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Oligomerization and insulin interactions of proinsulin C-peptide: Threefold relationships to properties of insulin.

Abstract：

:Three principally different sites of action have been reported for proinsulin C-peptide, at surface-mediated, intracellular, and extracellular locations. Following up on the latter, we now find that (i) mass spectrometric analyses reveal the presence of the C-peptide monomer in apparent equilibrium with a low-yield set of oligomers in weakly acidic or basic aqueous solutions, even at low peptide concentrations (sub-muM). It further shows not only C-peptide to interact with insulin oligomers (known before), but also the other way around. (ii) Polyacrylamide gel electrophoresis of C-peptide shows detectable oligomers upon Western blotting. Formation of thioflavin T positive material was also detected. (iii) Cleavage patterns of analogues are compatible with C-peptide as a substrate of insulin degrading enzyme. Combined, the results demonstrate three links with insulin properties, in a manner reminiscent of amyloidogenic peptides and their chaperons in other systems. If so, peripheral C-peptide/insulin interactions, absolute amounts of both peptides and their ratios may be relevant to consider in diabetic and associated diseases.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Jörnvall H,Lindahl E,Astorga-Wells J,Lind J,Holmlund A,Melles E,Alvelius G,Nerelius C,Mäler L,Johansson J

doi

10.1016/j.bbrc.2009.12.125

subject

Has Abstract

pub_date

2010-01-15 00:00:00

pages

1561-6

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)02498-X

journal_volume

391

pub_type

杂志文章

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