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Action of brain cathepsin B, cathepsin D, and high-molecular-weight aspartic proteinase on angiotensins I and II

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Abstract

The action of three previously isolated electrophoretically homogeneous brain proteinases—cathepsin B (EC 3.4.22.1), cathepsin D (EC 3.4.23.5), and high-molecular-weight aspartic proteinase (Mr=90K; EC 3.4.23.−)—on human angiotensins I and II has been investigated. The products of enzymatic hydrolysis have been identified by thin-layer chromatography on Silufol plates using authentic standards and by N-terminal amino acid residue analysis using a dansyl chloride method. Cathepsin D and high-molecular-weight aspartic proteinase did not split angiotensin I or angiotensin II. Cathepsin B hydrolyzed angiotensin I via a dipeptidyl carboxypeptidase mechanism removing His-Leu to form angiotensin II, and it degraded angiotensin II as an endopeptidase at the Val3-Tyr4 bond. Cathepsin B did not split off His-Leu from Z-Phe-His-Leu. Brain cathepsin B may have a role in the generation and degradation of angiotensin II in physiological conditions.

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Authors and Affiliations

  1. Institute of Biochemistry, Sevak str 5/1, 375044, Yervan, USSR

    Anahit Azaryan, Nina Barkhudaryan & Armen Galoyan

  2. Center for Neurochemistry Ward's Island, 10035, New York, New York

    Abel Lajtha

Authors
  1. Anahit Azaryan
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  2. Nina Barkhudaryan
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  3. Armen Galoyan
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  4. Abel Lajtha
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Special Issue dedicated to Dr. Eugene Kreps.

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Azaryan, A., Barkhudaryan, N., Galoyan, A. et al. Action of brain cathepsin B, cathepsin D, and high-molecular-weight aspartic proteinase on angiotensins I and II. Neurochem Res 10, 1525–1532 (1985). https://doi.org/10.1007/BF00988864

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