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Papers In Press, published online ahead of print February 7, 2005
Biochemistry, Boston University School of Medicine, Boston, MA 02118
Corresponding Author: ppilch{at}bu.edu
The presence of cell surface caveolin/caveolae has been postulated to influence the localization, expression levels and kinase activity of numerous receptors including the insulin receptor. However, there are conflicting data concerning the effects of caveolin on insulin receptor expression and function. To help clarify this issue, we created a gain of function situation by expressing caveolin at various levels in HEK293 cells where the endogenous level of caveolin is very low. We generated 4 permanent lines of this cell expressing amounts of caveolin-1 ranging from 10 to 40 times that of parental cells. The amount of caveolin in the HEK cells expressing the highest caveolin levels is comparable to that of adipocytes, cells that naturally express one of the highest levels of caveolin. We measured insulin receptor amount and insulin-dependent receptor autophosphorylation as well as IRS1 tyrosine phosphorylation as an index of insulin signaling. We found that the insulin receptor level was essentially the same in the parental and in all 4 derived cell lines. Likewise, we determined that insulin-dependent insulin receptor and IRS1 tyrosine phosphorylation was not significantly different in four cell lines representing parental, low, medium and high levels of caveolin-1 expression. We conclude that insulin receptor expression and ligand-dependent signaling is independent of caveolin expression.
J. Biol. Chem, 10.1074/jbc.M413891200
Submitted on December 9, 2004
Revised on February 7, 2005
Accepted on February 7, 2005
Dissociation of insulin receptor expression and signaling from caveolin-1 expression
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