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Implication of acyl chain of diacylglycerols in activation of different isoforms of protein kinase C

Université de Bourgogne, UPRES Lipides et Nutrition EA 2422, Faculté des Sciences, F-21000 Dijon, France; and
^* Laboratoire de Pharmacologie Moléculaire, Faculté de Pharmacie, Université de Rennes I, France

¹Correspondence: Université de Bourgogne, UPRES Lipides et Nutrition EA 2422, Faculté des Sciences, 6 Blvd. Gabriel, F-21000 Dijon, France. E-mail: naim.khan{at}u-bourgogne.fr

We synthesized diacylglycerols (DAGs) containing -6 or -3 polyunsaturated fatty acids [i.e., 1-stearoyl-2-arachidonoyl-sn-glycerol (SAG), 1-stearoyl-2-docosahexaenoyl-sn-glycerol (SDG), and 1-stearoyl-2-eicosapentaenoyl-sn-glycerol (SEG)] and assessed their efficiency on activation of conventional (, ßI, ) and novel (, ) protein kinase C (PKC). SAG exerted significantly higher stimulatory effects than SDG and SEG on activation of PKC and PKC. Activation of PKCßI by SEG and SDG was higher than that by SAG. Activation of PKC did not differ significantly among DAG molecular species. Addition of SAG to assays containing SEG and SDG exerted additive effects on activation of and , but not on ßI and , isoforms of PKC. SDG- and SEG-induced activation of PKC was significantly curtailed by the addition of SAG. Three DAG species significantly curtailed the PMA-induced activation of ßI, , and , but not of and , isoforms of PKC. Our study demonstrates for the first time that in vitro activation of different PKC isoenzymes vary in response to different DAG species, and one can envisage that this differential regulation may be responsible for their in vivo effects on target organs.—Madani, S., Hichami, A., Legrand, A., Belleville, J., Khan, N. A. Implication of acyl chain of diacylglycerols in activation of different isoforms of protein kinase C.

Key Words: DAG • -3/-6 fatty acids • PKC isoenzymes

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