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Conversion of Angiotensin I to Angiotensin II by cathepsin A isoenzymes of porcine kidney

Miller, James J., Changaris, David G., Levy, Robert S.·1988·Biochemical and Biophysical Research Communications
DOI 10.1016/0006-291x(88)90257-4
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Abstract

We have reported the existence of a carboxypeptidase in a human renal extract that converts Angiotensin I (AI) to Angiotensin II (AII) in two steps with des-leu-AI (dl-AI) being formed as an intermediate. Since this carboxypeptidase had properties similar to cathepsin A, the ability of cathepsin A to metabolize AI was studied. Cathepsin A was purified from hog kidney with enzyme activity being monitored using both benzyloxycarbonyl-glutamyl-tyrosine (ZGT) and AI as substrates. The procedure separated the expected large and small molecular weight forms of cathepsin A as well as two additional isoenzymes. All of the isoenzymes had carboxypeptidase activity with ZGT, AI, and dl-AI. No detectable cleavage of AII was observed. Cathepsin A,S (small) activity with ZGT or AI as substrate was inhibited to a similar extent by diisopropylfluorophosphate, mersalyl acid, and a decapeptide renin inhibitor. It is concluded that the renal angiotensin carboxypeptidase activity is catalyzed by cathepsin A. By its ability to convert AI to AII, cathepsin A may be a component of the intrarenal renin-angiotensin system.

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Crossref · 10.1016/0006-291x(88)90257-4

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  • CTSA is an important member/player of the renin-angiotensin system regulating blood pressure and water balance.

    “The role of CTSA in conversion of angiotensin-I to angiotensin-II suggests that CTSA may be an important player of the renin-angiotensin system regulating blood pressure and water balance (Miller et al., 1988).”

    From Lysosomal Cathepsin A Plays a Significant Role in the Processing of Endogenous Bioactive Peptides (2016) · cites this paper as Miller et al., 1988

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Research works printed but not linked: 16

  1. Changaris, 1986, Biochem. Biophys. Res. Commun, 138, 573, 10.1016/S0006-291X(86)80535-6 · DOI
  2. Tallan, 1952, J. Biol. Chem, 194, 793, 10.1016/S0021-9258(18)55834-8 · DOI
  3. Lichtenstein, 1960, 46, 787
  4. Doi, 1974, J. Biochem, 75, 881, 10.1093/oxfordjournals.jbchem.a130461 · DOI
  5. Doi, 1974, J. Biochem, 75, 889, 10.1093/oxfordjournals.jbchem.a130462 · DOI
  6. Kawamura, 1974, J. Biochem, 76, 915
  7. Kawamura, 1975, J. Biochem, 77, 729, 10.1093/oxfordjournals.jbchem.a130776 · DOI
  8. Kawamura, 1977, J. Biochem, 81, 435, 10.1093/oxfordjournals.jbchem.a131476 · DOI
  9. Miller, 1988, FASEB Journal, 2, A1479
  10. Matsuda, 1974, J. Biochem, 76, 639, 10.1093/oxfordjournals.jbchem.a130608 · DOI
  11. Matsuda, 1975, J. Biochem, 78, 31
  12. Grynbaum, 1976, J. Neurochem, 26, 313, 10.1111/j.1471-4159.1976.tb04482.x · DOI
  13. Logunov, 1972, Biochem. Biophys. Res. Commun, 46, 1161, 10.1016/S0006-291X(72)80096-2 · DOI
  14. Snyder, 1985, J. Biol. Chem, 260, 7857, 10.1016/S0021-9258(17)39531-5 · DOI
  15. Marks, 1976, J. Neurochem, 27, 765, 10.1111/j.1471-4159.1976.tb10405.x · DOI
  16. Rajaraman, 1988, FASEB Journal, 2, A1478

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Metadata

Authors
Miller, J. J., Changaris, D. G., & Levy, R. S.
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
1988-08
Volume
154
Issue
3
Pages
1122-1129
ISSN
0006-291X
DOI
10.1016/0006-291x(88)90257-4
Cited by
28
References
0
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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