Identification of neuropeptide-degrading enzymes in the pancreas

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

doi:10.1016/0196-9781(92)90181-2

Identification of neuropeptide-degrading enzymes in the pancreas

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

Molecular Pathobiology

Research output: Contribution to journal › Article › peer-review

Abstract

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 language	English (US)
Pages (from-to)	741-748
Number of pages	8
Journal	Peptides
Volume	13
Issue number	4
DOIs	https://doi.org/10.1016/0196-9781(92)90181-2
State	Published - 1992

Keywords

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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10.1016/0196-9781(92)90181-2

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title = "Identification of neuropeptide-degrading enzymes in the pancreas",

abstract = "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.",

keywords = "Aminopeptidase M, Enkephalins, Neutral endopeptidase, Pancreatic acinar cells, Pancreatic secretion",

author = "H. Terashima and A. Okamoto and D. Menozzi and Goetzl, {E. J.} and Bunnett, {N. W.}",

year = "1992",

doi = "10.1016/0196-9781(92)90181-2",

language = "English (US)",

volume = "13",

pages = "741--748",

journal = "Peptides",

issn = "0196-9781",

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T1 - Identification of neuropeptide-degrading enzymes in the pancreas

AU - Terashima, H.

AU - Okamoto, A.

AU - Menozzi, D.

AU - Goetzl, E. J.

AU - Bunnett, N. W.

PY - 1992

Y1 - 1992

N2 - 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.

AB - 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.

KW - Aminopeptidase M

KW - Enkephalins

KW - Neutral endopeptidase

KW - Pancreatic acinar cells

KW - Pancreatic secretion

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AN - SCOPUS:0026488480

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JO - Peptides

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ER -

Identification of neuropeptide-degrading enzymes in the pancreas

Abstract

Keywords

ASJC Scopus subject areas

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