Glyceraldehyde-3-phosphate dehydrogenase interacts with phosphorylated Akt resulting from increased blood glucose in rat cardiac muscle

Baba, Takeshi; Kobayashi, Hiroyuki; Kawasaki, Hiroaki; Mineki, Reiko; Naito, Hisashi; Ohmori, Daijiro

doi:10.1016/j.febslet.2010.05.015

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Volume 584, Issue 13 , Pages 2796-2800, 2 July 2010

Glyceraldehyde-3-phosphate dehydrogenase interacts with phosphorylated Akt resulting from increased blood glucose in rat cardiac muscle

Edited by Gianni Cesareni

Takeshi Baba
- Department of Chemistry, Faculty of Medicine, Juntendo University, 1-1 Hiragagakuendai, Inzai-shi, Chiba 270-1695, Japan
- Corresponding author. Fax: +81 476 98 1011.
Hiroyuki Kobayashi
- Department of General Medicine, Mito Medical Center, University of Tsukuba, 3-2-7 Miya-machi, Mito-shi, Ibaraki 310-0015, Japan
Hiroaki Kawasaki
- The Institute for Environmental and Gender-specific Medicine, Juntendo University, 2-1-1 Tomioka, Urayasu-shi, Chiba 279-0021, Japan
Reiko Mineki
- Department of Biochemistry, Central Laboratory of Medical Science, Faculty of Medicine, Juntendo University, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan
Hisashi Naito
- Department of Exercise Physiology, School of Health and Sports Science, Juntendo University, 1-1 Hiragagakuendai, Inzai-shi, Chiba 270-1695, Japan
Daijiro Ohmori
- Department of Chemistry, Faculty of Medicine, Juntendo University, 1-1 Hiragagakuendai, Inzai-shi, Chiba 270-1695, Japan

Received 24 March 2010; received in revised form 23 April 2010; accepted 3 May 2010. published online 17 May 2010.

Abstract

Here we describe the interaction of phosphorylated ∼40kDa protein with phosphorylated Akt which is a serine/threonine kinase resulting from increased blood glucose in rat cardiac muscle. Mass spectrometry analysis revealed that this protein was glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Furthermore, increase in Akt and GAPDH phosporylation and induction of their association were both observed after insulin stimulation in the H9c2 cell line derived from embryonic rat ventricle. Moreover, the activation of GAPDH was upregulated when the GAPDH phosphorylation was increased. Our data suggest that GAPDH phosphorylation and association with Akt by insulin treatment have some bearing on the enhancement of GAPDH activity.

Structured summary

MINT-7891324, MINT-7891304, MINT-7891314: GAPDH (uniprotkb:P04797) physically interacts (MI:0915) with Akt (uniprotkb:P47196) by anti bait coimmunoprecipitation (MI:0006)

Keywords: Insulin, Akt, Glyceraldehyde-3-phosphate dehydrogenase, Cardiac muscle

Abbreviations: EDL, extensor digitorum longus, IP, immunoprecipitate, MALDI-TOF, matrix-assisted laser desorption/ionization time-of-flight, PVDF, polyvinylidene difluoride, GAPDH, glyceraldehyde-3-phosphate dehydrogenase, PDK, phosphoinositide-dependent protein kinase