Delle Bovi, Richard J.; Kim, JiHyun; Suresh, Pavana; London, Erwin; Miller, W. Todd published the artcile< Sterol structure dependence of insulin receptor and insulin-like growth factor 1 receptor activation>, Synthetic Route of 434-16-2, the main research area is insulin receptor IGF1R autophosphorylation cholesterol sterol plasma membrane; Autophosphorylation; Cholesterol; Receptor tyrosine kinase.
The plasma membrane is a dynamic environment with a complex composition of lipids, proteins, and cholesterol. Areas enriched in cholesterol and sphingolipids are believed to form lipid rafts, domains of highly ordered lipids. The unique phys. properties of these domains have been proposed to influence many cellular processes. Here, we demonstrate that the activation of insulin receptor (IR) and insulin-like growth factor 1 receptor (IGF1R) depends critically on the structures of membrane sterols. IR and IGF1R autophosphorylation in vivo was inhibited by cholesterol depletion, and autophosphorylation was restored by the replacement with exogenous cholesterol. We next screened a variety of sterols for effects on IR activation. The ability of sterols to support IR autophosphorylation was strongly correlated to the propensity of the sterols to form ordered domains. IR autophosphorylation was fully restored by the incorporation of ergosterol, dihydrocholesterol, 7-dehydrocholesterol, lathosterol, desmosterol, and allocholesterol, partially restored by epicholesterol, and not restored by lanosterol, coprostanol, and 4-cholesten-3-one. These data support the hypothesis that the ability to form ordered domains is sufficient for a sterol to support ligand-induced activation of IR and IGF1R in intact mammalian cells.
Biochimica et Biophysica Acta, Biomembranes published new progress about Cell membrane. 434-16-2 belongs to class alcohols-buliding-blocks, and the molecular formula is C27H44O, Synthetic Route of 434-16-2.
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