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Titolo:
BREFELDIN-A INHIBITS INSULIN-INDUCED GLUCOSE-TRANSPORT STIMULATION AND GLUT4 RECRUITMENT IN RAT ADIPOCYTES
Autore:
LACHAAL M; MORONSKI C; LIU HZ; JUNG CY;
Indirizzi:
VET ADM MED CTR,BIOPHYS LAB BUFFALO NY 14215 SUNY BUFFALO,DEPT BIOPHYS SCI BUFFALO NY 14215
Titolo Testata:
The Journal of biological chemistry
fascicolo: 38, volume: 269, anno: 1994,
pagine: 23689 - 23693
SICI:
0021-9258(1994)269:38<23689:BIIGSA>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-FACTOR; CELL-SURFACE; RECEPTOR INTERNALIZATION; ORGANELLE STRUCTURE; PLASMA-MEMBRANE; OKADAIC ACID; BETA-COP; TRANSLOCATION; ENDOSOMES; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
M. Lachaal et al., "BREFELDIN-A INHIBITS INSULIN-INDUCED GLUCOSE-TRANSPORT STIMULATION AND GLUT4 RECRUITMENT IN RAT ADIPOCYTES", The Journal of biological chemistry, 269(38), 1994, pp. 23689-23693

Abstract

GLUT4, the major insulin-responsive glucose transporter isoform in rat adipocytes, rapidly recycles between an intracellular pool and the plasma membrane in the basal and insulin-stimulated states. To gain insight into the route of this GLUT4 recycling, we studied the effects ofbrefeldin A (BFA) on glucose transport and glucose transporter subcellular distribution in rat adipocytes in the absence and in the presence of insulin. 3-O-Methyl-D-glucose equilibrium exchange measurements revealed that BFA inhibits insulin-stimulated glucose transport by as much as 80%, whereas the inactive BFA analog, B36, was without effect. The inhibition was reversible and was a saturable function of BFA concentration with an apparent K-i of less than 1 mu M. In the absence of insulin, on the other hand, BFA caused a slight (up to 2-fold) increase in glucose transport. Subcellular fractionation and semiquantitativeimmunoblotting analysis revealed that BFA inhibits insulin-induced redistribution of GLUT4 from microsomes to the plasma membranes, with a dose dependence similar to that for glucose transport inhibition. BFA also caused a slight increase in the plasma membrane GLUT4 level in the absence of insulin. BFA did not affect the subcellular distribution of GLUT1 in these experiments. These findings strongly suggest that GLUT4 recycling in rat adipocytes involves a BFA-sensitive, coat protein-mediated, membrane budding step, which is distinct between the constitutive and the insulin induced pathways.

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Documento generato il 03/04/20 alle ore 11:11:56