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Isoproterenol stimulates phosphorylation of the insulin-regulatable glucose transporter in rat adipocytes

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
; ;  [1]
  1. Washington Univ. School of Medicine, St. Louis, MO (USA)

The authors have examined the acute effect of insulin and isoproterenol on the phosphorylation state of the insulin-regulatable glucose transporter (IRGT) in rat adipocytes. The IRGT was immunoprecipitated from either detergent-solubilized whole-cell homogenates or subcellular fraction of {sup 32}P-labeled fat cells and subjected to sodium dodecyl sulfate/polyarcylamide gel electrophoresis. The {sup 32}P-labeled IRGT was detected by autoradiography as a species of apparent M{sub r} 46,000. Insulin stimulated translocation of the IRGT from low-density microsomes to the plasma membrane but did not affect phosphorylation of the transporter in either fraction. Isoproterenol inhibited insulin-stimulated glucose transport by 40% but was without effect on the subcellar distribution of the transporter in either the presence or absence of insulin. Isoproterenol stimulated phosphorylation of the IRGT 2-fold. Incubating cells with dibutyryl-cAMP and 8-bromo-cAMP also stimulated phosphorylation 2-fold, and the transporter was phosphorylated in vitro when IRGT-enriched vesicles were incubated with cAMP-dependent protein kinase and ({gamma}-{sup 32}P)ATP. These results suggest that isoproterenol stimulates phosphorylation of the IRGT via a cAMP-dependent pathway and that phosphorylation of the transporter may modulate its ability to transport glucose.

OSTI ID:
6906576
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 86:21; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English