Proinsulin C-peptide activates α-enolase: implications for C-peptide--cell membrane interaction

Journal of Biochemistry
Tatsuya IshiiKazuhiro Kimura

Abstract

Proinsulin C-peptide shows beneficial effects on microvascular complications of Type 1 diabetes. However, the possible occurrence of membrane C-peptide receptor(s) has not been elucidated. The aim of this study was to identify and characterize membrane proteins to which C-peptide binds. The enzyme α-enolase was co-immunoprecipitated with C-peptide after chemical cross-linking to HL-60 cell surface proteins and identified by mass spectrometry. Recombinant α-enolase activity was modulated by C-peptide, with a significant decrease in K(m) for 2-phosphoglycerate without affecting V(max). The enzyme modulation by C-peptide was abolished when C-terminal basic lysine residue (K434) of the enzyme was replaced by neutral alanine or acidic glutamate, but not with basic arginine. The enzyme modulation by C-peptide was reproduced with the C-peptide fragments containing glutamate corresponding to position 27 (E27) of the full-length C-peptide. Addition of a lysine analogue to the assay and A31 cell culture abrogated the enzyme modulation and MAP kinase activation by C-peptide, respectively. The results indicate that C-peptide has the capacity to activate α-enolase through a specific interaction between E27 of the peptide and K434 of the enz...Continue Reading

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Citations

Jun 7, 2013·Current Atherosclerosis Reports·Corinna Lebherz, Nikolaus Marx
Feb 1, 2013·International Journal of Peptides·Masayuki KomatsuKoichi Nishigaki
Dec 13, 2017·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Yanning LiWeigang Luo
Sep 25, 2014·American Journal of Physiology. Endocrinology and Metabolism·Gina L C YostenJohn Wahren
Jul 3, 2015·Physiology·Gina L C Yosten, Grant R Kolar
Oct 24, 2020·Physiological Research·D VejrazkovaB Bendlova

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