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Am J Physiol Cell Physiol 281: C514-C523, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 2, C514-C523, August 2001

Negative regulation of ligand-initiated Ca2+ uptake by PKC-beta II in differentiated HL60 cells

Helen M. Korchak1, Barbara E. Corkey2, Gordon C. Yaney2, and Laurie E. Kilpatrick1

1 Departments of Pediatrics and Biochemistry/Biophysics, University of Pennsylvania School of Medicine, The Joseph Stokes Jr. Research Institute of the Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104; and 2 Obesity Research Unit, Department of Medicine, Boston University School of Medicine, Boston, Massachusetts 02118

In phagocytic cells, fMet-Leu-Phe triggers phosphoinositide remodeling, activation of protein kinase C (PKC), release of intracellular Ca2+ and uptake of extracellular Ca2+. Uptake of extracellular Ca2+ can be triggered by store-operated Ca2+ channels (SOCC) and via a receptor-operated nonselective cation channel(s). In neutrophilic HL60 cells, the PKC activator phorbol myristate acetate (PMA) activates multiple PKC isotypes, PKC-alpha , PKC-beta , and PKC-delta , and inhibits ligand-initiated mobilization of intracellular Ca2+ and uptake of extracellular Ca2+. Therefore PKC is a negative regulator at several points in Ca2+ mobilization. In contrast, selective depletion of PKC-beta in HL60 cells by an antisense strategy enhanced fMet-Leu-Phe-initiated Ca2+ uptake but not mobilization of intracellular Ca2+. Thapsigargin-induced Ca2+ uptake through SOCC was not affected by PKC-beta II depletion. Thus PKC-beta II is a selective negative regulator of Ca2+ uptake but not release of intracellular Ca2+ stores. PKC-beta II inhibits a receptor-operated cation or Ca2+ channel, thus inhibiting ligand-initiated Ca2+ uptake.

calcium mobilization; protein kinase C isotypes; inositol 1,4,5-trisphosphate; signal transduction


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