Molecular biology of the angiotensin I converting enzyme: I. Biochemistry and structure of the gene

Soubrier, Florent; Hübert, Christine; Testut, Patrice; Nadaud, Sophie; Alhenc-Gelas, Fran ois; Corvol, P

doi:10.1097/00004872-199305000-00001

Cited by 79 publications

(59 citation statements)

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“…The molecular mass found for the ACE forms S-1/SP-1/ Sen-1 (80 kDa), S-2/SP-2/Sen-2 (65 kDa) from urine of SHR, SHR-SP, SRHen rats; C-2 (65 kDa) from urine of 1K1C rats; DC-2/D2 (65 kDa) from urine of DOCA salt control and D-2 DOCA salt and BN-2 (65 kDa) from urine of BN rats was much lower than testicular ACE (90 to 100 kDa), which is heavily glycosylated, although they were similar to that of the nonglycosylated form of the single-domain tACE (76 to 84 kDa) 36,37 and the N-domain ACE (65 to 68 kDa) found recently in human urine 19 and ileal fluid. 38 When we compared the forms from WKY rats and ACE BN-1, with 190 kDa and BN-2, with 65 kDa, the data indicated that different strains presented the same enzyme forms.…”

Section: Discussionmentioning

confidence: 93%

N-Domain Angiotensin I-Converting Enzyme With 80 kDa as a Possible Genetic Marker of Hypertension

et al. 2003

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Abstract-We have previously described angiotensin I-converting enzyme (ACE) forms in urine of normotensive (190 and 65 kDa) and hypertensive patients (90 and 65 kDa, N-domain ACEs). Based on the results described above, experimental and genetic models of hypertension were investigated to distinguish hemodynamic and genetic influence on the generation of ACE profile in urine: Wistar-Kyoto and Brown Norway rats (WKY and BN), spontaneously and stroke-prone spontaneously hypertensive rats (SHR and SHR-SP), one kidney/one clip rats (1K1C), deoxycorticosterone acetate (DOCA) salt-treated and untreated rats, and enalapril-treated SHR (SHRen). Two peaks with ACE activity were separated from the urine of WKY and BN rats submitted to an AcA-44 column, WK-1/BN-1 (190 kDa), and WK-2/BN-2 (65 kDa), as described for urine of normotensive subjects. The same results were obtained for urine of 1K1C and DOCA salt-treated and untreated rats, analyzed to evaluate the influence of hemodynamic factors in the ACE profile in urine. The urine from SHR, SHR-SP, and SHRen presented 80 (S-1, SP-1, Sen-1) and 65 (S-2, SP-2, Sen-2) kDa ACE forms, differing from the urine profile of normotensive rats, but similar to that described for hypertensive patients. The presence of 80 kDa ACE in urine of SHR, SHR-SP, and SHRen and its absence in urine of experimental hypertensive rats (1K1C and DOCA salt) support the hypothesis that this enzyme could be a possible genetic marker of hypertension. Taken together, our results provide evidence that ACE forms with 90/80 kDa isolated from the urine of hypertensive subjects and genetic hypertensive animals behaves as a possible genetic marker of hypertension and not as a marker of high blood pressure.

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Section: Discussionmentioning

confidence: 93%

N-Domain Angiotensin I-Converting Enzyme With 80 kDa as a Possible Genetic Marker of Hypertension

et al. 2003

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“…Some, like those responsible for posttranslational processing of proteins or peptides, e.g., Angiotensin Converting Enzyme, are highly sequence specific [12]. Others, like Proteinase K, cleave all peptide bonds non-specifically [13].…”

Section: Introductionmentioning

confidence: 99%

Metal assisted peptide bond hydrolysis: Chemistry, biotechnology and toxicological implications

Wezynfeld

Frączyk

Bal

2016

Coordination Chemistry Reviews

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“…Ang-(1-7) was incubated with another source of C-ACE, somatic ACE, 23,24 where His in positions 361 and 365 was mutated to Lys, thereby rendering the N-ACE domain inactive. Ang-(1-7) in these experiments was not hydrolyzed by the C-ACE (10 nmol/L), although the enzyme cleaved HipHis-Leu (data not shown).…”

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confidence: 99%

N-Domain–Specific Substrate and C-Domain Inhibitors of Angiotensin-Converting Enzyme

et al. 1998

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Abstract-We used the isolated N-and C-domains of the angiotensin I-converting enzyme (N-ACE and C-ACE; ACE; kininase II) to investigate the hydrolysis of the active 1-7 derivative of angiotensin (Ang) II and inhibition by 5-S-5-benzamido-4-oxo-6-phenylhexanoyl-L-proline (keto-ACE). Ang-(1-7) is both a substrate and an inhibitor; it is cleaved by N-ACE at approximately one half the rate of bradykinin but negligibly by C-ACE. It inhibits C-ACE, however, at an order of magnitude lower concentration than N-ACE; the IC 50 of C-ACE with 100 mol/L Ang I substrate was 1.2 mol/L and the K i was 0.13. While searching for a specific inhibitor of a single active site of ACE, we found that keto-ACE inhibited bradykinin and Ang I hydrolysis by C-ACE in approximately a 38-to 47-times lower concentration than by N-ACE; IC 50 values with C-ACE were 0.5 and 0.04 mol/L. Furthermore, we investigated how Ang-(1-7) acts via bradykinin and the involvement of its B 2 receptor. Ang-(1-7) was ineffective directly on the human bradykinin B 2 receptor transfected and expressed in Chinese hamster ovary cells. However, Ang-(1-7) potentiated arachidonic acid release by an ACE-resistant bradykinin analogue (1 mol/L), acting on the B 2 receptor when the cells were cotransfected with cDNAs of both B 2 receptor and ACE and the proteins were expressed on the plasma membrane of Chinese hamster ovary cells. Thus like other ACE inhibitors, Ang-(1-7) can potentiate the actions of a ligand of the B 2 receptor indirectly by binding to the active site of ACE and independent of blocking ligand hydrolysis. This potentiation of kinins at the receptor level can explain some of the well-documented kininlike actions of Ang-(1-7).(Hypertension. 1998;31:912-917.)

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Molecular biology of the angiotensin I converting enzyme: I. Biochemistry and structure of the gene

Cited by 79 publications

References 0 publications

N-Domain Angiotensin I-Converting Enzyme With 80 kDa as a Possible Genetic Marker of Hypertension

N-Domain Angiotensin I-Converting Enzyme With 80 kDa as a Possible Genetic Marker of Hypertension

Metal assisted peptide bond hydrolysis: Chemistry, biotechnology and toxicological implications

N-Domain–Specific Substrate and C-Domain Inhibitors of Angiotensin-Converting Enzyme

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