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Human converting enzyme.

E G Erdös, J T Gafford

    Clinical and Experimental Hypertension. Part A, Theory and Practice
    |January 1, 1983
    PubMed
    Summary

    This study purified human kidney angiotensin I converting enzyme (ACE), revealing its transmembrane nature and presence in the central nervous system. Immunological identity across tissues and a correlation with sarcoidosis lung function were also found.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Neuroscience

    Background:

    • Angiotensin I converting enzyme (ACE), also known as kininase II or peptidyl dipeptidase, plays crucial roles in various physiological processes.
    • Understanding the structure, localization, and function of ACE is essential for comprehending its involvement in both normal physiology and disease states.

    Purpose of the Study:

    • To purify and characterize Angiotensin I converting enzyme (ACE) from human kidney membranes.
    • To investigate the localization and immunological properties of ACE in different tissues, including the central nervous system (CNS).
    • To explore the potential correlation between plasma ACE levels and pulmonary function in patients with sarcoidosis.

    Main Methods:

    • Purification of ACE using reverse immunoadsorption from human kidney membrane fractions.
    • Enzymatic treatment with trypsin to identify membrane-bound fragments.
    • Immunohistochemical localization of ACE in the CNS using specific antibodies.
    • Radioimmunoassay (RIA) to assess ACE levels and immunological identity across various origins.
    • Direct RIA to correlate plasma ACE levels with pulmonary diffusing capacity in sarcoidosis patients.

    Main Results:

    • ACE was successfully purified and identified as a likely transmembrane peptidase, with a portion potentially anchoring it to the plasma membrane.
    • ACE was localized in the CNS, specifically on the plasma membrane of neuroepithelial cells in areas like the globus pallidus and substantia nigra.
    • Radioimmunoassays demonstrated that ACE from endothelial, epithelial, and neuroepithelial sources are immunologically identical.
    • A significant negative correlation was observed between plasma ACE levels and pulmonary diffusing capacity in patients suffering from sarcoidosis.
    • Homogeneous human ACE was shown to cleave specific fluorogenic substrates, including those with a modified C-terminal amino acid.

    Conclusions:

    • Human kidney ACE is a transmembrane enzyme with a distinct membrane-anchoring peptide.
    • ACE is present in the CNS, associated with neuroepithelial cells, suggesting potential roles in neural functions.
    • The immunological similarity of ACE across different cell types supports a conserved structure and function.
    • Plasma ACE levels may serve as a biomarker for assessing lung function impairment in sarcoidosis.
    • The substrate specificity of purified human ACE provides insights into its enzymatic activity.

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