Title : Reversible change in thiol redox status of the insulin receptor alpha-subunit in intact cells.

Pub. Date : 1999 May 4

PMID : 10231542






2 Functional Relationships(s)
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Compound Name
Protein Name
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1 Short-term treatment of intact cells expressing large numbers of IR with GSH or NAC led to a rapid and reversible reduction of IR alpha-subunit disulfides, without affecting the receptor beta-subunit thiol reactivity. Sulfhydryl Compounds insulin receptor Homo sapiens
2 No difference in insulin binding was observed in GSH-treated cells; however, ligand-mediated increases in IR autophosphorylation, tyrosine phosphorylation of cellular substrates, and dual phosphorylation of the downstream target mitogen-activated protein kinase were inhibited at concentrations of GSH (10 mM or greater) that yielded a significant increase in IR alpha-subunit thiol reactivity. Sulfhydryl Compounds insulin receptor Homo sapiens