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PMID: 7821740 Published · ppublish English Biography Historical Article Journal Article Portrait Research Support, Non-U.S. Gov't Review

Insulin secretory granule biogenesis and the proinsulin-processing endopeptidases.

Diabetologia ·Vol. 37 Suppl 2 ·1994-09-00 ·Pages S48-56

Hutton JC

Abstract

The insulin storage granule of the pancreatic beta cell is assembled within the trans Golgi network from around 50 or so gene products many of which are synthesized coordinately with the major component, proinsulin. An important contribution to our understanding of the regulation of this process has come from studies of the post-translational processing of proinsulin and of other proteins which are stored in the granule, particularly the processing enzymes themselves. The present review focusses on recent insights into the molecular nature of the processing machinery, and the granule Ca(2+)-dependent subtilisin-related endopeptidases which catalyse the initial rate-limiting step in the enzymic conversion of proinsulin.

MeSH Terms
Amino Acid Sequence Animals Australia Awards and Prizes Cytoplasmic Granules/physiology,ultrastructure Diabetes Mellitus/history Endopeptidases/metabolism Europe History, 20th Century Humans Insulin/biosynthesis Islets of Langerhans/physiology,ultrastructure Proinsulin/chemistry,metabolism Protein Processing, Post-Translational Societies, Medical Substrate Specificity United Kingdom
Chemicals
Insulin Proinsulin Endopeptidases proinsulin endopeptidase I proinsulin endopeptidase II
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Hutton J C
Department of Clinical Biochemistry, Addenbrooke's Hospital, Cambridge, UK.
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Article Info
Journal
Diabetologia
Abbr.
Diabetologia
ISSN
0012-186X
DOI
10.1007/BF00400826
Published
1994-09-00
Pages
S48-56
Language
English
Region
Germany
NLM ID
0006777
Subset
IM
Grants
Wellcome Trust · United Kingdom
External Links
PubMed source DOI: 10.1007/BF00400826 View journal details
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