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Regulation fo protein kinase C activity by various lipids

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Abstract

Protein kinase C has recently attracted considerable attention because of its importance in the control of cell division, cell differentiation, and signal transduction across the cell membrane. The activity of this enzyme is altered by several lipids such as diacylglycerol, free fatty acids, lipoxins, gangliosides, and sulfatides. These lipids may interact with protein kinase C either directly or through calcium ions and produce their regulatory effect (activation or inhibition) on the activities of the enzymes phosphorylated by this kinase. These processes widen our perspective of the regulation of intercellular and intracelluular communication.

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Abbreviations

(PK-C):

Protein kinase C

(cAMP-PK):

cAMP dependent protein kinase

(DAG):

diacylglycerol

(PtdSer):

phosphatidylserine

(InsP 3):

inositol 1,4,5-trisphosphate

(PtdIns 4,5-P2):

inositol 4,5 bisphosphate

(FFA):

free fatty acid

(MBP):

myelin basic protein

(ATP):

adenosine triphosphate

(GTP):

guanine triphosphate

(TPA):

12-tetradecanoylphorbol-13-acetate

(EGF):

epidermal growth factor

(PDGF):

platelet derived growth factor

(NeuNAc):

and N-acetylneuraminic acid

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Authors and Affiliations

  1. Department of Physiological Chemistry, The Ohio State University, 1645 Neil Ave., Rm. 214, 43210, Columbus, Ohio

    Akhlaq A. Farooqui & Lloyd A. Horrocks

  2. Department Pathology, and Neuroscience Program College of Medicine, The Ohio State University, 1645 Neil Ave., Rm. 214, 43210, Columbus, Ohio

    Allan J. Yates

  3. Division of Pharmacology, College of Pharmacy, The Ohio State University, 1645 Neil Ave., Rm. 214, 43210, Columbus, Ohio

    Tahira Farooqui

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  1. Akhlaq A. Farooqui
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Farooqui, A.A., Farooqui, T., Yates, A.J. et al. Regulation fo protein kinase C activity by various lipids. Neurochem Res 13, 499–511 (1988). https://doi.org/10.1007/BF00973288

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