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Combination of insulinomimetic agents H2O2 and vanadate enhances insulin receptor mediated tyrosine phosphorylation of IRS-1 leading to IRS-1 association with the phosphatidylinositol 3-kinase.
J Cell Biochem 1995; 58(3):279-91JC

Abstract

To analyze the mechanism of action of the insulinomimetic agents H2O2, vanadate, and pervanadate (H2O2 and vanadate), CHO cells or CHO cells that overexpress wild-type or mutant insulin receptor and/or the insulin receptor substrate (IRS-1) were used. H2O2 or vanadate treatment alone had little or no effect on tyrosine phosphorylation of cellular proteins; however, pervanadate treatment dramatically enhanced tyrosine phosphorylation of a number of proteins including the insulin receptor and IRS-1. However, the insulin receptor and IRS-1 coimmunoprecipitate from insulin-treated but not from pervanadate-treated cells. Pervanadate-induced tyrosine phosphorylation of the insulin receptor led to an increase in insulin receptor tyrosine kinase activity toward IRS-1 in vivo and IRS-1 peptides in vitro equal to that induced by insulin treatment. Pervanadate-enhanced phosphorylation of IRS-1 led to a fifteenfold increase in IRS-1-associated phosphatidylinositol (PtdIns) 3-kinase activity. However, insulin receptor-associated PtdIns 3-kinase activity from pervanadate-treated cells was not detectable, while insulin receptor-associated PtdIns 3-kinase activity from insulin-treated cells was 20% of the IRS-1-associated activity. Thus, pervanadate but not H2O2 or vanadate alone under these conditions mimics many of insulin actions, but pervanadate treatment does not induce insulin receptor/IRS-1 association.

Authors+Show Affiliations

Department of Pharmacology, University of Missouri-Columbia, School of Medicine 65212, USA.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

7593251

Citation

Wilden, P A., and D Broadway. "Combination of Insulinomimetic Agents H2O2 and Vanadate Enhances Insulin Receptor Mediated Tyrosine Phosphorylation of IRS-1 Leading to IRS-1 Association With the Phosphatidylinositol 3-kinase." Journal of Cellular Biochemistry, vol. 58, no. 3, 1995, pp. 279-91.
Wilden PA, Broadway D. Combination of insulinomimetic agents H2O2 and vanadate enhances insulin receptor mediated tyrosine phosphorylation of IRS-1 leading to IRS-1 association with the phosphatidylinositol 3-kinase. J Cell Biochem. 1995;58(3):279-91.
Wilden, P. A., & Broadway, D. (1995). Combination of insulinomimetic agents H2O2 and vanadate enhances insulin receptor mediated tyrosine phosphorylation of IRS-1 leading to IRS-1 association with the phosphatidylinositol 3-kinase. Journal of Cellular Biochemistry, 58(3), pp. 279-91.
Wilden PA, Broadway D. Combination of Insulinomimetic Agents H2O2 and Vanadate Enhances Insulin Receptor Mediated Tyrosine Phosphorylation of IRS-1 Leading to IRS-1 Association With the Phosphatidylinositol 3-kinase. J Cell Biochem. 1995;58(3):279-91. PubMed PMID: 7593251.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Combination of insulinomimetic agents H2O2 and vanadate enhances insulin receptor mediated tyrosine phosphorylation of IRS-1 leading to IRS-1 association with the phosphatidylinositol 3-kinase. AU - Wilden,P A, AU - Broadway,D, PY - 1995/7/1/pubmed PY - 1995/7/1/medline PY - 1995/7/1/entrez SP - 279 EP - 91 JF - Journal of cellular biochemistry JO - J. Cell. Biochem. VL - 58 IS - 3 N2 - To analyze the mechanism of action of the insulinomimetic agents H2O2, vanadate, and pervanadate (H2O2 and vanadate), CHO cells or CHO cells that overexpress wild-type or mutant insulin receptor and/or the insulin receptor substrate (IRS-1) were used. H2O2 or vanadate treatment alone had little or no effect on tyrosine phosphorylation of cellular proteins; however, pervanadate treatment dramatically enhanced tyrosine phosphorylation of a number of proteins including the insulin receptor and IRS-1. However, the insulin receptor and IRS-1 coimmunoprecipitate from insulin-treated but not from pervanadate-treated cells. Pervanadate-induced tyrosine phosphorylation of the insulin receptor led to an increase in insulin receptor tyrosine kinase activity toward IRS-1 in vivo and IRS-1 peptides in vitro equal to that induced by insulin treatment. Pervanadate-enhanced phosphorylation of IRS-1 led to a fifteenfold increase in IRS-1-associated phosphatidylinositol (PtdIns) 3-kinase activity. However, insulin receptor-associated PtdIns 3-kinase activity from pervanadate-treated cells was not detectable, while insulin receptor-associated PtdIns 3-kinase activity from insulin-treated cells was 20% of the IRS-1-associated activity. Thus, pervanadate but not H2O2 or vanadate alone under these conditions mimics many of insulin actions, but pervanadate treatment does not induce insulin receptor/IRS-1 association. SN - 0730-2312 UR - https://www.unboundmedicine.com/medline/citation/7593251/Combination_of_insulinomimetic_agents_H2O2_and_vanadate_enhances_insulin_receptor_mediated_tyrosine_phosphorylation_of_IRS_1_leading_to_IRS_1_association_with_the_phosphatidylinositol_3_kinase_ L2 - https://doi.org/10.1002/jcb.240580303 DB - PRIME DP - Unbound Medicine ER -