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Proinsulin C-peptide activates α-enolase : implications for C-peptide-cell membrane interaction
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 | α-enolase | ENO1 | MAP kinase | plasminogen |
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: http://jb.oxfordjournals.org/content/152/1/53 |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/52691 |
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)
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Submitter: 木村 和弘
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