Document Detail


Effects of contraction on localization of GLUT4 and v-SNARE isoforms in rat skeletal muscle.
MedLine Citation:
PMID:  19675279     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In skeletal muscle, contractions increase glucose uptake due to a translocation of GLUT4 glucose transporters from intracellular storage sites to the surface membrane. Vesicle-associated membrane proteins (VAMPs) are believed to play an important role in docking and fusion of the GLUT4 transporters at the surface membrane. However, knowledge about which VAMP isoforms colocalize with GLUT4 vesicles in mature skeletal muscle and whether they translocate during muscle contractions is incomplete. The aim of the present study was to further identify VAMP isoforms, which are associated with GLUT4 vesicles and examine which VAMP isoforms translocate to surface membranes in skeletal muscles undergoing contractions. VAMP2, VAMP3, VAMP5, and VAMP7 were enriched in immunoprecipitated GLUT4 vesicles. In response to 20 min of in situ contractions, there was a redistribution of GLUT4 (+64 +/- 13%), transferrin receptor (TfR; +75 +/- 22%), and insulin-regulated aminopeptidase (IRAP; +70 +/- 13%) to fractions enriched in heavy membranes away from low-density membranes (-32 +/- 7%; -18 +/- 12%; -33 +/- 9%; respectively), when compared with the resting contralateral muscle. Similarly, there was a redistribution of VAMP2 (+240 +/- 40%), VAMP5 (+79 +/- 9%), and VAMP7 (+79 +/- 29%), but not VAMP3, to fractions enriched in heavy membranes away from low-density membranes (-49 +/- 10%, -54 +/- 9%, -14 +/- 11%, respectively) in contracted vs. resting muscle. In summary, VAMP2, VAMP3, VAMP5, and VAMP7 coimmunoprecipitate with intracellular GLUT4 vesicles in muscle, and VAMP2, VAMP5, VAMP7, but not VAMP3, translocate to the cell surface membranes similar to GLUT4, TfR, and IRAP in response to muscle contractions. These findings suggest that VAMP2, VAMP5, and VAMP7 may be involved in translocation of GLUT4 during muscle contractions.
Authors:
Adam J Rose; Jacob Jeppesen; Bente Kiens; Erik A Richter
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-08-12
Journal Detail:
Title:  American journal of physiology. Regulatory, integrative and comparative physiology     Volume:  297     ISSN:  1522-1490     ISO Abbreviation:  Am. J. Physiol. Regul. Integr. Comp. Physiol.     Publication Date:  2009 Nov 
Date Detail:
Created Date:  2009-11-02     Completed Date:  2009-12-03     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100901230     Medline TA:  Am J Physiol Regul Integr Comp Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  R1228-37     Citation Subset:  IM    
Affiliation:
Molecular Physiology Group, Department of Exercise and Sport Sciences, Copenhagen, Denmark. erichter@ifi.ku.dk
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MeSH Terms
Descriptor/Qualifier:
Animals
Blood Glucose / metabolism
Cystinyl Aminopeptidase / metabolism
Cytoplasmic Vesicles / metabolism
Glucose Transporter Type 4 / metabolism*
Hypoglycemic Agents / pharmacology
Insulin / pharmacology
Male
Models, Animal
Muscle Contraction / physiology*
Muscle, Skeletal / drug effects,  metabolism*
Protein Isoforms / metabolism
R-SNARE Proteins / metabolism
Rats
Rats, Wistar
Receptors, Transferrin / metabolism
SNARE Proteins / metabolism*
Vesicle-Associated Membrane Protein 2 / metabolism
Vesicle-Associated Membrane Protein 3 / metabolism
Chemical
Reg. No./Substance:
0/Blood Glucose; 0/Glucose Transporter Type 4; 0/Hypoglycemic Agents; 0/Protein Isoforms; 0/R-SNARE Proteins; 0/Receptors, Transferrin; 0/SNARE Proteins; 0/Slc2a4 protein, rat; 0/Sybl1 protein, rat; 0/VAMP5 protein, rat; 0/Vesicle-Associated Membrane Protein 2; 0/Vesicle-Associated Membrane Protein 3; 11061-68-0/Insulin; EC 3.4.11.3/Cystinyl Aminopeptidase; EC 3.4.11.3/leucyl-cystinyl aminopeptidase

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