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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Specific and direct binding of protein kinase C to an immobilized tamoxifen analogue.

We have previously demonstrated that tamoxifen and related triphenylethylene compounds are potent inhibitors of protein kinase C ( PKC). The present study demonstrates that PKC binds specifically and reversibly to the antiestrogen N-didesmethyltamoxifen when the drug is coupled to CNBr-activated agarose through its primary amine, in the absence of lipid and other cofactors of the enzyme. PKC did not bind to 4-hydroxytamoxifen, which had been immobilized on epoxy-activated Sepharose through its hydroxyl moiety. This shows that the binding of PKC to immobilized N-didesmethyltamoxifen was not merely due to hydrophobic interactions, since N-didesmethyltamoxifen and 4-hydroxytamoxifen have nearly identical hydrophobicities. These results demonstrate that PKC has specific triphenylethylene-binding sites, which may mediate the inhibition of PKC activity by these antiestrogens.[1]

References

  1. Specific and direct binding of protein kinase C to an immobilized tamoxifen analogue. O'Brian, C.A., Housey, G.M., Weinstein, I.B. Cancer Res. (1988) [Pubmed]
 
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