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Structural analogies between protein kinase C activators.

R Brasseur, V Cabiaux, P Huart

    Biochemical and Biophysical Research Communications
    |March 29, 1985
    PubMed
    Summary
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    Specific structural features of diacylglycerols and phorbol esters are crucial for activating protein kinase C. Understanding these conformations aids in designing tumor promoter inhibitors and predicting new promoters.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Pharmacology

    Background:

    • Protein kinase C (PKC) activation is modulated by phorbol esters and diacylglycerols.
    • Specific structural requirements for PKC activation by these compounds are not fully understood.

    Purpose of the Study:

    • To analyze the conformation of potent and non-potent diacylglycerols and phorbol esters.
    • To identify key structural parameters responsible for protein kinase C activation.

    Main Methods:

    • Conformational analysis of diacylglycerols and phorbol esters.
    • Structure-activity relationship assessment for enzyme activation.

    Main Results:

    • A specific orientation of the CH2OH group at C3 of 1,2 diolein mirrors that at C-20 of 4 beta phorbol didecanoate.

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  • This specific conformation is critical for potent protein kinase C activation.

    • Conclusions:

    • Conformational analysis provides a rational approach to understanding PKC activation.
    • This strategy can guide the design of specific inhibitors for tumor promoters.
    • The approach may aid in predicting the structure of novel tumor promoters.