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The angiotensin I converting enzyme.

E G Erdös

    Federation Proceedings
    |April 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Angiotensin I converting enzyme (ACE) has a dual role in converting angiotensin I to angiotensin II and inactivating bradykinin. ACE inhibitors are crucial for understanding its function in various conditions.

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    Area of Science:

    • Biochemistry
    • Physiology
    • Pharmacology

    Background:

    • The angiotensin I converting enzyme (ACE), also known as kininase II, is a key enzyme in the renin-angiotensin system.
    • ACE possesses a dual function: catalyzing the conversion of angiotensin I to angiotensin II and the degradation of bradykinin.
    • This enzyme is widely distributed, with rich sources found in lung, kidney, guinea pig plasma, and testicles.

    Purpose of the Study:

    • To elucidate the physiological and pathological roles of ACE.
    • To highlight the significance of ACE in cardiovascular regulation and other biological processes.
    • To underscore the utility of synthetic peptide inhibitors in studying ACE function.

    Main Methods:

    • Enzyme activity assays to determine ACE function.

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  • Localization studies to identify high-concentration tissue sources.
  • Pharmacological studies utilizing synthetic peptide inhibitors.

    • Main Results:

    • ACE was confirmed to have a dual role in angiotensin II production and bradykinin inactivation.
    • High concentrations of ACE were identified in vascular endothelial cells and renal proximal tubular cells.
    • Synthetic peptide inhibitors proved instrumental in dissecting ACE's functions.

    Conclusions:

    • ACE plays a critical role in both the renin-angiotensin system and kinin-kallikrein system.
    • The enzyme's distribution highlights its importance in vascular and renal physiology.
    • Pharmacological tools, particularly ACE inhibitors, are essential for advancing our understanding of this enzyme's multifaceted roles.