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Am J Physiol Gastrointest Liver Physiol 276: G993-G1004, 1999;
0193-1857/99 $5.00
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Vol. 276, Issue 4, G993-G1004, April 1999

1,25-Dihydroxyvitamin D3 and TPA activate phospholipase D in Caco-2 cells: role of PKC-alpha

Sharad Khare, Marc Bissonnette, Beth Scaglione-Sewell, Ramesh K. Wali, Michael D. Sitrin, and Thomas A. Brasitus

Department of Medicine, University of Chicago, Chicago, Illinois 60637

1,25-Dihydroxyvitamin D3 [1,25(OH)2D3] and 12-O-tetradecanoylphorbol 13-acetate (TPA) both activated phospholipase D (PLD) in Caco-2 cells. GF-109203x, an inhibitor of protein kinase C (PKC) isoforms, inhibited this activation by both of these agonists. 1,25(OH)2D3 activated PKC-alpha , but not PKC-beta 1, -beta II, -delta , or -zeta , whereas TPA activated PKC-alpha , -beta 1, and -delta . Chronic treatment with TPA (1 µM, 24 h) significantly reduced the expression of PKC-alpha , -beta I, and -delta and markedly reduced the ability of 1,25(OH)2D3 or TPA to acutely stimulate PLD. Removal of Ca2+ from the medium, as well as preincubation of cells with Gö-6976, an inhibitor of Ca2+-dependent PKC isoforms, significantly reduced the stimulation of PLD by 1,25(OH)2D3 or TPA. Treatment with 12-deoxyphorbol-13-phenylacetate-20-acetate, which specifically activates PKC-beta I and -beta II, however, failed to stimulate PLD. In addition, the activation of PLD by 1,25(OH)2D3 or TPA was markedly reduced or accentuated in stably transfected cells with inhibited or amplified PKC-alpha expression, respectively. Taken together, these observations indicate that PKC-alpha is intimately involved in the stimulation of PLD in Caco-2 cells by 1,25(OH)2D3 or TPA.

calcitriol; phorbol esters; intracellular calcium; phospholipases; protein kinase C isoforms


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