lewis B., Halperin W. H. Nephropathy in cadmium workers: assessment of risk from airborne occupational exposure to cadmium. Br. J. Ind. Med. 1989; 46: 689
   PubMedGoogle Scholar
• Smith T. J., Anderson R. J., Reading J. C. Chronic cadmium exposures associated with kidney function effects. Am. J. Ind. Med. 1980; 1: 339
   PubMedGoogle Scholar
• Roels H., Lauwerys R., Buchet J. P., Bernard A., Chettle D. R., Harvey T. C., Ai-Haddad I. K. in vivo measurement of liver and kidney cadmium in workers exposed to this metal. Environ. Res. 1981; 26: 217
   PubMed Web of Science ®Google Scholar
• Roels H., Lauwerys R., Buchet J. P., Bernard A. Environmental exposure to cadmium and renal function of aged women in three areas of Belgium. Environ. Res. 1981; 24: 117
   PubMed Web of Science ®Google Scholar
• Ellis K. J., Morgan W. C., Zanzi I., Yasumura S., Vartsky D., Conn S. H. Critical concentration of Cd in human renal cortex: dose-effect studies in Cd smelter workers. J. Toxicol. Environ. Health 1981; 7: 691
   PubMed Web of Science ®Google Scholar
• Hansen L., Kjellström T., Vesterberg O. Evaluation of different urinary proteins after occupational Cd exposure. Int. Arch. Occup. Environ. Health 1977; 40: 273
   PubMedGoogle Scholar
• Kjellström T., Evrin P. E., Rahnsler B. Dose-response relationship of cadmium-induced tubular proteinuria. A study of urinary béta2-microglobulin excretion among workers in a battery factory. Environ. Res. 1977; 13: 303
   PubMed Web of Science ®Google Scholar
• Kjellström T., Shiroishi K., Evrin P. Urinary bta2-microglobulin excretion among people exposed to cadmium in the general environment. An epidemiological study in cooperation between Japan and Sweden. Environ. Res. 1977; 13: 318
   PubMed Web of Science ®Google Scholar
• Shiroishi K., Kjellström T., Kubota K., Evrin P. E., Anayama M., Vesterberg O., Shimada T., Piscator M., Iwata T., Nishino H. Urinary analysis for detection of cadmium-induced renal changes, with special reference to bta2-microgloublin. Environ. Res. 1977; 13: 407
   PubMed Web of Science ®Google Scholar
• Bernard A., Buchet J. P., Roels H., Masson P., Lauwerys R. Renal excretion of proteins and enzymes in workers exposed to cadmium. Ear. J. Clin. Invest. 1979; 9: 11
   PubMed Web of Science ®Google Scholar
• Nogawa K., Ishizaki A., Kobayashi E. A comparison between health effects of cadmium and cadmium concentration in urine among inhabitants of the Itai-Itai disease endemic districts. Environ. Res. 1979; 18: 397
   PubMed Web of Science ®Google Scholar
• Lauwerys R., Bernard A., Roels H., Buchet J. P., Viau C. Characterization of cadmium proteinuria in man and in rat. Environ. Health Perspect 1984; 54: 147
   PubMedGoogle Scholar
• Ewers U., Brockhaus A., Dolgner R., Freir I., Jermann E., Bernard A., Stiller-Winkler R., Hohn R., Monoflovic N. Environmental exposure to cadmium and renal function of elderly women living in two cadmium-polluted areas of West-Germany. Int. Arch. Occup. Environ. Health 1985; 55: 217
   PubMed Web of Science ®Google Scholar
• Smith N. J., Topping M. D., Stewart J. D., Fletcher J. G. Occupational cadmium exposure in jig solderers. Br. J. Ind. Med. 1986; 43: 663
   PubMedGoogle Scholar
• Schiele R. Kidney damage from occupational cadmium exposure. Trace Elements Med. 1986; 3: 62
   Google Scholar
• Jakubowski M., Trojanowska B., Kowalska G., Gendek E., Starzynski Z., Krajewska B., Jajte J. Occupational exposure to cadmium and kidney dysfunction. Int. Arch. Occup. Environ. Health 1987; 59: 567
   PubMed Web of Science ®Google Scholar
• Itoh Y., Enomoto H., Kawai T. Alphai-microgloublin in cadmium poisoning. Nephron 1983; 35: 211
   PubMedGoogle Scholar
• Tohyama C., Kobayashi E., Saito H., Sugihara N., Nakano A., Mitane Y. Urinary alphai-microglobulin as an indicator protein of renal tubular dysfunction caused by environmental cadmium exposure. J. Appl. Toxicol. 1986; 6: 171
   PubMed Web of Science ®Google Scholar
• Alt J., Schiele R., Schaller K. H. Untersuchungen zur Kadmiumbelastung and zur Häufigkeit von Nierenerkrankungen Iterer Frauen in verschie denen Gebieten der Bundersrepublik Deutschland. Nieren Hochdrt Mr. 1985; 12: 546
   Google Scholar
• Bernard A., Moreau D., Lauwerys R. Comparison of retinol-binding protein and bta2-microglobulin determination in urine for the early detection of tubular proteinuria. Clin. Chim. Acta 1982; 126: 1
   PubMed Web of Science ®Google Scholar
• Donaldson M. D. C., Chambers R. E., Wαolridge M. W., Whicher J. T. Stability of alphai-microglobulin, bta2-microgloubulin and retinol-binding protein in urine. Clin. Chim. Acta 1989; 179: 73
   PubMed Web of Science ®Google Scholar
• Bernard A., Ouled A., Lauwerys R. Decrease of erythrocyte and glomerular membrane negative charges in chronic cadmium poisoning. Br. J. Ind. Med. 1988; 45: 112
   PubMedGoogle Scholar
• Roels H., Djubgang J., Buchet J. P., Bernard A., Lauwerys R. Evolution of cadmium-induced renal dysfunction in workers removed from exposure. Scand. J. Work Environ. Health 1982; 8: 191
   PubMed Web of Science ®Google Scholar
• Thun M. J., Baker D. B., Steenland K., Smith A. B., Halperin W., Berl I. B. Renal toxicity in uranium mill workers. Scand. J. Work Environ. Health 1985; 11: 83
   PubMed Web of Science ®Google Scholar
• Snndennan F. W., Jr., Horak E. Biochemical indices of nephrotoxicity exemplified by studies of nickel nephropathy. Organ-Directed Toxicity: Chemical Indices and Mechanisms, S. S. Brown, D. S. Davies. Pergamon Press, Oxford 1981; 55
   Google Scholar
• Lauwerys R., Bernard A., Viau C., Buchet J. P. Kidney disorders and hematoxicity from organic solvent exposure. Scand. J. Work Environ. Health 1985; 11(Suppl. 1)84
   Google Scholar
• Daniell W. E., Couser W. G., Rosenstock L. Occupational solvent exposure and glomerulonephritis. A case report and review of the literature. JAMA 1988; 259: 2280
   PubMed Web of Science ®Google Scholar
• Churchill D. N., Fine A., Gault M. H. Association between hydrocarbon exposure and glomerulonephritis: an appraisal of the evidence. Nephron 1983; 33: 169
   PubMed Web of Science ®Google Scholar
• Askergren A. Studies on kidney function in subjects exposed to organic solvents. III. Excretion of cells in the urine. Acta Med. Scand. 1981; 210: 103
   PubMedGoogle Scholar
• Askergren A., Augen L. G., Karlsson C., Lundberg I., Nyberg E. Studies on kidney function in subjects exposed to inorganic solvents. I. Excretion of albumin and bta2-microglobulin in the urine. Acta Med. Scand. 1981; 209: 379
   PubMedGoogle Scholar
• Mutti A., Lucertini S., Falzoi M., Cavartorta A., Franchini I. Organic solvents and chronic glomerulonephritis: a cross-sectional study with negative findings for aliphatic and alicyclic C5-C7 hydrocarbons. J. Appl. Toxicol. 1981; 1: 224
   PubMedGoogle Scholar
• Franchini I., Cavatorta A., Falzoi M., Lucertini S., Mutti A. Early indicators of renal damage in workers exposed to organic solvents. Int. Arch. Occup. Environ. Health 1983; 52: 1
   PubMed Web of Science ®Google Scholar
• Krusell L., Kraemmer-Nielsen H., Baelum J., Lundqvist G., Omland O., Vaeth M., Hasted S. E., Mogensen C. E., Geday E. Renal effects of chronic exposure to organic solvents. Acta Med. Scand. 1985; 218: 323
   PubMedGoogle Scholar
• Viau C., Bernard A., Lauwerys R., Quaeghebeur L., Cornu M. E., Philips S. C., Mutti A., Lucertini S., Franchini I. A cross-sectional survey of kidney function in refinery employees. Am. J. Ind. Med. 1987; 11: 177
   PubMedGoogle Scholar
• Viau C., Bernard A., De Russis R., Ouled A., Maldague P., Lauwerys R. Evaluation of the nephrotoxic potential of styrene in man and in rat. J. Appl. Toxicol. 1987; 1: 313
   Google Scholar
• Vyskocil A., Bernard A., Emminger S., Malir F., Fiala Z., Tusl M., Bttlerova E. Lack of nephrotoxicity of styrene at current TLV level (50 ppm). Int. Arch. Occup. Environ. Health 1989; 61: 409
   PubMed Web of Science ®Google Scholar
• Ng T. P., Ong S. G., Lam W. K., Jones M. G., Cheung C. K., Ong C. N. Urinary levels of proteins and metabolite in workers exposed to toluene. A cross-sectional study. Int. Arch. Occup. Environ. Health 1990; 62: 43
   PubMed Web of Science ®Google Scholar
• Normand J. C., Bernard A., Buchet J. P., Roels H., Michaux J. L., Dewandeleer B., Lauwerys R. Recherche d'anomalies rénales infracüniques chez les travailleurs de deux entreprises prod-uctrices de peintures. Arch. Mai. Prof. Hyg. Toxicol. Ind. 1990; 51: 261
   Google Scholar
• Schentag J. J., Sutfin T. A., Plant M. E., Jusfco W. J. Early detection of aminoglycoside nephrotoxicity with urinary bta2-microglobulin. J. Med. 1978; 9: 201
   PubMedGoogle Scholar
• Kaye W. A., Griffiths W. C., Camera P. D., Treblin W. M., Solomon R. J., Diamond L. The significance of bta2-microglobulinuria associated with gentamicin therapy. Ann. Clin. Lab. Set. 1981; 11: 530
   PubMedGoogle Scholar
• Schena F. P., De C'esaris R., Tedesco A., La Raia E., Bonomo L. Urinary excretion of bta2-microglobulin and albumin during antibiotic therapy in urinary tract infections. Contrib. Nephrol. 1981; 26: 42
   PubMedGoogle Scholar
• Fleming J. J., Coins C., Peckham M. J. Renal damage after cis-platinum. Lancet 1979; ii: 960
   Google Scholar
• Cohen A. L, Rose D. P., Citrin D. L. Abnormal bta2 microglobulin excretion following CDDP (cis-platinum) therapy. Proc. Am. Assoc. Cancer Res. 1980; 21: 137
   Google Scholar
• Jones B. R., Bhalla R. B., Mladek J., Kaleya R. N., Gralla R. J., Alltech N. N., Schwartz M. K., Young C. W., Keidenberg M. M. Comparison of methods of evaluating nephrotoxicity of cis-platinujn. Clin. Pharmacol. Ther. 1980; 24: 557
   Google Scholar
• Hacke M., Schmold H., Alt J., Baumann K., Stolte H. Nephrotoxicity of cis-diamminedichloroplatinum with or without ifosfamide in cancer treatment. Clin. Physiol. Biochem. 1983; 1: 17
   PubMedGoogle Scholar
• Ehninger G., Kaufmann T., Vossler G., Wernet P., Pfleiderer G., Risler T. Nephrotoxicity of cis-diaminedichloroplatinum measured by bta2-microglobulin, albumin, enzymes and magnesium in urine. Renal Heterogeneity and Target Cell Toxicity, P. H. Bach, E. A. Lock. John Wiley & Sons, Chichester 1985; 415
   Google Scholar
• Russ G. R., Horgan B. A., Mathew T. H., Brown H., Mills L., Kirkland J. A. Beta2-microglobulin excretion and urinary cytology in analgesic nephropathy. Clin. Nephrol. 1982; 18: 148
   PubMedGoogle Scholar
• Dawney A., Lucey M., Thornley C., Butham R., Cattell B., Williams R. The effects of cyclosporin A on the urine excretion of specific proteins in humans. Nephrotoxicity: In Vitro to In Vivo, Animals to Man, P. H. Bach, E. A. Lock. Plenum Press, New York 1989; 285
   Google Scholar
• Merle L. J., Reidenberg M. M., Camacho M. T., Jones B. R., Drayer D. E. Renal injury in patients with arthritis rheumatoid treated with gold. Clin. Pharmacol. 1980; 28: 216
   Google Scholar
• Latt D., Weiss J. B., Mayson M. I. V. Beta2-microglobulin levels in serum and urine of rheumatoid arthritis patients on gold therapy. Ann. Rheum. Dis. 1981; 40: 157
   PubMedGoogle Scholar
• Hansen H. E., Mogensen C. E., Sørensen J. L., Nørgaard K., Heiskov J., Amdisin A. Albumin and beta2-microglobulin excretion in patients on long term lithium treatment. Nephron 1981; 29: 229
   PubMedGoogle Scholar
• Donker A. J. M., Prins E., Meijer S., Slaiter W. J., Van Berkestijn J. W. B. M., Dols L. C. A renal function study in 30 patients on long-term lithium therapy. Clin. Nephrol. 1979; 12: 243
   PubMedGoogle Scholar
• Vree T. B., Zeens K., Huige P. J. C., Guelen P. J. M., Jongman-Nix B. Interaction between the renal excretion rates of betaj-microglobulin and tobramycin in man. Clin. Chim. Acta 1984; 138: 49
   PubMedGoogle Scholar
• Whiteside C., Prutis K., Cameron R., Thompson J. Glomerular epithelial detachment, not reduced charge density, correlates with proteinuria in adryamicin and puromycin nephrosis. Lab. Invest. 1989; 61: 650
   PubMedGoogle Scholar
• Bernard A., Ouled A., de Russis R., Lauwerys R. Potentiation of cadmium nephrotoxicity. Arch. Toxicol. 1988; 62: 291
   PubMedGoogle Scholar
• Axelsson B., Piscator M. Renal damage after prolonged exposure to cadmium. Arch. Environ. Health 1966; 12: 360
   PubMed Web of Science ®Google Scholar
• Nomiyama K., Nomiyama H., Yotoriyama M., Matsui K. Sodium dodecyl sulfate acrylamide gel electrophoresis studies on low-motecufar weight proteinuria, an early sign of cadmium health effects, in rabbits. Ind. Health 1982; 20: 11
   PubMedGoogle Scholar
• Bernard A., Goret A., Roels H., Buchet J. P., Lauwerys R. Experimental confirmation in rats of the mixed type proteinuria observed in workers exposed to cadmium. Toxicology 1978; 10: 369
   PubMed Web of Science ®Google Scholar
• Bernard A., Lauwerys R., Gengoux P. Characterization of the proteinuria induced by prolonged oral administration of cadmium in female rats. Toxicology 1981; 20: 345
   PubMed Web of Science ®Google Scholar
• Bernard A., Lauwerys R. The effects of sodium chromate and carbon tetrachloride on the urinary excretion and tissue distribution of cadmium in cadmium-pretreated rats. Toxicol. Appl. Pharmacol. 1981; 57: 30
   PubMed Web of Science ®Google Scholar
• Perassi R., Martin A. Urinary protein of the rat during carbon tetrachloride poisoning. Pathol. Biol. 1973; 21: 569
   PubMedGoogle Scholar
• Litterst C. L., Copley M. P. Cisplatin and doxorubicin: a comparative evaluation of nephrotoxicity using serum chemistry, urinalysis and histology. Renal Heterogeneity and Target Cell Toxicity, P. H. Bach, E. A. Lock. John Wiley & Sons, Chichester 1983; 393
   Google Scholar
• Diamond G. L., Morrow P. E., Fanner P. J., Gelein R. M., Baggs R. B. Nephrotoxicity of uranyl fluoride and reversibility of renal injury in the rat. Nephrotoxicity: In Vitro to In Vivo, Animals to Man, P. E. Bach, E. A. Lock. Plenum Press, New York 1989; 127
   Google Scholar
• Plaa G. L., Larson R. E. Relative nephrotoxic properties of chlorinated methane, ethane and ethylene derivatives in mice. Toxicol. Appl. Pharmacol. 1965; 7: 37
   PubMed Web of Science ®Google Scholar
• Alden C. L., Parker R. D., Eastman D. T. Development of an acute model for the study of chloromethanediphosphonate nephrotoxicity. Toxicol. Pathol. 1989; 17: 27
   PubMedGoogle Scholar
• Odum J., Grun T. The metabolism and nephrotoxicity of tetrafluoroethylene in the rat. Toxicol. Appl. Pharmacol. 1984; 76: 306
   PubMed Web of Science ®Google Scholar
• Dohn D. R., Leininger J. R., Lash L. H., Quebbemann A. J., Anders M. W. Nephrotoxicity of S-(2-chloro-1,1,2 trifluoroethyl) glutathione and S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine, the glutathione and cystein conjugates of chlorotrifluoroethene. J. Pharmacol. Exp. Ther. 1985; 235: 851
   PubMed Web of Science ®Google Scholar
• Bernard A., De Russis R., Normand J. C., Lauwerys R. R. Evaluation of the subacute nephrotoxicity of cyclohexane and other industrial solvents in the female Sprague-Dawley rats. Toxicol. Lett. 1989; 45: 271
   PubMedGoogle Scholar
• Viau C., Bernard A., Ouled A. A., Lauwerys R. Determination of rat beta2-microglobulin in urine and in serum. II. Application of its urinary measurement to selected nephrotoxicity models. J. Appl. Toxicol. 1986; 6: 191
   PubMed Web of Science ®Google Scholar
• Cojocel C., Dociu N., Ceacmacudis E., Baumann K. Nephrotoxic effects of aminoglycoside treatment on renal protein reabsorption and accumulation. Nephron 1984; 37: 113
   PubMedGoogle Scholar
• Ueda S., Wakashin M., Wakashin Y., Yoshida H., Lesato K., Mori T., Mori Y., Avikusa B., Okuda K. Experimental gold nephropathy in guinea pigs: detection of auto-antibodies to renal antigens. Kidney Int. 1986; 29: 539
   PubMed Web of Science ®Google Scholar
• Burnham W. M., Lycharz B., Avila J., Livingston K. E., Racine R. J. Effect of hexachlorobutadiene on renal function in the rat. Toxicol. Appl. Pharmacol. 1978; 45: 296
   Google Scholar
• Stonard M. D. Urinary enzymes and the pattern of proteinuria as indicators of renal injury. Renal Heterogeneity and Target Cell Toxicity, P. H. Bach, E. A. Lock. John Wiley & Sons, Chichester 1985; 291
   Google Scholar
• Vyskocü A., Panel J., Tusl M., Ettlerova E., Semecky V., Kasparova L., Lauwerys R., Bernard A. Dose-related proximal tubular dysfunction in male rats chronically exposed to lead. J. Appl. Toxicol. 1989; 9: 395
   PubMedGoogle Scholar
• Druet P., Druet E., Potdevin F., Saprin C. Immune type glomerulonephritis induced by HgCI2 in the Brown-Norway rat. Ann. Immunol. (Paris) 1978; 129c: 777
   Google Scholar
• Kluwe W. M. Development of resistance to nephrotoxic insult: changes in urine composition and kidney morphology on repeated exposures to mercuric chloride or biphenyl. J. Toxicol. Environ. Health 1982; 9: 619
   PubMed Web of Science ®Google Scholar
• Halman J., Fowler J. S. L., Price R. G. Urinary enzymes, proteinuria and renal function tests in the assessment of nephrotoxicity in the rat. Renal Heterogeneity and Target Cell Toxicity, P. H. Bach, E. A. Lock. John Wiley & Sons, Chichester 1985; 295
   Google Scholar
• Verschueren H. G., Kroes R., DenTonkelaar E. M., Berkvens J. M., Helleman P. W., Rauwes A. G., Schuller P. L., Van Esch G. J. Toxicity of methylmercury chloride in rats. I. Short-term study. Toxicology 1976; 6: 85
   PubMedGoogle Scholar
• Zimmerman S. W. Characterization of chronic N, N′-diacetylbenzidine induced nephropathy. Am. J. Pathol. 1979; 94: 285
   PubMedGoogle Scholar
• Halman J., Miller J., Fowler J. S. L., Price R. G. Renal toxicity of propyleneimine assessment by noninvasive techniques in the rat. Toxicology 1986; 41: 43
   PubMedGoogle Scholar
• Silber P. M., Gandolfl A. J., Brendel K. Early biological indicators of S-(1,2-dichlorovinyl)-2-cysteine nephrotoxicity in the rabbit. Drug Chem. Toxicol. 1986; 9: 285
   PubMed Web of Science ®Google Scholar
• Evan P. A., Dail W. G. The effects of sodium chromate on the proximal tubules of rat kidney. Lab. Invest. 1974; 30: 704
   PubMed Web of Science ®Google Scholar
• Christensen E. I., Maunsbach A. B. Proteinuria induced by sodium maleate in rats: effects on ultrastructure and protein handling in renal proximal tubule. Kidney Int. 1980; 17: 771
   PubMedGoogle Scholar
• Nomiyama K., Nomiyama A., Yotoriyama M. Low-molecular weight proteins in urine from rabbits given nephrotoxic compounds. Ind. Health 1982; 20: 1
   PubMedGoogle Scholar
• Fukuda S., Kopple J. D. Chronic uremia syndrome in dogs induced with uranyl nitrate. Nephron 1980; 25: 139
   PubMed Web of Science ®Google Scholar
• Vian C., Bernard A., Lauwerys R. Determination of rat beta2-microglobulin in urine and in serum. I. Development of an immunoassay based on latex particles agglutination. J. Appl. Toxicol. 1986; 6: 185
   PubMedGoogle Scholar
• Lehman-McKeeman L. D., Rivera-Torres M. I., Caudill D. Lysosomal degradation of alpha2u-globulin and alpha2u-globulin xenobiotics conjugates. Toxicol. Appl. Pharmacol. 1990; 103: 539
   PubMed Web of Science ®Google Scholar
• Olson M., Johnson T., Reidy C. A comparison of male rat and human urinary proteins: implications for human resistance to hyaline droplet nephropathy. Toxicol. Appl. Pharmacol. 1990; 102: 524
   PubMed Web of Science ®Google Scholar
• Swenberg J. A., Short B., Borghoff S., Strasser J., Charbonneau M. The comparative pathology of alpha2u-globulin nephropathy. Toxicol. Appl. Pharmacol. 1989; 97: 35
   PubMed Web of Science ®Google Scholar
• Alden C. L. Male rat specific alpha2u-globulin nephropathy and renal tumorigenesis. Nephrotoxicity In Vitro to In Vivo, Animals to Man, P. H. Bach, E. A. Lock. Plenum Press, New York 1989; 535
   Google Scholar
• Pedersen E. B., Selling J., Mogensen C. E., Christensen K. D. Urinary excretion of albumin and beta2-microglobulin, glomerular filtration rate and immune complexes in serum during infectious mononucleosis. Acta Pathol. Microbiol. Immunol. Scand. Sect. C. 1982; 90: 301
   PubMedGoogle Scholar
• Glassock R. J. Postural (orthostatic proteinuria): no cause for concern. New Engl. J. Med. 1981; 305: 639
   PubMedGoogle Scholar
• Reels H., Lauwerys R., Buchet J. P., Bernard A., Vos A., Oversteyns M. Health significance of cadmium induced renal dysfunction: a five year follow-up. Br. J. Ind. Med. 1989; 46: 755
   PubMedGoogle Scholar
• Bhunsohn A., Morris B. W., Griffltts H., Ramsey C. F. Stability of beta2-microglobulin and retinol binding protein at different values of pH and temperature in normal and pathological urine. Clin, Chim. Acta 1990; 195: 133
   Google Scholar