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Articles in PresS, published online ahead of print December 5, 2001
Am J Physiol Cell Physiol, 10.1152/ajpcell.00352.2001
Submitted on July 26, 2001
Accepted on November 27, 2001
1 Oral Physiology, Meikai University, Saitama, Japan; NIDCR/GTTB, National Institutes of Health, Bethesda, MD, USA
2 Biochemistry, Meikai University, Saitama, Japan
3 NIDCR/GTTB, National Institutes of Health, Bethesda, MD, USA
* To whom correspondence should be addressed. E-mail: rjturner{at}nih.gov.
We study the phosphorylation of the secretory Na+-K+-2Cl- cotransporter (NKCC1) in rat parotid acinar cells. We have previously shown that NKCC1 activity in these cells is dramatically up-regulated in response to ß-adrenergic stimulation and that this up-regulation correlates with NKCC1 phosphorylation, possibly due to protein kinase A (PKA). We show here that when ATP is added to purified acinar basolateral membranes (BLM) NKCC1 is phosphorylated as a result of membrane-associated protein kinase activity. Additional NKCC1 phosphorylation is seen when PKA is added to BLMs, but our data indicate that this is due to an effect of PKA on endogenous membrane kinase or phosphatase activities rather than its direct phosphorylation of NKCC1. Also, phosphopeptide mapping demonstrates that these phosphorylations do not take place at the site associated with the up-regulation of NKCC1 by ß-adrenergic stimulation. But this up-regulatory phosphorylation can be mimicked by the addition of cAMP to permeabilized acini and this effect can blocked by a specific PKA inhibitor. These latter results provide good evidence that protein kinase A is indeed involved in the up-regulatory phosphorylation of NKCC1 and suggest that an additional factor present in the acinar cell but absent from isolated membranes is required to bring about the phosphorylation.
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