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Peptide processing in the central nervous system.

N Marks, A Suhar, M Benuck

    Advances in Biochemical Psychopharmacology
    |January 1, 1981
    PubMed
    Summary
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    Researchers purified a human pituitary thiol proteinase, identifying it as cathepsin-B-like. They also found distinct dipeptidyl carboxypeptidases in rat brain membranes, separate from angiotensin-converting enzyme (ACE).

    Area of Science:

    • Biochemistry
    • Enzymology
    • Neuroscience

    Background:

    • Proteolytic enzymes play crucial roles in biological processes.
    • Understanding enzyme specificity and function is key to deciphering cellular mechanisms.
    • Previous research has identified various proteases in the central nervous system, but their precise characterization remains ongoing.

    Purpose of the Study:

    • To purify and characterize a thiol proteinase from human pituitaries.
    • To investigate the presence and properties of enkephalinases and other peptidases in rat brain membranes.
    • To differentiate these enzymes from known peptidases like angiotensin-converting enzyme (ACE).

    Main Methods:

    • Purification of thiol proteinase using chromatography.
    • Enzyme activity assays with various protein and peptide substrates.

    Related Experiment Videos

  • Characterization of enzyme properties including pH optimum, substrate specificity, and inhibitor sensitivity.
  • DEAE-cellulose chromatography and affinity chromatography (IgG-Sepharose) for enzyme fractionation.
  • Testing enzyme activity with specific peptide substrates like Leu-Gly-Gly, Leu-Nap, and Ala-Ala-Nap.

    • Main Results:

    • A human pituitary thiol proteinase was purified ~400-fold, exhibiting properties consistent with a cathepsin-B-like enzyme.
    • This enzyme cleaved substrates including myelin basic protein, histones, beta-lipotropin, neurophysin, and Substance P.
    • Rat brain membranes contained multiple enkephalinases and dipeptidyl carboxypeptidases distinct from ACE.
    • Various aminopeptidase activities were also detected in the rat brain fractions.

    Conclusions:

    • The human pituitary enzyme represents a cathepsin-B-like thiol proteinase with broad substrate specificity.
    • Rat brain membranes possess diverse peptidases, including enkephalinases and dipeptidyl carboxypeptidases, which are biochemically distinct from ACE.
    • These findings contribute to the understanding of proteolytic enzyme activity in the human pituitary and rat brain.