期刊
FEBS LETTERS
卷 584, 期 13, 页码 2796-2800出版社
WILEY
DOI: 10.1016/j.febslet.2010.05.015
关键词
Insulin; Akt; Glyceraldehyde-3-phosphate dehydrogenase; Cardiac muscle
资金
- JSPS [20500628]
- Grants-in-Aid for Scientific Research [20500628] Funding Source: KAKEN
Here we describe the interaction of phosphorylated similar to 40 kDa 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.
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