Insulin secretory granule biogenesis and the proinsulin-processing endopeptidases

Diabetologia. 1994 Sep;37 Suppl 2:S48-56. doi: 10.1007/BF00400826.


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.

Publication types

  • Biography
  • Historical Article
  • Portrait
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Australia
  • Awards and Prizes*
  • Cytoplasmic Granules / physiology*
  • Cytoplasmic Granules / ultrastructure
  • Diabetes Mellitus* / history
  • Endopeptidases / metabolism*
  • Europe
  • History, 20th Century
  • Humans
  • Insulin / biosynthesis*
  • Islets of Langerhans / physiology*
  • Islets of Langerhans / ultrastructure
  • Proinsulin / chemistry
  • Proinsulin / metabolism*
  • Protein Processing, Post-Translational*
  • Societies, Medical
  • Substrate Specificity
  • United Kingdom


  • Insulin
  • Proinsulin
  • Endopeptidases
  • proinsulin endopeptidase I
  • proinsulin endopeptidase II

Personal name as subject

  • J C Jutton