|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5 Pt 1
|
|
pubmed:dateCreated |
1999-6-7
|
|
pubmed:abstractText |
The acute stimulation of glucose uptake by insulin in fat and muscle cells is primarily the result of translocation of facilitative glucose transporter 4 (GLUT-4) from an internal compartment to the plasma membrane. Here, we investigate the role of SNAP23 (a 23-kDa molecule resembling the 25-kDa synaptosome associated protein) in GLUT-4 translocation and glucose uptake in 3T3-L1 adipocytes. Microinjection of a polyclonal antibody directed to the carboxy terminus of SNAP23 inhibited GLUT-4 incorporation into the membrane in response to insulin, whereas microinjection of full-length recombinant SNAP23 enhanced the insulin effect. Introduction of recombinant SNAP23 into chemically permeabilized cells also enhanced insulin-stimulated glucose transport. These results indicate that SNAP23 is required for insulin-dependent, functional incorporation of GLUT-4 into the plasma membrane and that the carboxy terminus of the protein is essential for this process. SNAP23 is therefore likely to be a fusion catalyst along with syntaxin-4 and vesicle-associated membrane protein (VAMP)-2. Furthermore, the endogenous content of SNAP23 appears to be limiting for insulin-dependent GLUT-4 exposure at the cell surface. A measurable fraction of SNAP23 was sedimented with cytoskeletal elements when extracted with Triton X-100, unlike VAMP-2 and syntaxin-4, which were exclusively soluble in detergent. We hypothesize that SNAP23 and its interaction with the cytoskeleton may be targets for regulation of GLUT-4 traffic.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 4,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Qb-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Qc-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNAP23 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Slc2a4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Snap23 protein, mouse
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0002-9513
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
276
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
C1108-14
|
|
pubmed:dateRevised |
2011-11-17
|
|
pubmed:meshHeading |
pubmed-meshheading:10329959-3T3 Cells,
pubmed-meshheading:10329959-Adipocytes,
pubmed-meshheading:10329959-Animals,
pubmed-meshheading:10329959-Antibodies,
pubmed-meshheading:10329959-Carrier Proteins,
pubmed-meshheading:10329959-Cell Membrane,
pubmed-meshheading:10329959-Cytoskeleton,
pubmed-meshheading:10329959-Glucose,
pubmed-meshheading:10329959-Glucose Transporter Type 4,
pubmed-meshheading:10329959-Glutathione Transferase,
pubmed-meshheading:10329959-Insulin,
pubmed-meshheading:10329959-Kinetics,
pubmed-meshheading:10329959-Mice,
pubmed-meshheading:10329959-Microinjections,
pubmed-meshheading:10329959-Monosaccharide Transport Proteins,
pubmed-meshheading:10329959-Muscle Proteins,
pubmed-meshheading:10329959-Peptide Fragments,
pubmed-meshheading:10329959-Qb-SNARE Proteins,
pubmed-meshheading:10329959-Qc-SNARE Proteins,
pubmed-meshheading:10329959-Recombinant Fusion Proteins
|
|
pubmed:year |
1999
|
|
pubmed:articleTitle |
SNAP23 promotes insulin-dependent glucose uptake in 3T3-L1 adipocytes: possible interaction with cytoskeleton.
|
|
pubmed:affiliation |
Cell Biology Programme, Hospital for Sick Children, Toronto, Ontario M5G 1X8; and Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
