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Multicatalytic, high-Mr endopeptidase from postmortem human brain.

J R McDermott1, A M Gibson, A E Oakley

  • 1Medical Research Council, Neurochemical Pathology Unit, Newcastle General Hospital, England.

Journal of Neurochemistry
|May 1, 1991
PubMed
Summary
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This study purified a high molecular weight multicatalytic endopeptidase from human brain. The enzyme exhibits three distinct activities, cleaving neuropeptides and proteins, with specific bond preferences.

Area of Science:

  • Biochemistry
  • Neuroscience
  • Enzymology

Background:

  • Postmortem human cerebral cortex contains a high molecular weight (650K) multicatalytic endopeptidase.
  • This enzyme, similar to those in other tissues and species, comprises 24-31K subunits.

Purpose of the Study:

  • To purify and characterize the multicatalytic endopeptidase from human cerebral cortex.
  • To elucidate the enzyme's catalytic activities, substrate specificities, and bond cleavage patterns.

Main Methods:

  • Purification of the endopeptidase from postmortem human cerebral cortex.
  • Assay of enzyme activity using fluorogenic tripeptide substrates and natural neuropeptides.
  • Determination of bond specificity by analyzing degradation products of 15 naturally occurring peptide sequences.

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Main Results:

  • The purified enzyme demonstrated three distinct catalytic activities against substrates with hydrophobic (Phe), basic (Arg), and acidic (Glu) P1 residues.
  • Enzyme efficiently hydrolyzed neuropeptides (e.g., substance-P, bradykinin) and casein (proteinase activity).
  • Optimal hydrolysis occurred at P1 hydrophobic residues and small or hydrophobic P'1 residues, with specific cleavage of Glu-X and Arg-Arg bonds observed.

Conclusions:

  • The three catalytic activities identified using fluorogenic substrates are also expressed against natural oligopeptides.
  • This multicatalytic endopeptidase plays a significant role in neuropeptide and protein degradation in the human brain.