Identification of neuropeptide-degrading enzymes in the pancreas

H. Terashima, A. Okamoto, D. Menozzi, E. J. Goetzl, N. W. Bunnett

Research output: Contribution to journalArticlepeer-review


Neutral endopeptidase (NEP) and aminopeptidase M (APM) were identified in the pancreas by enzymatic assays and Western blotting. The NEP activity, assessed by the phosphoramidon- and dl-thiorphan-inhibitable degradation of glutaryl-Ala-Ala-Phe-4-methoxy-2-naphthylamine, was 28.8 pmol/h/μg of pancreatic membrane protein and 124 pmol/h/106 pancreatic acinar cells. The APM enzymatic activity, assessed by the actinonin- and amastatin-inhibitable degradation of Ala-4-methoxy-2-naphthylamine, was 633 pmol/h/μg pancreatic membrane protein and 17.4 nmol/h/106 pancreatic acinar cells. Proteins corresponding to NEP (95 kDa) and APM (140 kDa) were identified in membranes by Western blotting. Both NEP and APM on acinar cells may degrade neuropeptides and regulate their effects on exocrine secretion.

Original languageEnglish (US)
Pages (from-to)741-748
Number of pages8
Issue number4
StatePublished - 1992


  • Aminopeptidase M
  • Enkephalins
  • Neutral endopeptidase
  • Pancreatic acinar cells
  • Pancreatic secretion

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience


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