HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine >
Peer-reviewed Journal Articles, etc >

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

Files in This Item:
JB152-1_53-62.pdf791.86 kBPDFView/Open
Please use this identifier to cite or link to this item:

Title: Proinsulin C-peptide activates α-enolase : implications for C-peptide-cell membrane interaction
Authors: Ishii, Tatsuya Browse this author
Fukano, Keigo Browse this author
Shimada, Kohei Browse this author
Kamikawa, Akihiro Browse this author
Okamatsu-Ogura, Yuko Browse this author →KAKEN DB
Terao, Akira Browse this author →KAKEN DB
Yoshida, Toshihide Browse this author
Saito, Masayuki Browse this author
Kimura, Kazuhiro Browse this author →KAKEN DB
Keywords: C-peptide
MAP kinase
Issue Date: Jul-2012
Publisher: Oxford University Press
Journal Title: The Journal of Biochemistry
Volume: 152
Issue: 1
Start Page: 53
End Page: 62
Publisher DOI: 10.1093/jb/mvs052
PMID: 22577163
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 Km for 2-phosphoglycerate without affecting Vmax. 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 via a specific interaction between E27 of the peptide and K434 of the enzyme. Since α-enolase plays a role as a cell surface receptor for plasminogen, it may conceivably also serve as a receptor for C-peptide in vivo.
Rights: This is a pre-copy-editing, author-produced PDF of an article accepted for publication in The Journal of Biochemistry following peer review. The definitive publisher-authenticated version, J Biochem (2012) 152 (1): 53-62 is available online at:
Type: article (author version)
Appears in Collections:獣医学院・獣医学研究院 (Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 木村 和弘

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 - Hokkaido University