Angiotensin I Converting Enzyme in Glycerol-Induced Acute Renal Failure in Rats

References

• Erdös E G, Skidgel R A. The angiotensin I-converting enzyme. Lab Invest 1987; 56: 345–348
   PubMed Web of Science ®Google Scholar
• Ehlers M RW, Riordan J F. Angiotensin-converting enzyme: biochemistry and molecular biology. Hypertension: Pathophysiology, Diagnosis, and Management, J H Laragh, B M Brenner. Raven Press, New York 1990; 1217–1231
   Google Scholar
• Cushman D W, Cheung H S. Concentration of angiotensin converting enzyme in tissues of the rat. Biochim Biophys Acta 1971; 250: 261–265
   PubMed Web of Science ®Google Scholar
• Wilson S K, Lynch D R, Snyder S H. Angiotensin-converting enzyme labeled with [3H]captopril. Tissue localizations and changes in different models of hypertension in the rat. J Clin Invest 1987; 80: 841–851
   Google Scholar
• Kohzuki M, Johnston C I, Chai S Y, Jackson B, Perich R, Paxton D, Mendelsohn F AO. Measurement of angiotensin converting enzyme induction and inhibition using quantitative in vitro autoradiography: tissue selective induction after chronic lisinopril treatment. J Hyperten 1991; 9: 579–587
   PubMed Web of Science ®Google Scholar
• Schulz W W, Hagler H K, Buja L M, Erdös E G. Ultrastructural localization of angiotensin I-converting enzyme (EC 3.4.15.1) and neutral metalloendopeptidase (EC 3.4.24.11) in the proximal tubule of the human kidney. Lab Invest 1988; 59: 789–797
   PubMedGoogle Scholar
• Ikemoto F, Song G B, Tominaga M, Kanayama Y, Yamamoto K. Angiotensin converting enzyme predominates in the inner cortex and medulla of the rat kidney. Biochem Biophys Res Commun 1987; 144: 915–921
   PubMed Web of Science ®Google Scholar
• Kokubu T, Kato Y, Nishimura K, Hiwada K, Ueda E. Angiotensin I-converting enzyme in human urine. Clin Chim Acta 1978; 89: 375–379
   PubMed Web of Science ®Google Scholar
• Baggio B, Favaro S, Cantaro S, Bertazzo L, Frunzio A, Borsatti A. Increased urine angiotensin I-converting enzyme activity in patients with upper urinary tract infection. Clin Chim Acta 1981; 109: 211–218
   PubMedGoogle Scholar
• Baggio B, Picolli A, Favaro S, Antonello A, Bertaglia E, Borsatti A. Urinary angiotensin I-converting enzyme activity as a marker of tubulo-interstitial involvement in kidney diseases. Contr Nephrol 1989; 70: 208–212
   PubMedGoogle Scholar
• Pitotti A, Maurich V, Moneghini M, Vianello S. HPLC method for evaluation of urinary angiotensin-converting enzyme: some examples of normal subjects and patients with renal transplantation. J Pharm Biomed Anal 1986; 4: 677–683
   PubMedGoogle Scholar
• Hosojima H, Miyauchi E, Morimoto S. Urinary excretion of angiotensin-converting enzyme in NIDDM patients with nephropathy. Diabetes Care 1989; 12: 580–582
   PubMedGoogle Scholar
• Kato J, Takada Y, Nishimura K, Hiwada K, Kokubu T. Increased urinary excretion of angiotensin converting enzyme in patients with renal diseases. J Clin Chem Clin Biochem 1982; 20: 473–476
   PubMedGoogle Scholar
• Pedraza-Chaverrí J, Cruz C, Hernández-Pando R, Santana T, Arévalo A E, González L, Tapia E, Peña J C, Panduro A. Angiotensin I-converting enzyme activity in rats with carbon tetrachloride-induced acute renal failure. Ren Fail 1993; 15: 19–26
   PubMed Web of Science ®Google Scholar
• Wolfert A I, Oken D E. Glomerular hemodynamics in established glycerol-induced acute renal failure in the rat. J Clin Invest 1989; 84: 1967–1973
   PubMed Web of Science ®Google Scholar
• Thiel G, Wilson D R, Arce M L, Oken D E. Glycerol induced hemoglobinuric acute renal failure in the rat. Nephron 1967; 4: 276–297
   PubMedGoogle Scholar
• Westenfelder C, Arevalo G J, Crawford P W, Zerwer P, Baranowski R L, Birch F M, Earnest W R, Hamburger R K, Coleman R D, Kurtzman N A. Renal tubular function in glycerol-induced acute renal failure. Kidney Int 1980; 18: 432–444
   PubMedGoogle Scholar
• Pedraza-Chaverrí J, Tapia E, Bobadilla N. Ischemia-reperfusion induced acute renal failure in the rat is ameliorated by the spin-trapping agent α-phenyl-N-tert-butyl nitrone (PBN). Ren Fail 1992; 14: 467–471
   PubMed Web of Science ®Google Scholar
• Urinary Enzymes in Clinical and Experimental Medicine, K Jung, H Mattenheimer, U Burchardt. Springer-Verlag, Berlin 1992
   Google Scholar
• Wolf G, Scherberich J E, Nowack A, Stein O, Schoeppe W. Urinary excretion of dipeptidyl aminopeptidase IV in patients with renal disease. Clin Nephrol 1990; 33: 136–142
   PubMedGoogle Scholar
• Pesce A J, Boreisha I, Pollak V E. Rapid differentiation of glomerular and tubular proteinuria by sodium dodecyl sulfate polyacrilamide gel electrophoresis. Clin Chim Acta 1972; 40: 27–34
   PubMed Web of Science ®Google Scholar
• Bernard A, Lauwrys R R. Proteinuria: changes and mechanisms in toxic nephropathies. Cr Rev Toxicol 1991; 21: 373–405
   PubMed Web of Science ®Google Scholar
• Pedraza-Chaverrí J, Calderón P, Cruz C, Peña J C. Electrophoretic analysis of serum and urinary proteins in rats with aminonucleoside-induced nephrotic syndrome. Ren Fail 1993; 15: 149–155
   PubMed Web of Science ®Google Scholar
• Pedraza-Chaverrí J, Cruz C, Tapia E, Peña J C. Activity of serum enzymes in puromycin aminonucleoside-induced nephrotic syndrome. Ren Fail 1992; 14: 523–531
   PubMed Web of Science ®Google Scholar
• Nagatsu T, Hino M, Fuyamada H, Hayakawa T, Sakakibara S, Nakagawa Y, Takemoto T. New chromogenic substrates for X-prolyl dipeptidyl-aminopeptidase. Anal Biochem 1976; 74: 466–476
   PubMed Web of Science ®Google Scholar
• Skhra J, Perusicová J, Stolba P, Stibor V, Páv J. Comparison of N-acetyl-β-glucosaminidase and albuminuria with clinical finding of microangiopathy in type I diabetes mellitus. Clin Chim Acta 1987; 166: 135–141
   Google Scholar
• Wellwood J M, Price R G, Ellis B G, Thompson A E. A note on the practical aspects of the assay of N-acetyl-β-glucosaminidase in human urine. Clin Chim Acta 1976; 69: 85–91
   PubMedGoogle Scholar
• Nortier J, Abramowicz D, Najdovski T, Kinnaert P, Vanherweghem J-L., Goldman M, Deschodt-Lanckman M. Urinary endopeptidase 24.11 as a new marker of proximal tubular injury. Contr Nephrol 1993; 101: 169–176
   Google Scholar
• Erman A, Van Dyk D J, Chen-Gal B, Giler I DS, Rosenfeld J B, Boner G. Angiotensin converting enzyme activity in the serum, lung and kidney of diabetic rats. Eur J Clin Invest 1993; 23: 615–620
   Google Scholar
• Erman A, Chen-Gal B, Zabludowski J, Rosenfeld J B. Cyclosporin A treatment enhances angiotensin converting enzyme activity in lung and serum of rats. J Pharm Pharmacol 1990; 42: 525–527
   PubMed Web of Science ®Google Scholar
• Hollinger M A, Giri S N, Patwell S, Zuckerman J E, Gorin A, Parsons G. Effect of acute lung injury on angiotensin-converting enzyme in serum, lung lavage, and effusate. Am Rev Resp Dis 1980; 121: 373–376
   PubMed Web of Science ®Google Scholar
• Pedraza-Chaverrí J, Maciel A H, Cruz C, Peña J C. Captopril magnifies the increase in angiotensin I-converting enzyme activity in rats with aminonucleoside nephrosis. Clin Exp Pharmacol Physiol 1992; 19: 439–445
   PubMedGoogle Scholar
• Forslund T, Kouvonen I, Fyhrquist F. Tissue distribution of angiotensin converting enzyme in the rat: effect of captopril treatment. Acta Pharmacol Toxicol 1984; 54: 124–128
   PubMedGoogle Scholar
• Kokubu T, Ueda E, Ono M, Kawabe T, Hayashi Y, Kan T. Effects of captopril (SQ 14,225) on the reninangiotensin-aldosterone system in normal rats. Eur J Pharmacol 1980; 62: 269–275
   PubMed Web of Science ®Google Scholar