Effects of metformin on insulin receptor tyrosine kinase activity in rat adipocytes
Autor: | D. B. Jacobs, Gary R Hayes, Dean H. Lockwood, Joseph A. Truglia |
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Rok vydání: | 1986 |
Předmět: |
Blood Glucose
Male medicine.medical_specialty medicine.drug_class Endocrinology Diabetes and Metabolism medicine.medical_treatment Internal medicine Insulin receptor substrate Internal Medicine medicine Animals Phosphorylation Hexose transport Hexoses biology Biguanide Insulin Rats Inbred Strains Protein-Tyrosine Kinases Metformin Receptor Insulin Rats Insulin receptor Endocrinology Adipose Tissue Insulin receptor binding biology.protein Tyrosine kinase medicine.drug |
Zdroj: | Diabetologia. 29:798-801 |
ISSN: | 1432-0428 0012-186X |
DOI: | 10.1007/bf00873219 |
Popis: | The cellular mechanism(s) by which the biguanide, metformin, exerts its antihyperglycaemic effect was investigated. Rat adipocytes were either treated acutely (2 h) or maintained in a biochemically defined medium (20 h) in the presence or absence of metformin (1 X 10(-4) mol/l). Exposure to the drug resulted in a significant enhancement (p less than 0.01) of hexose transport in both the absence (basal) and presence of insulin. Stimulation of transport was not explained by the increase in the basal state alone, since the incremental response to maximally effective concentrations of insulin was significantly enhanced p less than 0.025. Insulin-receptor tyrosine kinase activity was examined under the same experimental conditions. Activity of the kinase was unaltered as evaluated by phosphorylation of an artificial substrate and by phosphorylation of the receptor in situ. Furthermore, in this investigation neither insulin receptor number nor affinity was changed in adipose tissue treated with metformin. These studies indicate that metformin potentiates the effect of insulin on glucose transport at a site(s) beyond insulin receptor binding and phosphorylation. |
Databáze: | OpenAIRE |
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