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.

authors

Patzelt C,Labrecque AD,Duguid JR,Carroll RJ,Keim PS,Heinrikson RL,Steiner DF

doi

10.1073/pnas.75.3.1260

subject

Has Abstract

pub_date

1978-03-01 00:00:00

pages

1260-4

issue

3

eissn

0027-8424

issn

1091-6490

journal_volume

75

pub_type

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