Document Detail

SPARC interacts with AMPK and regulates GLUT4 expression.
MedLine Citation:
PMID:  20460104     Owner:  NLM     Status:  MEDLINE    
AMP-activated protein kinase (AMPK) is a critical regulator of glucose metabolism. To elucidate the biochemical mechanisms by which AMPK regulates glucose and fat metabolism, we conducted a yeast two-hybrid screen to identify its interacting partners. A yeast two-hybrid system was used to screen a mouse embryo cDNA library for proteins able to bind mouse AMPK alpha 1. We also demonstrated an endogenous interaction between AMPK alpha 1 and its interacting partner by co-immunoprecipitation of the endogenous proteins using specific antibodies in HepG2 cells, and in rat kidney, liver, skeletal muscle, and fat tissue. We show that secreted protein acidic and rich in cysteine (SPARC) is an AMPK-interacting protein, and the two proteins enhance each other. AMPK activation increases SPARC expression, and knockdown of AMPK to inhibit endogenous AMPK expression reduces SPARC protein levels. On the other hand, SPARC siRNA reduces AICAR-stimulated AMPK phosphorylation. SPARC affects AMPK-mediated glucose metabolism through regulation of Glut4 expression in L6 myocytes. Our findings suggest that SPARC may be involved in regulating glucose metabolism via AMPK activation. These results provide a starting point for efforts to clarify the relationship between AMPK and SPARC, and deepen our understanding of their roles in fat and glucose metabolism.
Haiyan Song; Yuanyuan Guan; Liping Zhang; Kun Li; Chunli Dong
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-05-10
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  396     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2010 Jun 
Date Detail:
Created Date:  2010-06-14     Completed Date:  2010-07-13     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  961-6     Citation Subset:  IM    
Copyright Information:
(c) 2010 Elsevier Inc. All rights reserved.
Department of Endocrinology and Metabolism, The Second Affiliated Hospital of Harbin Medical University, Xuefu Road 246, Harbin 150080, China.
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MeSH Terms
AMP-Activated Protein Kinases / genetics,  metabolism*
COS Cells
Cell Line
Cercopithecus aethiops
Glucose / metabolism
Glucose Transporter Type 4 / biosynthesis*
Muscle Cells / metabolism
RNA, Small Interfering / genetics
Rats, Wistar
Two-Hybrid System Techniques
Reg. No./Substance:
0/Glucose Transporter Type 4; 0/RNA, Small Interfering; 0/Slc2a4 protein, mouse; 50-99-7/Glucose; EC Protein Kinases; EC alpha1 subunit, mouse

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