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Volume 271, Number 43, Issue of October 25, 1996 pp. 26732-26738
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Evidence for a Phorbol Ester-insensitive Phosphorylation Step in Capacitative Calcium Entry in Rat Thymic Lymphocytes

(Received for publication, March 22, 1996, and in revised form, June 25, 1996)

From the Department of Physiology, Tulane University School of Medicine, New Orleans, Louisiana 70112

Experiments were undertaken to investigate the regulation of capacitative Ca²⁺ entry by phorbol ester-sensitive protein kinase C and serine/threonine protein phosphatase activity. The thapsigargin-activated Ca²⁺ entry pathway was probed in control cells and cells treated with phosphatase type 1/2A inhibitors, okadaic acid and calyculin A, or with the phorbol ester, phorbol 12-myristate 13-acetate. The permeability state of this pathway was monitored in the presence or absence of these agents using fluorometric measurements of intracellular Ca²⁺ concentration, unidirectional Mn²⁺ entry, and membrane potential and unidirectional measurements of Ca²⁺ uptake using ⁴⁵Ca²⁺. The results of these studies demonstrate that modification of the phosphorylation state of target protein(s) on serine/threonine amino acid residues by inhibition of phosphatase type 1/2A inhibits the capacitative Ca²⁺ entry pathway in rat thymic lymphocytes. Importantly, the capacitative Ca²⁺ entry pathway in rat thymic lymphocytes is not modulated by activation of phorbol ester-sensitive protein kinase C.

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