Clinical and Biological Aspects of Acid Phosphatase

References

• Hopkinson D. A., Spencer N., Harris H. Red cell acid phosphatase variants: a new human polymorphism. Nature 1963; 199: 969–971
   PubMedGoogle Scholar
• Sur B. K., Moss D. W., King E. J. Starch gel electrophoresis of prostatic acid phosphatase. Proc Assoc Clin Biochem 1962; 2: 11–13
   Google Scholar
• Lam K-W, Li C. Y., Yam L. T., et al. Comparison of prostatic and nonprostatic acid phosphatase. Ann NY Acad Sci 1982; 390: 1–15
   PubMed Web of Science ®Google Scholar
• Ostrowski W., Wasyl Z., Weber M., et al. The role of neuraminic acid in the heterogeneity of acid phosphomonoesterase from the human prostate gland. Biochim Biophys Acta 1970; 221: 297–306
   PubMedGoogle Scholar
• Wo Y-YP, McCormack A. L., Shabanowitz J., et al. Sequencing, cloning and expression of human red cell-type acid phosphatase, a cytoplasmic protein phosphatase. J Biol Chem 1992; 267: 10856–65
   PubMed Web of Science ®Google Scholar
• Swallow D. M., Povey S., Harris H. Activity of the red 'cell' acid phosphatase locus in other tissues. Ann Hum Genet. 1973; 37: 31–8
   PubMed Web of Science ®Google Scholar
• Blake N. M., Kirk R. L., Barnes K. R., et al. Expression of red cell acid phosphatase activity in placenta and other tissues. Jpn J Hum Genet 1973; 18: 10–23
   Google Scholar
• Pohlmann R., Krentler C., Schmidt B., et al. Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment. EM BO J. 1988; 7: 2343–50
   PubMedGoogle Scholar
• Lam K-W, Lee P., Eastlund T., et al. Antigenic and molecular relationship of human prostatic acid phosphatase isoenzymes. Invest Urol. 1980; 18: 209–11
   PubMedGoogle Scholar
• Heller J. E. Prostatic acid phosphatase: its current clinical status. J Urol 1987; 137: 1091–3
   PubMed Web of Science ®Google Scholar
• Kaczmarek M. J. On the isoenzymes of human red cell acid phosphatase. Biochem Med. 1976; 16: 173–6
   PubMedGoogle Scholar
• Kimura N., Sasano N. Prostate-specific acid phosphatase in carcinoid tumors. Virchows Arch (A) 1986; 410: 247–51
   Google Scholar
• Drenckhahn D., Waheed A., Van Etten R. Demonstration of prostatic-type acid phosphatase in non-lysosomal granules in the crypt epithelium of the human duodenum. Histochemistry 1987; 88: 47–52
   PubMedGoogle Scholar
• Epstein J. I., Kuhajda F. P., Lieberman P. H. Prostate-specific acid phosphatase immunoreactivity in adenocarcinomas of the urinary bladder. Hum Pathol 1986; 17: 939–42
   PubMed Web of Science ®Google Scholar
• Lord D. K., Cross NCP, Bevilacqua M. A., et al. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage. Eur J Biochem. 1990; 189: 287–93
   PubMedGoogle Scholar
• Behrendt H. Phosphatase activity of human erythrocytes. Proc Soc Exp Biol Med 1943; 54: 268–70
   Google Scholar
• Tsuboi K. K., Hudson P. B. Acid phosphatase. I. Human red cell phosphomonoesterase: general properties. Arch Biochem Biophys 1953; 43: 339–57
   PubMedGoogle Scholar
• Tsuboi K. K., Hudson P. B. Acid phosphatase. II. Purification of human red cell phosphomonoesterase. Arch Biochem Biophys. 1954; 53: 341–7
   PubMedGoogle Scholar
• Tsuboi K. K., Hudson P. B. Acid phosphatase. V. The nature of inactivation and stabilisation of purified human red cell phosphomonoesterase. Arch Biochem Biophys. 1955; 55: 206–18
   PubMedGoogle Scholar
• Tsuboi K. K., Hudson P. B. Acid phosphatase. VI. Kinetic properties of purified yeast and red cell phosphomonoesterase. Arch Biochem Biophys 1956; 61: 197–210
   PubMedGoogle Scholar
• Golden V. L., Sensabaugh G. F. Phenotypic variation in the phosphotransferase activity of human red cell acid phosphatase (ACP-1). Human Genet 1986; 72: 340–3
   PubMedGoogle Scholar
• Sokal R. R., Oden N. L., Wilson C. Genetic evidence for the spread of agriculture in Europe by demic diffusion. Nature 1991; 351: 143–5
   PubMed Web of Science ®Google Scholar
• Ferguson-Smith M. A., Newman B. F., Ellis P. M., et al. Assignment by deletion of human red cell acid phosphatase gene locus to the short arm of chromosome 2. Nature New Biol. 1973; 243: 271–4
   PubMedGoogle Scholar
• Dissing J., Svensmark O. Human red cell acid phosphatase: purification and properties of A, B and C isozymes. Biochim Biophys Acta. 1990; 1041: 232–42
   PubMedGoogle Scholar
• White INH, Butterworth P. J. Isoenzymes of human erythrocyte acid phosphatase. Biochim Biophys Acta. 1971; 229: 193–201
   PubMedGoogle Scholar
• Dissing J., Sensabaugh G. F. Human red cell acid phosphatase (ACP 1): differences in the primary structure of the two isoenzymes encoded by the ACP*B allele. Biochem Genet. 1987; 25: 919–27
   PubMedGoogle Scholar
• Dissing J., Johnsen A. H., Sensabaugh G. F. Human red cell acid phosphatase (ACP 1). J Biol Chem. 1991; 266: 20619–25
   PubMedGoogle Scholar
• Dissing J., Dahl O., Svensmark O. Phosphoric and arsonic acids as inhibitors of human red cell acid phosphatase and their use in affinity chromatography. Biochim Biophys Acta. 1979; 569: 159–76
   PubMedGoogle Scholar
• Zhang Z. Y., Van Etten R. L. Purification and characterisation of a low molecular weight acid phosphatase – a phosphotyrosyl protein from bovine heart. Arch Biochem Biophys 1990; 282: 39–49
   PubMed Web of Science ®Google Scholar
• Di Pietro D. L., Zengerle F. S. Separation and properties of three acid phosphatases from human placenta. J Biol Chem. 1967; 242: 3391–5
   PubMedGoogle Scholar
• Waheed A., Laidler P. M., Wo Y-YP, et al. Purification and physicochemical characterisation of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity. Biochemistry 1988; 27: 4265–73
   PubMedGoogle Scholar
• Heinrikson R. L. Purification and characterisation of a low molecular weight acid phosphatase from bovine liver. J Biol Chem. 1969; 244: 299–307
   PubMedGoogle Scholar
• Fujimoto S., Murakami K., Ishikawa A., et al. Two distinct low molecular weight acid phosphatases from rat liver. Chem Pharm Bull (Tokyo) 1988; 36: 3020–6
   PubMedGoogle Scholar
• Luffnian J. E., Harris H. A comparison of some properties of human red cell acid phosphatase in different phenotypes. Ann Hum Genet. 1967; 30: 387–401
   PubMedGoogle Scholar
• Taga E. M., Van Etten R. L. Human liver acid phosphatases: purification and properties of a low molecular weight isoenzyme. Arch Biochem Biophys. 1982; 214: 505–15
   PubMed Web of Science ®Google Scholar
• Chaimovich H., Nome F. Purification and properties of an acid phosphatase from bovine brain. Arch Biochem Biophys. 1970; 139: 9–16
   PubMed Web of Science ®Google Scholar
• Lai L., Revo S., Steinberg A. G. Acid phosphatases of human red cells: predicted phenotype conforms to a genetic hypothesis. Science 1964; 145: 1187–8
   PubMedGoogle Scholar
• Karp G. W., Sutton H. E. Some new phenotypes of human red cell acid phosphatase. Am J Hum Genet. 1967; 19: 54–62
   PubMed Web of Science ®Google Scholar
• Giblett E. R., Scott N. M. Red cell acid phosphatase: racial distribution and report of a new phenotype. Am J Hum Genet 1965; 17: 425–32
   PubMedGoogle Scholar
• Fuhrmann W., Lichte K. H. Human red cell acid phosphatase polymorphisms. Humangenetik 1966; 3: 121–6
   PubMedGoogle Scholar
• Hopkinson D. A., Spencer N., Harris H. Genetic studies on human red cell acid phosphatase. Am J Hum Genet 1964; 16: 141–54
   PubMed Web of Science ®Google Scholar
• Modiano G., Filippi G., Brunelli F., et al. Studies on red cell acid phosphatases in Sardinia and Rome. Absence of correlation with past malarial morbidity. Acta Genet 1967; 17: 17–28
   Google Scholar
• Lai LYC. Hereditary red cell acid phosphatase types in Australian white and New Guinea native populations. Acta Genet 1966; 16: 313–20
   PubMedGoogle Scholar
• Lai LYC, Kwa S. B. Red cell acid phosphatase types in some populations of south-east Asia. Acta Genet 1968; 18: 45–54
   PubMedGoogle Scholar
• Tashian R. E., Brewer G. J., Lehmann H., et al. Further studies on the Xavante Indians. V. Genetic variability in some serum and erythrocyte enzymes, hemoglobin, and the urinary excretion of β-amino-isobutyric acid. Am J Hum Genet. 1967; 19: 524–31
   PubMedGoogle Scholar
• Shinoda T. Red cell acid phosphatase types in a Japanese population. Jpn J Hum Genet. 1967; 11: 252–6
   Google Scholar
• Brewer G. J., Bowbeer D. F., Tashian R. E. The electrophoretic phenotypes of red cell phosphoglu-comutase, adenylate kinase, and acid phosphatase in the American Negro. Acta Genet Stat Med 1967; 17: 97–103
   PubMedGoogle Scholar
• Scott E. M., Duncan L. W., Ekstrand V., et al. Frequency of polymorphic types of red cell enzymes and serum factors in Alaskan Eskimos and Indians. Am J Hum Genet 1966; 18: 408–11
   PubMedGoogle Scholar
• Dissing J. Immunochemical characterisation of human red cell acid phosphatase isozymes. Biochem Genet. 1987; 25: 901–18
   PubMedGoogle Scholar
• Spencer N., Hopkinson D. A., Harris H. Quantitative difference and gene dosage in the human red cell acid phosphatase polymorphism. Nature 1964; 201: 299–300
   PubMed Web of Science ®Google Scholar
• Mansfield E., Sensabaugh G. F. The red cell, G. J. Brewer. Alan R. Liss, New York 1978; Vol 4: 233–44
   Google Scholar
• Sensabaugh G. F., Golden V. L. Phenotype dependence in the inhibition of red cell acid phosphatase (ACP) by folates. Am J Hum Genet 1978; 30: 553–60
   PubMedGoogle Scholar
• Wurzinger K. H., Novotny J. E., Mohrenweiser H. W. Studies of the purine analog associated modulation of human erythrocyte acid phosphatase activity. Mol Cell Biochem. 1985; 66: 127–36
   PubMedGoogle Scholar
• Boivin P., Galand C. The human red cell acid phosphatase is a phosphotyrosine protein phosphatase which dephosphorylates the membrane protein band 3. Biochem Biophys Res Commun. 1986; 134: 557–64
   PubMed Web of Science ®Google Scholar
• Harrison M. L., Rathinavelu P., Arese P., et al. Role of band 3 tyrosine phosphorylation in the regulation of erythrocyte glycolysis. J Biol Chem 1991; 266: 4106–11
   PubMed Web of Science ®Google Scholar
• Naidu J. M., Mohrenweiser H. W. Erythrocyte acid phosphatase – species specificity in activity modulation by purine analogs. Comp Biochem Physiol B. 1985; 81: 615–9
   PubMedGoogle Scholar
• Panara F., Angiolillo A., Secca T., et al. Acid phosphatases in the frog (Rana esculenta) skeletal muscle. Purification and some properties of the low molecular weight enzyme. lnt J Biochem 1991; 23: 1115–22
   Google Scholar
• Baxter J. H., Suelter C. H. Resolution of the low molecular weight acid phosphatase in avian pectoral muscle into two distinct enzyme forms. Arch Biochem Biophys. 1985; 239: 29–37
   PubMedGoogle Scholar
• Saeed A., Tremori E., Manao G., et al. Bovine brain low Mracid phosphatase: purification and properties. Physiol Chem Phys Med NMR. 1990; 22: 81–94
   PubMed Web of Science ®Google Scholar
• Manao G., Pazzagli L., Cirri P., et al. Rat liver low M(r) phosphotyrosine protein phosphatase isoenzymes: purification and amino acid sequences. Prot Chem 1992; 11: 333–45
   PubMedGoogle Scholar
• Dissing J., Johnsen A. H. Human red cell acid phosphatase (ACP 1): the primary structure of the two pairs of isozymes encoded by the ACPIA and ACP1C alleles. Biochim Biophys Acta. 1992; 1121: 261–8
   PubMedGoogle Scholar
• Divall G. B. Studies on the use of isoelectric focusing as a method of phenotyping erythrocyte acid phosphatase. Forensic Sci lnt. 1976; 18: 67–78
   Google Scholar
• Harris H., Hopkinson D. A., Loffman J. E., et al. Electrophoretic variation in erythrocyte enzymes. Hereditary disorders of erythrocyte metabolism, E. Beutler. Grune & Stratton, New York 1968; 1–20
   Google Scholar
• Ayer K.D. Lazaruk, Dissing J. M., Sensabaugh G. F. Exon structure at the human ACPI locus supports alternative splicing model for f and s isozyme generation. Biochim Biophys Res Commun. 1993; 296: 440–6
   Google Scholar
• Ruskin B., Greene J. M., Green M. R. Cryptic branch point activation allows accurate in vitro splicing of human beta-globulin intron mutants. Cell. 1985; 41: 833–44
   PubMedGoogle Scholar
• Gilman J. F. Haemoglobin (3-chain structural variation in mice – evolutionary and functional implications. Science 1972; 178: 873–4
   PubMedGoogle Scholar
• Doolittle R. F. The protein.3rd ed., H. Neurath, R. L. Hill. Academic Press, New York 1979; Vol 4: 1–18
   Google Scholar
• Nadley H. L., Egan T. J. Deficiency of lysosomal acid phosphatase. A new familial metabolic disorder. N Engl J Med. 1970; 282: 302–7
   PubMedGoogle Scholar
• Geier C., Figura K., Pohlmann K. Structure of the human lysosomal phosphatase gene. Eur J Biochem 1989; 183: 611–6
   PubMedGoogle Scholar
• De Duve C. Lysosomes revisited. Eur J Biochem. 1983; 137: 391–7
   PubMedGoogle Scholar
• Tsuboi K. K., Hudson P. B. Acid phosphatase. II. Purification of human red cell phosphomo-noesterase. Arch Biochem Biophys 1954; 53: 341–4
   PubMedGoogle Scholar
• Gieselmann V., Hasilik A., von Figura K. Tartrate-inhibitable acid phosphatase. Purification from placenta, characterisation and subcellular distribution in fibroblasts. Hoppe-Seylers' Z Physiol Chem. 1984; 365: 651–60
   PubMedGoogle Scholar
• Komfield S. Trafficking of lysosomal enzymes. FASEB J. 1987; 5: 462–8
   Google Scholar
• Kornfield D., Hellman I. The biogenesis of lysosomes. Annu Rev Cell Biol. 1989; 5: 483–525
   PubMedGoogle Scholar
• Nolan C. M., Sly W. S. I-cell disease and pseudoHurler polydystrophy: disorders of lysosomal enzyme phosphorylation and localisation. The metabolic basis of inherited disease, C. R. Scriver, A. L. Beaudet, W. S. Sly, D. Valle. McGraw-Hill, New York 1989; 1589–603
   Google Scholar
• Leroy J. G., Wan Ho M., Macbrinn M. C., et al. I-cell disease: biochemical studies. Pediatr Res. 1972; 6: 752–7
   PubMed Web of Science ®Google Scholar
• Reitman M. L., Kornfield S. UDP-A'-acetylglucosamine: glycoprotein ALacetylglucosamine-l-phosphotransferase. Proposed enzyme for the phosphorylation of the high mannose oligosaccharide units of lysosomal enzymes. J Biol Chem. 1981; 256: 4275–81
   PubMed Web of Science ®Google Scholar
• Waheed A., Hasibh A., von Figura K. Processing of the phosphorylated recognition marker in lysosomal enzymes. Characterisation and partial purification of a microsomala-N-acetyloglucosaminyl phosphotransferase. J Biol Chem. 1981; 256: 5717–21
   PubMed Web of Science ®Google Scholar
• Gottschalk S., Waheed A., Schmidt B., et al. Sequential processing of lysosomal acid phosphatase by a cytoplasmic thiol proteinase and a lysosomal aspartyl proteinase. EMBO J. 1989; 8: 3215–19
   PubMedGoogle Scholar
• Van Dongen J. M., Willemsen R., Ginns E. I., et al. The subcellular localisation of soluble and membrane-bound lysosomal enzymes in I-cell fibroblasts: a comparative immunocytochemi-cal study. Eur J Cell Biol 1985; 39: 179–89
   PubMedGoogle Scholar
• Willemsen R., Briiken R., Sorber CWJ, et al. A semiquantitative immunoelectro-microscopic study on soluble, membrane associated and membrane-bound lysosomal enzymes in human intestinal epithelial cells. Histochem J. 1991; 23: 467–73
   PubMedGoogle Scholar
• Fambrough D. M., Takayasu K., Lippincott-Schwartz J., et al. Structure of LEP 100, a glycoprotein that shuttles between lysosomes and the plasma membrane, deduced from the nucleotide sequence of the encoding c-DNA. J Cell Biol. 1988; 106: 61–7
   PubMedGoogle Scholar
• Viitala J., Carlsson S. R., Siebert P. D., et al. Molecular cloning of c-DNAs encoding lamp A, a human lysosomal membrane glycoprotein with apparent Mr= 120.000. Proc Natl Acad Sci USA 1988; 85: 3743–7
   PubMed Web of Science ®Google Scholar
• Howe C. L., Granger B. L., Hull M., et al. Derived protein sequence, oligosaccharides and membrane insertion of the 120 kDa lysosomal membrane glycosylation (lgp 120) identification of a highly conserved family of lysosomal membrane glycoproteins. Proc Natl Acad Sci USA 1988; 85: 7577–81
   PubMed Web of Science ®Google Scholar
• Peters C., Braun M., Weber B., et al. Targeting of a lysosomal membrane protein: a tyrosine-containing endocytosis signal in the cytoplasmic tail of lysosomal acid phosphatase is necessary and sufficient for targeting to lysosomes. EMBO J. 1990; 9: 3497–3506
   PubMedGoogle Scholar
• Braun M., Waheed A., von Figura K. Lysosomal acid phosphatase is transported to lysosomes via the cell surface. EMBO J. 1989; 8: 3633–40
   PubMedGoogle Scholar
• Waheed A., Gottschalk S., Hille A., et al. Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes in transfected baby hamster kidney cells. EMBO J. 1988; 7: 2351–8
   PubMed Web of Science ®Google Scholar
• Sharief F. S., Lee H., Leuderman M. M., et al. Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase. Biochem Biophys Res Commun. 1989; 160: 70–86
   Google Scholar
• Yam L. T., Li C-Y, Lam K. W. The non-prostatic acid phosphatases. Male accessory sex glands, E. Spring-Mills, ESE Hafez. Elsevier/North-Holland, Amsterdam 1980; 183–96
   Google Scholar
• Yeh L-CC, Lee A. J., Lee N. E., Kam K. W., et al. Molecular cloning of cDNA for human prostatic acid phosphatase. Genet. 1987; 60: 191–6
   Google Scholar
• Vihko P., Virkkunen P., Henttu P., et al. Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. FEBS Lett. 1988; 236: 275–81
   PubMed Web of Science ®Google Scholar
• Sharief F. S., Li SS-L. Structure of human prostatic acid phosphatase gene. Biochem Biophys Res Commun. 1992; 184: 1468–4
   PubMedGoogle Scholar
• Lin C-T, Liu J. W., Song G. X., et al. Immunoultrastructural demonstration of prostatic acid phosphatase isoenzyme 2 in prostatic carcinoma. J Urol. 1986; 136: 173–80
   PubMedGoogle Scholar
• Van Etten R. L., Davidson R., Stevis P. E., et al. Covalent structure, disulfide bonding and identification of reactive surface and active site residues of human prostatic acid phosphatase. J Biol Chem. 1991; 266: 2313–9
   PubMed Web of Science ®Google Scholar
• Tailor P. G., Govindan M. V., Patel P. C. Nucleotide sequence of human prostatic acid phosphatase determined from a full-length c-DNA clone. Nucleic Acids Res. 1990; 18: 4928
   PubMedGoogle Scholar
• Derechin M., Ostrowski W., Galka M., et al. Acid phosphomonoesterase of human prostate: molecular weight, dissociation and chemical composition. Biochim Biophys Acta. 1971; 250: 143–54
   PubMed Web of Science ®Google Scholar
• Luchter-Wasyl E., Ostrowski W. Subunit structure of human prostatic acid phosphatase. Biochim Biophys Acta 1974; 365: 349–59
   PubMedGoogle Scholar
• Ostrowski W., Bhargava A. K., Dziembor E., et al. Acid phosphomonoesterase of human prostate: carbohydrate content and optical properties. Biochim Biophys Acta. 1976; 453: 262–9
   PubMedGoogle Scholar
• Risley J. M., Van Etten R. L. Structures of the carbohydrate moieties of human prostatic acid phosphatase elucidated by H, nuclear magnetic resonance spectroscopy. Arch Biochem Biophys. 1987; 258: 404–12
   PubMedGoogle Scholar
• Peters C., Geier C., Pohlmann R., et al. High degree of homology between primary structure of human lysosomal acid phosphatase and human prostatic acid phosphatase. Biol Chem Hoppe Seyler. 1989; 370: 177–81
   PubMedGoogle Scholar
• Roiko P., Jänne O. A., Vihko P. Primary structure of rat secretory acid phosphatase and comparison to other acid phosphatases. Gene. 1990; 89: 223–9
   PubMedGoogle Scholar
• Vihko P., Kurkela R., Porvari K., et al. Rat acid phosphatase: overexpression of active, secreted enzyme by recombinant baculovirus infected insect cells, molecular properties and crystallization. Proc Natl Acad Sci USA 1993; 90: 799–803
   PubMedGoogle Scholar
• Morris M. F., Waheed A., Risley J. M., et al. Carbohydrate removal fails to eliminate the heterogeneity of human prostatic acid phosphatase. Clin Chim Acta. 1989; 182: 9–20
   PubMedGoogle Scholar
• Lam K-W, Li CY, Yam L. T., et al. Comparison of prostatic and nonprostatic acid phosphatase. Ann NY Acad Sci. 1982; 390: 1–15
   PubMed Web of Science ®Google Scholar
• Lam WKW, Lai L. C., Yam L. T. Tartrate-resistant (band 5) acid phosphatase activity measured by electrophoresis on acrylamide gel. Clin Chem. 1978; 24: 309–12
   PubMedGoogle Scholar
• Hibbard M. D., McCarthy R. C., Markowitz H. Isolation and characterisation of electrophoretic variants of human prostatic acid phosphatase. Clin Chem. 1983; 29: 1886–9
   PubMedGoogle Scholar
• Bais R., Huxtable A., Edwards J. B. Human prostatic acid phosphatase: properties of the native enzyme, and the enzyme antibody complex. Ann Clin Biochem. 1983; 20: 374–80
   PubMedGoogle Scholar
• Taga E. M., Moore D. L., Van Etten R. L. Studies on the structural basis of the heterogeneity of human prostatic and seminal acid phosphatases. Prostate. 1983; 4: 141–50
   PubMed Web of Science ®Google Scholar
• McTigue J. J., Van Etten R. L. Isolation, characterisation and spontaneous interconversion of two forms of human prostatic acid phosphatase. Prostate. 1982; 3: 165–81
   PubMedGoogle Scholar
• Smith J. K., Whitby L. G. The heterogeneity of prostatic acid phosphatase. Biochim Biophys Acta 1968; 151: 607–18
   PubMedGoogle Scholar
• Lam W. K., Yam L. T., Wilbur H. J., et al. Comparison of acid phosphatase isoenzymes of human seminal fluid, prostate, and leukocytes. Clin Chem. 1979; 25: 1285–9
   PubMedGoogle Scholar
• Ostrowski W., Wasyl Z., Weber M., et al. The role of neuramic acid in the heterogeneity of acid phosphomonoesterase from the human prostate gland. Biochim Biophys Acta. 1970; 221: 297–306
   PubMedGoogle Scholar
• Lin M. F., Lee C-L, Li SS-L, et al. Purification and characterisation of a new human prostatic acid phosphatase isoenzyme. Biochemistry 1983; 22: 1055–62
   PubMedGoogle Scholar
• Lad P. M., Leam D. B., Cooper J. F., et al. Distribution of prostatic acid phosphatase isoenzymes in normal and cancerous states. Clin Chim Acta. 1984; 151: 51–65
   Google Scholar
• Pais V. M., Mangold A. W., Mahoney S. A. Fractionation and purification of prostatic acid phosphatase. Invest Urol 1974; 12: 13–6
   PubMedGoogle Scholar
• McTigue J. J., Van Etten R. L. An essential arginine residue in human prostatic acid phosphatase. Biochim Biophys Acta. 1978; 523: 422–9
   PubMedGoogle Scholar
• Saini M. S., Van Etten R. L. An essential carboxylic acid group in human prostatic acid phosphatase. Biochim Biophys Acta. 1979; 568: 370–6
   PubMedGoogle Scholar
• Ostrowski W. Isolation of tau-phosphohistidine from a phosphoryl-enzyme intermediate of human prostatic acid. Biochim Biophys Acta. 1978; 523: 147–53
   PubMedGoogle Scholar
• Davidson R. E. Structural aspects of human prostatic acid phosphatase and fast atom bombardment mass spectrometric analysis ofE. coliL-threonine deaminase. Ph.D. thesis, Purdue University, West Lafayette, IN, 1990. 1990
   Google Scholar
• Ostanin K., Saeed A., Van Etten R. L. Heterologous expression of human prostatic acid phosphatase and site-directed mutagenesis of the enzyme active site. J Biol Chem 1974; 269: 8971–8
   Google Scholar
• Ostanin K., Harms E. H., Stevis P. E., et al. Overexpression, site directed mutagenesis and mechanism-ofEscherichia coliacid phosphatase. J Biol Chem. 1992; 267: 22830–6
   PubMed Web of Science ®Google Scholar
• Ostanin K., Van Etten R. L. Asp 304 ofEscherichia coliacid phosphatase is involved in leaving group protonation. J Biol Chem. 1993; 268: 20778–84
   PubMed Web of Science ®Google Scholar
• Schneider G., Lindqvist Y., Vihko P. Three-dimensional structure of rat acid phosphatase. EMBO J 1993; 12: 2609–15
   PubMedGoogle Scholar
• Lindqvist Y., Schneider G., Vihko P. Three-dimensional structure of rat acid phosphatase in complex with L(+) tartrate. J Biol Chem. 1993; 268: 20744–6
   PubMedGoogle Scholar
• Lindqvist Y., Schneider G., Vihko P. Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism. EurJBiochem. 1994; 221: 139–42
   Google Scholar
• Hillmann G. Fortlaufende photometrische Messund der sauren Prostataphosphatase-activitat. Z. Klin Chem Klin Biochem. 1971; 9: 273–4
   PubMedGoogle Scholar
• Warren R. J., Moss D. W. An automated continuous monitoring procedure for the determination of acid phosphatase activity in serum. Clin Chim Acta. 1977; 77: 179–88
   PubMedGoogle Scholar
• Fabing-Byrd D. L., Ertingshausen G. Kinetic method for determining acid phosphatase activity in serum with use of the “CentrifiChem”. Clin Chem. 1972; 18: 841–4
   PubMedGoogle Scholar
• Valcour A. A., Bowers G. N., McComb R. B. Evaluation of a kinetic method for prostatic acid phosphatase with use of self-indicating substrate, 2,6-dichloro-4-nitrophenyl phosphate. Clin Chem. 1989; 35: 939–45
   PubMedGoogle Scholar
• Appleyard J. The effect of alcohol on the hydrolysis of sodium phenolphthalein diphosphate by prostatic extracts. Biochem J 1948; 42: 596–7
   Google Scholar
• Gallati H., Roth M. Aktivierung der sauren Prostataphosphatase durch 1-pentanol. J Clin Chem Clin Biochem 1976; 14: 581–7
   PubMedGoogle Scholar
• Poindexter C., Ervin K., Rice E. G. A kinetic acid phosphatase (Hillmann) procedure of improved sensitivity. Clin Chem. 1980; 26: 1009
   Google Scholar
• Vihko P. Characterisation of the principal human prostatic acid phosphatase isoenzyme, purified by affinity chromatography and isoelectric focussing. II. Clin Chem 1978; 24: 1783–7
   PubMedGoogle Scholar
• McCarthy R. C., Jakubowski H. V., Markowitz H. Human prostatic acid phosphatase: purification, characterisation, and optimisation of conditions for radioimmunoassay. Clin Chem Acta. 1983; 132: 287–99
   PubMedGoogle Scholar
• Roy A. V., Brower M. E., Hayden J. E. Sodium thymolphthalein monophosphate: a new acid phosphatase substrate with greater specificity for the prostatic enzyme in serum. Clin Chem 1971; 17: 1093–1102
   PubMed Web of Science ®Google Scholar
• Bais R., Edwards J. B. An optimized continuous-monitoring procedure for semi-automated determination of serum acid phosphatase activity. Clin Chem 1976; 22: 2025–8
   PubMed Web of Science ®Google Scholar
• Crans D. N., Simone C. M., Saha A. K., et al. Vanadate monomers and dimers both inhibit the human prostatic acid phosphatase. Biochem Biophys Res Commun. 1989; 165: 246–50
   PubMedGoogle Scholar
• Taga E. M., Moore D. L., Van Etten R. L. Studies on the structural basis of the heterogeneity of human prostatic and seminal acid phosphatases. Prostate. 1983; 4: 141–50
   PubMed Web of Science ®Google Scholar
• Yam LT. Clinical significance of the human acid phosphatases. Am J Med. 1981; 56: 604–16
   Google Scholar
• Van Etten R. L. Human prostatic acid phosphatase: a histidine phosphatase. Ann NY Acad Sci. 1982; 390: 27–51
   PubMed Web of Science ®Google Scholar
• Francis J. M., Moss D. W., Colinet E., et al. A reference preparation of human prostatic acid phosphatase: purification, characterization and field trials. Ann Clin Biochem 1992; 29: 176
   PubMedGoogle Scholar
• Lantz R. K., Eisenberg R. E. Preservation of acid phosphatase activity in medico-legal specimens. Clin Chem 1978; 24: 486–8
   PubMedGoogle Scholar
• Vihko P., Kontturi M., Korhonen L. K. Purification of human prostatic acid phosphatase by affinity chromatography and isoelectric focusing. I. Clin Chem 1978; 24: 466–70
   PubMed Web of Science ®Google Scholar
• Van Etten R. L., Saini M. S. Selective purification of tartrate-inhibitable acid phosphatases: rapid and efficient purification (to homogeneity) of human and canine prostatic acid phosphatases. Clin Chem 1978; 24: 1525–30
   PubMed Web of Science ®Google Scholar
• Duncan P. H., Van Etten R. L., MacNeil M. L., et al. Development of a stable reference material for prostatic acid phosphatase. Clin Chem. 1984; 30: 1327–31
   PubMedGoogle Scholar
• Francis J. M. A reference preparation of human prostatic acid phosphatase. Ph.D. thesis, University of London. 1992
   Google Scholar
• Dang H., Lam K. W., Li C-Y, et al. Monoclonal antibody specific to acid phosphatase isoenzyme. Prostate 1986; 9: 47–55
   PubMedGoogle Scholar
• Patel P. C., Aubin L., Cote J. Use of monoclonal and polyclonal antibodies to detect prostatic acid phosphatase by immunoblotting. Clin Chem 1986; 32: 1832–5
   PubMedGoogle Scholar
• Hoyhtya M., Vihko P., Vaolas L., et al. High affinity monoclonal antibodies specific for human prostatic acid phosphatase. Clin Chem. 1987; 33: 103–7
   PubMedGoogle Scholar
• Lee C-L, Li SSL, Chu T. M. Immunologically reactive tryptic fragments of human prostatic acid phosphatase. Biochem J. 1984; 223: 871–7
   PubMedGoogle Scholar
• Lillehoj H., Choe B-K, Rose N. R. Monoclonal antibodies to human prostatic acid phosphatase: probes for antigenic study. Proc Natl Acad Sci USA 1982; 79: 5061–5065
   PubMedGoogle Scholar
• Ostrowski W., Weber M., Rybarska J. Immunochemical properties of acid phosphomonoesterase from human prostate gland. Acta Biochim. Pol. 1966; 13: 343–52
   PubMedGoogle Scholar
• Foti A. G., Glovsky M. M., Cooper J. F. The effect of antibody on human prostatic acid phosphatase activity. I. Temperature and pH stabilisation of acid phosphatase enzyme activity by rabbit antibody to acid phosphatase. Immunochemistry 1975; 12: 131–6
   Google Scholar
• Choe B. K., Dong M. K., Walz D., et al. A single domain of human prostatic acid phosphatase shows antibody-mediated restoration of catalytic activity. Proc Natl Acad Sci USA 1982; 79: 6052–5
   PubMedGoogle Scholar
• London M., McHugh R., Hudson P. B. On low acid phosphatase values of patients with known metastatic carcinoma of prostate. Cancer Res 1953; 14: 718–24
   Google Scholar
• Wasylewska E., Dulinska J. T., Frubetskoy V. S., et al. Stabilisation of human prostate acid phosphatase by cross-linking with diimidoesters. Acta Biochim Pol 1987; 34: 145–56
   PubMedGoogle Scholar
• Gutman E. B., Sproul E. E., Gutman A. B. Significance of increased phosphatase activity of bone at the site of osteoplastic metastases secondary to carcinoma of the prostate gland. Am J Cancer 1936; 28: 485–95
   Google Scholar
• Chu T. M., Wang M. C., Lee C-L, et al. Prostatic acid phosphatase in human prostate cancer. Biochemical markers for cancer, TM Chu. Marcel Dekker, New York 1982; 117–36
   Google Scholar
• Kutscher W., Wolbergs H. Prostataphosphatase. Hoppe Seyler's Z Physiol Chem. 1935; 236: 237–40
   Google Scholar
• Gutman A. B., Gutman E. B. An acid phosphatase occurring in the serum of patients with metastasizing carcinoma of the prostate gland. J Clin Invest 1938; 17: 473–8
   PubMedGoogle Scholar
• Huggins C., Hodges C. V. Studies on prostatic cancer. I. The effect of castration, of oestrogen and of androgen injection on serum phosphatases in metastatic carcinoma of the prostate. Cancer Res. 1941; 1: 293–7
   Google Scholar
• Optenberg S A, Thompson I. M. Economics of screening of carcinoma of the prostate. Urol Clin North Am. 1990; 17: 719–37
   PubMed Web of Science ®Google Scholar
• Chodak G. W. Early detection and screening for prostatic cancer. Urology 1989; 34: 10–56
   PubMedGoogle Scholar
• Gittes R. F. Prostate-specific antigen. N Engl J Med. 1987; 317: 954–5
   PubMed Web of Science ®Google Scholar
• Moncure C. W., Johnston C. L., Koontz W. W., et al. Investigation of specific antigens in prostatic cancer. Cancer Chemother Rep 1975; 59: 105–10
   PubMedGoogle Scholar
• Nadji M., Tabei S. Z., Castro A, et al. Prostatic-specific antigen: an immunohistologic marker for prostatic neoplasms. Cancer. 1981; 48: 1229–32
   PubMed Web of Science ®Google Scholar
• Raynor R. H., Hazra T. A., Moncure C. W., et al. Biochemical nature of the prostate-associated antigen identified by the monoclonal antibody, KR-P8. Prostate. 1986; 9: 21–31
   PubMed Web of Science ®Google Scholar
• Guinan P., Bhatti R., Ray P. An evaluation of prostate specific antigen in prostatic cancer. J Urol. 1987; 137: 686–9
   PubMed Web of Science ®Google Scholar
• Brawer M. K., Koyanagi Y., Inoue T., et al. Some physicochemical characteristics of gamma-seminoprotein: antigenic component specific for human seminal plasma. Jpn J Legal Med 1971; 25: 322–4
   PubMedGoogle Scholar
• Edson J. Pontes. Biological markers in prostate cancer. J Urol. 1983; 130: 1037–47
   PubMedGoogle Scholar
• Merrick M. V., Ding C. L., Chisholm G. D., et al. Prognostic significance of alkaline and acid phosphatase and skeletal scintigraphy in carcinoma of the prostate. Br J Urol. 1985; 57: 715–20
   PubMedGoogle Scholar
• DeVoogt H. J. Prognostic factors. Baillieres clinical oncology: prostatic cancer, BJA Furr, L. Denis. W. B. Saunders, Philadelphia 1988; Vol. 2: 521–26
   Google Scholar
• Killian C. S., Emrich L. J., Vargas F. P., et al. Relative reliability of five serially measured markers for prognosis of progression of prostate cancer. J Natl Cancer Inst 1986; 76: 179–85
   PubMedGoogle Scholar
• Ercole C. J., Lange P. H., Mathisen M., et al. Prostatic specific antigen and prostatic acid phosphatase in the monitoring and staging of patients with prostatic cancer. J Urol. 1987; 138: 1181–4
   PubMed Web of Science ®Google Scholar
• Salo J., Rannikko S. The value of acid phosphatase measurements in predicting extraprostatic cancer growth before prostatectomy. Br J Urol 1988; 62: 439–42
   PubMedGoogle Scholar
• Armbruster D. A. Prostate-specific antigen: biochemistry, analytical methods and clinical application. Clin Chem 1993; 39: 181–95
   PubMed Web of Science ®Google Scholar
• Kontturi M. Is acid phosphatase (PAP) still justified in the management of prostatic cancer%. Acta Oncol 1992; 30: 169–70
   Google Scholar
• Maatman T. J. The role of prostate specific antigen as a marker in men with advanced adenocarcinoma of the prostate. J Urol. 1989; 141: 1378–80
   PubMedGoogle Scholar
• Oesterling J. E. Prostate specific antigen: a crucial assessment of the most useful tumor marker for adenocarcinoma of the prostate. J Urol. 1991; 145: 907–23
   PubMed Web of Science ®Google Scholar
• Sharma S., Gupta M. K., Medendorp S., et al. PAP and PSA measurement in prostate cancer: indication to discontinue PAP testing (abstract). Clin Chem 1990; 36: 1048–9
   Google Scholar
• Drago J. R., Badalament R. A., Wientjes M. G., et al. Relative value of prostate-specific antigen and prostatic acid phosphatase in diagnosis and management of adenocarcinoma of the prostate. Urology 1989; 34: 187–92
   PubMed Web of Science ®Google Scholar
• Barak M., Macz Y., Lurie A., et al. Evaluation of prostate-specific antigen as a marker for adenocarcinoma of the prostate. J Lab Clin Med. 1989; 113: 598–603
   PubMedGoogle Scholar
• Arai Y., Yoshiki T., Okada K-I, et al. Multiple marker evaluation in prostate cancer using prostatic specific antigen, gamma-seminoprotein and prostatic acid phosphatase. Urol Int. 1989; 44: 135–40
   PubMed Web of Science ®Google Scholar
• Arai Y., Yoshiki T., Oishi K., et al. The role of prostatic specific antigen in monitoring prostatic cancer and its prognostic importance. Urol Res 1990; 18: 331–6
   PubMedGoogle Scholar
• Stamey T. A., Kabalin J. N., Ferradi M., et al. Prostate specific antigen in the diagnosis and treatment of adenocarcinoma of the prostate. Urol 1989; 141: 1070–5
   Google Scholar
• Oesterling J. E., Chan D. W., Epstein J. I., et al. Prostate specific antigen in the preoperative and postoperative evaluation of localized prostatic cancer treated with radical prostatectomy. J Urol. 1988; 139: 766–72
   PubMed Web of Science ®Google Scholar
• Schmid H. P., McNeal J. E., Stamey T. A. Observations on the doubling time of prostate cancer: the use of serial prostate-specific antigen in patients with untreated diseases as a measure of increasing cancer volume. Cancer 1993; 71: 2031–4
   PubMed Web of Science ®Google Scholar
• Lloyd AJI, Formby M. R. Conditions associated with normal levels of prostate-specific antigen and elevation of prostatic acid phosphatase. Am J Clin Oncol. 1992; 15: 487–9
   PubMedGoogle Scholar
• Gomella L. G., White J. L., McCue P. A., et al. Screening for occult nodal metastasis in localized carcinoma of the prostate. J Urol. 1993; 149: 776–8
   PubMedGoogle Scholar
• Cohen R. J., Glezerson G. Prostate-specific antigen and prostate-specific acid phosphatase in neuroendocrine cells of prostate cancer. Arch Pathol Lab Med. 1992; 116: 65–6
   PubMed Web of Science ®Google Scholar
• Gabby T., Winkleby W., Boyce T., et al. Sexual abuse of children: the detection of semen on skin. Am J Dis Child. 1992; 146: 700–3
   PubMedGoogle Scholar
• Roach B. A., Vladutiu A. O. Prostatic specific antigen and prostatic acid phosphatase measured by radioimmunoassay in vaginal washings from cases of suspected sexual assault. Clin Chim Acta. 1993; 216: 199–201
   PubMedGoogle Scholar
• Vihko P., Lukkarinen O., Kontturi M., et al. The effect of manipulation of the prostate gland on serum prostate-specific acid phosphatase measured by radioimmunoassay. Invest Urol 1981; 18: 334–6
   PubMedGoogle Scholar
• Johnson C. D., Costa D., Castro J. E. Acid phosphatase after examination of the prostate. Br J Urol. 1979; 51: 218–23
   PubMedGoogle Scholar
• Bannerjee S. K., Barker I. F., Waterworth T. A. Does rectal examination affect serum acid phosphatase levels%. Br J Surg 1979; 66: 512–3
   PubMedGoogle Scholar
• Pollen J. J., Dreilinger A. Immunohistochemical identification of prostatic acid phosphatase and prostate specific antigen in female periurethral glands. Urology 1984; 23: 303–4
   PubMed Web of Science ®Google Scholar
• Wernert N., Albrech M., Sesterhenn I. The female prostate: location, morphology, immunohistochemical characteristics and significance. Eur Urol. 1992; 22: 64–9
   PubMed Web of Science ®Google Scholar
• Korenchevsky V. The female prostatic gland and its reaction to male sexual compounds. J Physiol 1937; 90: 371–6
   PubMedGoogle Scholar
• Bruning E. J. Die Pathologie der weiblichen urethra und des Paraurethriums. Z. Geburtshilfe Gynaekol. 1959; 152: 1–111
   Google Scholar
• Huffman J. W. Clinical significance of the paraurethral ducts and glands. Arch Surg. 1951; 62: 615–26
   Web of Science ®Google Scholar
• Glenn J. F. Malignancy of the female urethra. NC Med J. 1953; 14: 201
   PubMedGoogle Scholar
• Knoblich R. Primary adenocarcinoma of the female urethra. Am J Obstet Gynecol 1950; 80: 353–64
   Google Scholar
• Sobin L. H., Hjermstad B. M., Sesterhenn I. A., et al. Prostatic acid phosphatase activity in carcinoid tumors. Cancer 1986; 58: 136–8
   PubMed Web of Science ®Google Scholar
• Peters O., Gorus F., De Boeck M., et al. Increased prostate-type acid phosphatase activity in serum and typical bone lesions stimulating the presence of prostatic carcinoma. Clin Chem 1984; 30: 803–4
   PubMedGoogle Scholar
• Klastersky J., Coune A. High serum acid phosphatase values in a case of lymphoblastic leukaemia. Br Med J. 1970; 4: 537–8
   PubMedGoogle Scholar
• Barracchia A., Vecce R., Lari R. An unusual increase in prostatic acid phosphatase not associated with prostate cancer (letter to editor). Haematologica 1988; 73: 249
   PubMedGoogle Scholar
• Lam KW, Li O., Li C. Y., Yam L. T. Biochemical properties of human prostatic acid phosphatase. Clin Chem. 1973; 19: 483–7
   PubMed Web of Science ®Google Scholar
• Efstratiadis T., Moss D. W. Tamate-resistant acid phosphatase of human lung: apparent identity with osteoclastic acid phosphatase. Enzyme. 1985; 33: 34–40
   PubMedGoogle Scholar
• Ketcham C. M., Baumbach G. A., Bazer F. W., et al. The type 5, acid phosphatase from spleen of humans with hairy cell leukemia. Purification, properties, immunological characterization and comparison with porcine uteroferrin. J Biol Chem. 1985; 260: 5768–76
   PubMed Web of Science ®Google Scholar
• Hayman A. R., Warburton M. J., Pringle JAS, et al. Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas. Biochem J. 1989; 261: 601–9
   PubMed Web of Science ®Google Scholar
• Burstone M. S. Histochemical demonstration of acid phosphatases with naphthol AS-phos-phates. J Natl Cancer Inst. 1958; 21: 523–39
   PubMed Web of Science ®Google Scholar
• Eggert F. M. Stable acid phosphatase. II. Effects of pH and inhibitors. Histochemistry 1980; 66: 319–29
   PubMedGoogle Scholar
• Minkin C. Bone acid phosphatase: tartrate-resistant acid phosphatase as a marker of osteoclast function. CalcifTiss Int. 1982; 34: 285–90
   PubMed Web of Science ®Google Scholar
• Efstratiadis T., Moss D. W. Tartrate-resistant acid phosphatase in human alveolar macrophages. Enzyme. 1985; 34: 140–3
   PubMedGoogle Scholar
• Moss D. W. Changes in enzyme expression related to differentiation and regulatory factors: the acid phosphatase of osteoclasts and other macrophages. Clin Chim Acta. 1992; 209: 131–8
   PubMed Web of Science ®Google Scholar
• Axline S. D. Isoenzymes of acid phosphatase in normal and Calmette-Guerin bacillus-induced rabbit alveolar macrophages. J Exp Med. 1968; 128: 1031–48
   PubMedGoogle Scholar
• Li C. U., Yam L. T., Lam K. W. Studies of acid phosphatase isoenzymes in human leukocytes. Demonstration of isoenzyme cell specificity. J Histochem Cytochem. 1970; 18: 901–10
   PubMed Web of Science ®Google Scholar
• Cassady Al, King A. G., Cross NCP, et al. Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase. Gene. 1993; 130: 201–7
   PubMed Web of Science ®Google Scholar
• Antanaitis B., Aisen P. Uteroferrin and the purple acid phosphatases. Advances in inorganic biochemistry, E. C. Thiel, G. L. Eichhorn, L. Marzilli. Elsevier, New York 1983; 111–36
   Google Scholar
• Hunt D. F., Yates J. R., III, Shabanowitz J., et al. Sequence homology in the metalloproteins: purple acid phosphatase from beef spleen and uteroferrin from porcine uterus. Biochem Biophys Res Commun 1987; 144: 1154–60
   PubMedGoogle Scholar
• Murray F. A., Bazer F. W., Wallace H. D., et al. Quantitative and qualitative variation in the secretion of protein by the porcine uterus during the estrous cycle. Biol Reprod. 1972; 7: 314
   PubMedGoogle Scholar
• Chen T. T., Bazer F. W., Gebhardt B., et al. Uterine secretion in mammals; synthesis and placental transport of a purple acid phosphatase in pigs. Biol Reprod. 1975; 13: 304–13
   PubMedGoogle Scholar
• Bevilacqua M. A., Lord D. K., Cross NCP, et al. Regulation and expression of type V (tartrate-resistant) acid phosphatase in human mononuclear phagocytes. Mol Biol Med. 1991; 8: 135–40
   PubMedGoogle Scholar
• Alcantara O., Reddy S. V., Roodman G. D., et al. Transcriptional regulation of the tartrate-resistant acid phosphatase (TRAP) gene by iron. Biochem J. 1994; 298: 421–5
   PubMed Web of Science ®Google Scholar
• Quesada T. R., Reuben J. R., Manning J. T., et al. Alpha interferon for induction of remission in hairy cell leukemia. N Engl J Med. 1984; 310: 15–8
   PubMed Web of Science ®Google Scholar
• Worman C. P., Catovsky D., Bevan P. C., et al. Interferon is effective in hairy cell leukaemia. Br J Haematol. 1985; 60: 757–63
   Google Scholar
• Ratain M. J., Golomb H. M., Vardiman J. W., et al. Treatment of hairy cell leukemia with recombinant alpha interferon. Blood 1985; 65: 644–8
   PubMed Web of Science ®Google Scholar
• Griffiths S. D., Catovsky J. C. The beneficial effects of a interferon in hairy cell leukemia are not attributable to NK cell-mediated cytotoxicity. Leukemia. 1987; 1: 372–6
   PubMed Web of Science ®Google Scholar
• Totterman T. H., Nilsson K., Sundstrom C. Phoibol ester-induced differentiation of chronic erythrocytic leukemia cells. Nature 1980; 288: 176–8
   PubMed Web of Science ®Google Scholar
• Caligaris-Cappio F., Pizzolo G., Chilosi M., et al. Phorbol ester induces abnormal chronic lymphocytic leukemia cells to express features of hairy cell leukemia. Blood. 1985; 66: 1035–42
   PubMed Web of Science ®Google Scholar
• Lam WKW, Eastlund D. T., Li C. T., et al. Biochemical properties of tartrate-resistant acid phosphatase in serum of adults and children. Clin Chem. 1978; 24: 1105–8
   PubMed Web of Science ®Google Scholar
• Robinson D. B., Glew R. H. Acid phosphatase in Gaucher's disease. Clin Chem. 1980; 26: 371–82
   PubMed Web of Science ®Google Scholar
• Yam L. T., Li C-Y, Finkel H. E. Leukemic reticuloendotheliosis. Arch Intern Med. 1972; 130: 248–56
   PubMed Web of Science ®Google Scholar
• Korsmeyer S. J., Greene W. C., Cossman J., et al. Rearrangement and expression of immunoglobulin genes and expression of Tac antigen in hairy cell leukemia. Proc Natl Acad Sci USA 1983; 80: 4522–5
   PubMed Web of Science ®Google Scholar
• Ketcham C. M., Roberts R. M., Simmen RCM, et al. Molecular cloning of the type 5, iron-containing, tartrate-resistant acid phosphatase from human placenta. J Biol Chem. 1989; 264: 557–63
   PubMed Web of Science ®Google Scholar
• Lam K. W., Yam L. T. Biochemical characterization of tartrate-resistant acid phosphatase of human spleen with leukemic reticuloendotheliosis as a pyrophosphatase. Clin Chem. 1977; 23: 89–94
   PubMed Web of Science ®Google Scholar
• Echetebu Z. O., Cox T. M., Moss D. W. Antibodies to porcine uteroferrin used in measurement of human tartrate-resistant acid phosphatase. Clin Chem. 1987; 33: 1832–6
   PubMed Web of Science ®Google Scholar
• Chersi A., Bemardi A., Bemardi G. Studies on acid hydrolases. II. Isolation and properties of spleen acid phosphomonoesterase. Biochim Biophys Acta 1966; 129: 12–22
   PubMedGoogle Scholar
• Lam K-W, Siemens M., Sun T., et al. Enzyme immunoassay for tartrate-resistant acid phosphatase. Clin Chem 1982; 28: 467–70
   PubMed Web of Science ®Google Scholar
• Zaidi M., Moonga B., Moss D. W., et al. Inhibition of osteoclastic acid phosphatase abolishes bone resorption. Biochem Biophys Res Commun. 1989; 159: 68–71
   PubMed Web of Science ®Google Scholar
• Hayman A. R., Cox T. M. Purple acid phosphatase of the human macrophage and osteoclast. Characterization, molecular properties, and crystallization of the recombinant di-iron-oxo protein secreted by baculovirus-infected insect cells. J Biol Chem. 1994; 269: 1294–1300
   PubMedGoogle Scholar
• Vaes G. On the mechanisms of bone resorption. The action of parathyroid hormone on the excretion and synthesis of lysosomal enzymes and on the extracellular release of acid by bone cells. J Cell Biol. 1968; 39: 676–97
   PubMed Web of Science ®Google Scholar
• Chambers T. J., Fuller K., Darby J. A. Hormonal regulation of acid phosphatase release by osteoclasts disaggregated from neonatal rat bone. J Cell Physiol. 1987; 132: 90–7
   PubMed Web of Science ®Google Scholar
• Moss D. W., Henderson R. A., Kachmar J. F. Acid phosphatase. Textbook of clinical chemistry, N. W. Tietz. W. B. Saunders, Philadelphia 1986; 752–63
   Google Scholar
• Bucher T., Durnwald M., Fuhrer S., et al. Quantitative evaluation of serum alkaline phosphatase isozyme patterns. Abstr commun, jt meet Assoc Clin Biochem, UK, Netherlands Soc Clin Chem, and German Soc for Clin Chem, Newcastle-upon-Tyne, UK. April, 1983
   Google Scholar
• Rosalki S. B., Foo Y. A. Two new methods for separating and quantifying bone and liver isoenzymes in plasma. Clin Chem 1984; 30: 1182–6
   PubMed Web of Science ®Google Scholar
• Moss D. W., Edwards R. K. Improved electrophoretic resolution of bone and liver alkaline phosphatases resulting from partial digestion with neuraminidase. Clin Chim Acta. 1984; 143: 177–82
   PubMedGoogle Scholar
• Moonga B. S., Moss D. W., Patchell A., et al. Intracellular regulation of enzyme secretion from rat osteoclasts and evidence for a functional role in bone resorption. J Physiol. 1990; 429: 29–45
   PubMed Web of Science ®Google Scholar
• Moonga B. S., Pazianas M., Towhidul Alam ASM, et al. Stimulation of a Gs-like G protein in the osteoclast inhibits bone resorption but enhances tartrate-resistant acid phosphatase secretion. Biochem Biophys Res Commun. 1993; 190: 496–501
   PubMedGoogle Scholar
• Felix R., Russell RGG, Fleisch H. The effect of several diphosphonates on acid phosphohydrolases and other lysosomal enzymes. Biochim Biophys Acta. 1976; 429: 429–38
   PubMed Web of Science ®Google Scholar
• Tuchman L. R., Swick M. High acid phosphatase level indicating Gaucher's disease in patient with prostatism. JAMA 1957; 164: 2034–5
   PubMedGoogle Scholar
• Matoth Y., Fried K. Chronic Gaucher's disease. hr J Med Sci 1965; 1: 521–30
   Google Scholar
• Streifler C. Study of acid phosphatase in sera of Gaucher's disease patients, subcellular tissue fractions and platelet extracts. hr J Med Sci 1970; 6: 479–87
   Google Scholar
• Bouroncle B. A., Wiseman B. K., Doan C. A. Leukemic reticuloendotheliosis. Blood. 1958; 13: 609–30
   PubMed Web of Science ®Google Scholar
• Katayama I., Finkel H. E. Leukemic reticuloendotheliosis. A clinicopathologic study with review of the literature. Am J Med 1974; 57: 115–26
   PubMed Web of Science ®Google Scholar
• Catovsky D. Hairy cell leukaemia and prolymphocytic leukaemia. Clin Haematol. 1977; 6: 245–68
   PubMedGoogle Scholar
• Golomb H. M., Catovsky D., Golde D. W. Hairy cell leukemia: a clinical review based on 71 cases. Ann Intern Med 1978; 89: 677–83
   PubMed Web of Science ®Google Scholar
• Bouroncle B. A. Leukemic reticuloendotheliosis (hairy cell leukemia). Blood 1979; 53: 412–36
   PubMed Web of Science ®Google Scholar
• Pilon V. A., Davey F. R., Gordon G. B., et al. Splenic alterations in hairy cell leukemia. II. An electron microscopic study. Cancer 1982; 49: 1617–23
   PubMedGoogle Scholar
• Golomb H. M., Vardiman J. W. Response to splenectomy in 65 patients with hairy cell leukemia: an evaluation of spleen weight and bone marrow involvement. Blood. 1983; 61: 349–52
   PubMed Web of Science ®Google Scholar
• Flandrin G., Sigaux F., Sebahoun G., et al. Hairy cell leukemia: clinical presentation and follow-up of 211 patients. Semin Oncol. 1984; 11: 458–71
   PubMed Web of Science ®Google Scholar
• Offerman M. R., Golomb H. M. Hairy cell leukemia. Curr Probl Cancer. 1984; 8: 1–39
   Google Scholar
• Golomb H. M., Ratain M. J., Vardiman J. W. Sequential treatment of hairy cell leukemia: a new role for interferon. Important advances in oncology, V. T. Devitas, S. Hellman, S. A. Rosenberg. J. B. Lippincott, Philadelphia 1986; 311–21
   Google Scholar
• Bouroncle B. A., Grever M. R., Kraut E. H. Treatment of hairy cell leukemia: the Ohio State experience with deoxycoformycin. Leukemia 1987; 1: 350–4
   PubMed Web of Science ®Google Scholar
• Yam L. T., Li C. Y., Finkel H. E. Leukemia reticuloendotheliosis. The role of tartrate-resistant acid phosphatase in diagnosis and splenectomy in treatment. Arch Intern Med. 1972; 130: 248–56
   PubMed Web of Science ®Google Scholar
• Yam L. T., Li C. Y., Lam K. W. Tartrate-resistant acid phosphatase isoenzyme in the reticulum cells of leukemic reticuloendotheliosis. N Engl J Med. 1971; 284: 357–60
   PubMed Web of Science ®Google Scholar
• Boesen A. M. Ultrastructural localization of acid phosphatase in immunologically defined neoplastic lymphocytic cells and hairy cells: a comparison between two different substrates. Scand J Haematol. 1984; 32: 245–52
   PubMedGoogle Scholar
• Yam L. T., Janckila A. J., Li C. Y., et al. Cytochemistry of tartrate-resistant acid phosphatase: 15 years' experience. Leukemia 1987; 1: 285–8
   PubMed Web of Science ®Google Scholar
• Variakojis D., Vardiman J. W. Golomb H. M. Cytochemistry of hairy cells. Cancer 1980; 45: 72–7
   PubMedGoogle Scholar
• Burns G. F., Cawley J. C., Worman C. P., et al. Multiple heavy chain isotypes on the surface of the cells of hairy cell leukemia. Blood 1978; 52: 1132–47
   PubMed Web of Science ®Google Scholar
• Golomb H. M., Davis S., Wilson C., et al. Surface immunoglobulins on hairy cells of 55 patients with hairy cell leukemia. Am J Hematol. 1982; 12: 397–401
   PubMed Web of Science ®Google Scholar
• Jansen J., Schuit H. R., Meijer C. J., et al. Cell markers in hairy cell leukemia studied in cells from 51 patients. Blood 1982; 59: 52–60
   PubMed Web of Science ®Google Scholar
• Jansen J., Le Bien T. W., Kersey J. H. The phenotype of the neoplastic cells of hairy cell leukemia studied with monoclonal antibodies. Blood 1982; 59: 609–14
   PubMed Web of Science ®Google Scholar
• Meijer C. J., van der Valk P., Jansen J. Hairy cell leukemia: an immunohistochemic and morphometric study. Semin Oncol. 1984; 11: 347–52
   PubMed Web of Science ®Google Scholar
• Jansen J., den Ottolander G. J., Schuit H. R., et al. Hairy cell leukemia: its place among the chronic B cell leukemias. Semin Oncol. 1984; 11: 386–93
   PubMed Web of Science ®Google Scholar
• Anderson K. C., Boyd A. W., Fisher D. C., et al. Hairy cell leukemia: a tumor of pre-plasma cells. Blood 1985; 65: 620–9
   PubMed Web of Science ®Google Scholar
• Gardner F. H., Pringle J. C., Jr. Androgens and erythropoiesis. Arch Intern Med. 1961; 107: 846–62
   PubMed Web of Science ®Google Scholar
• Spiers A. S., Parekh S. J. The treatment of hairy cell leukemia (HCL) with pentostatin (2'-deoxycoformycin, dCF). Bone Marrow Transpl. 1989; 4: 173–95
   PubMedGoogle Scholar
• Johnston J. B., Glazer R. I., Pugh L., et al. The treatment of hairy cell leukemia with 2-deoxycoformycin. Br J Haematol. 1986; 63: 525–34
   PubMed Web of Science ®Google Scholar
• Kraut E. H., Bouroncle B. A., Grever M. R. Low dose deoxycoformycin in the treatment of hairy cell leukemia. Blood 1986; 68: 1119–22
   PubMed Web of Science ®Google Scholar
• Spiers ASD, Moore D., Cassileth P. A., et al. Remissions in hairy cell leukemia with pentostatin (2-deoxycoformycin). N Engl J Med. 1987; 316: 825–30
   PubMed Web of Science ®Google Scholar
• Johnston J. B., Eisenhauer E., Corbett W. E., et al. Efficacy of 2'-deoxycoformycin in hairy-cell leukemia: a study of the National Cancer Institute of Canada Clinical Trials Group. JNC1 1988; 80: 765–9
   PubMed Web of Science ®Google Scholar
• Piro L. D., Carrera C. J., Carson D. A., et al. Lasting remissions in hairy cell-leukemia induced by a single infusion of 2-chlorodeoxyadenosine. N Engl J Med. 1990; 322: 1117–21
   PubMed Web of Science ®Google Scholar
• Durrelman S., Grem J. L., Cheson B. D. 2'-Deoxycoformycin after failure of alpha interferon in hairy cell leukaemia. Eur J Haematol 1989; 43: 297–302
   PubMedGoogle Scholar
• Capelli A., Lusuardi M., Carli S., et al. Acid phosphatase (EC 3.1.3.2). Activity in alveolar macrophages from patients with active sarcoidosis. Chest 1991; 99: 546–50
   PubMedGoogle Scholar