Article

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

Department of Chemistry, Faculty of Medicine, Juntendo University, Inzai-shi, Chiba, Japan.
FEBS letters (impact factor: 3.54). 07/2010; 584(13):2796-800. DOI:10.1016/j.febslet.2010.05.015 pp.2796-800
Source: PubMed

ABSTRACT Here we describe the interaction of phosphorylated approximately 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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Keywords

Akt
 
GAPDH
 
GAPDH activity
 
GAPDH phosphorylation
 
GAPDH phosporylation
 
H9c2 cell line
 
insulin stimulation
 
insulin treatment
 
Mass spectrometry analysis
 
phosphorylated
 
phosphorylated Akt
 
rat cardiac muscle
 
serine/threonine kinase
 

Takeshi Baba