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Am J Physiol Cell Physiol 275: C285-C292, 1998;
0363-6143/98 $5.00
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Vol. 275, Issue 1, C285-C292, July 1998

Ca2+ and protein kinase C activation of mucin granule exocytosis in permeabilized SPOC1 cells

C. E. Scott, Lubna H. Abdullah, and C. William Davis

Cystic Fibrosis/Pulmonary Research and Treatment Center and the Department of Physiology, University of North Carolina, Chapel Hill, North Carolina 27599-7248

Mucin secretion by airway goblet cells is under the control of apical P2Y2, phospholipase C-coupled purinergic receptors. In SPOC1 cells, the mobilization of intracellular Ca2+ by ionomycin or the activation of protein kinase C (PKC) by phorbol 12-myristate 13-acetate (PMA) stimulates mucin secretion in a fully additive fashion [L. H. Abdullah, J. D. Conway, J. A. Cohn, and C. W. Davis. Am. J. Physiol. 273 (Lung Cell. Mol. Physiol. 17): L201-L210, 1997]. This apparent independence between PKC and Ca2+ in the stimulation of mucin secretion was tested in streptolysin O-permeabilized SPOC1 cells. These cells were fully competent to secrete mucin when Ca2+ was elevated from 100 nM to 3.1 µM for 2 min following permeabilization; the Ca2+ EC50 was 2.29 ± 0.07 µM. Permeabilized SPOC1 cells were exposed to PMA or 4alpha -phorbol at Ca2+ activities ranging from 10 nM to 10 µM. PMA, but not 4alpha -phorbol, increased mucin release at all Ca2+ activities tested: at 10 nM Ca2+ mucin release was 2.1-fold greater than control and at 4.7 µM Ca2+ mucin release was maximal (3.6-fold increase). PMA stimulated 27% more mucin release at 4.7 µM than at 10 nM Ca2+. Hence, SPOC1 cells possess Ca2+-insensitive, PKC-dependent, and Ca2+-dependent PKC-potentiated pathways for mucin granule exocytosis.

lung; airways; mucus; goblet cells; cellular regulation


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