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Detection and kinetic behavior of preproinsulin in pancreatic islets.

Abstract
Newly synthesized rat islet proteins have been analyzed by polyacrylamide slab gel electrophoresis and fluorography. A minor component having an apparent molecular weight of 11,100 was identified as preproinsulin by the sensitivity of its synthesis to glucose, the pattern of NH2-terminal leucine residues, and the rapidity of its appearance and disappearance during incubation of islets or islet cell tumors. A small amount of labeled peptide material which may represent the excised NH2-terminal extension of preproinsulin or its fragment was also detected. The kinetics of formation and processing of the preproinsulin fraction were complex, consisting of a rapidly turning over component having a half-life of about 1 min and a slower minor fraction that may have bypassed the normal cleavage process. The electrophoretic resolution of the preproinsulin and proinsulin fractions into two bands each is consistent with the presence of two closely related gene products in rat islets rather than intermediate stages in the processing of these peptides.
AuthorsC Patzelt, A D Labrecque, J R Duguid, R J Carroll, P S Keim, R L Heinrikson, D F Steiner
JournalProceedings of the National Academy of Sciences of the United States of America (Proc Natl Acad Sci U S A) Vol. 75 Issue 3 Pg. 1260-4 (Mar 1978) ISSN: 0027-8424 [Print] United States
PMID206890 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Insulin
  • Peptide Fragments
  • Protein Precursors
  • preproinsulin
  • Proinsulin
  • Glucose
Topics
  • Adenoma, Islet Cell (metabolism)
  • Amino Acid Sequence
  • Animals
  • Glucose (pharmacology)
  • Insulin
  • Islets of Langerhans (metabolism)
  • Kinetics
  • Neoplasms, Experimental (metabolism)
  • Pancreatic Neoplasms (metabolism)
  • Peptide Fragments
  • Proinsulin (biosynthesis)
  • Protein Precursors (metabolism)
  • Rats

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