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Regulated secretory proteins in the exocrine pancreas aggregate under conditions that mimic the trans-Golgi network.

Abstract：

:Fifteen pancreatic secretory proteins, including seven serine-endoproteinases (isoenzyme forms of trypsinogen, chymotrypsinogen and proelastase), four metallo-exoproteinases (isoenzymic forms of procarboxypeptidase A and procarboxypeptidase B), amylase, lipase, and two forms of carboxyl ester lipase were observed to aggregate under conditions of acidic pH (5.5) and calcium that mimic the trans-Golgi network. Subsequent neutralization of the pH resulted in disruption of protein aggregates and solubilization of pancreatic (pro)enzymes. In the absence of secretory granule membranes, granule contents display an "intrinsic" property for reversible, pH-dependent aggregation under conditions of mild acidification.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Freedman SD,Scheele GA

doi

10.1006/bbrc.1993.2577

subject

Has Abstract

pub_date

1993-12-15 00:00:00

pages

992-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)72577-5

journal_volume

197

pub_type

杂志文章

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