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Journal of Neuroscience, Vol 12, 3071-3083, Copyright © 1992 by Society for Neuroscience
Phosphorylation of DARPP-32 and protein phosphatase inhibitor-1 in rat choroid plexus: regulation by factors other than dopamine
GL Snyder, JA Girault, JY Chen, AJ Czernik, JW Kebabian, JA Nathanson and P Greengard
Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, New York 10021.
The molecular mechanisms underlying regulation of fluid production by
secretory epithelia such as the choroid plexus are poorly understood. Two
cAMP-regulated inhibitors of protein phosphatase-1, inhibitor-1 (I1) and a
dopamine- and cAMP-regulated phosphoprotein, M(r) = 32,000 (DARPP-32), are
enriched in the choroid plexus. We show here that these two phosphoproteins
are colocalized in choroid plexus epithelial cells. We have developed a
novel method for studying the phosphorylation state of DARPP-32 and I1 in
intact cells, using a phosphorylation state- specific monoclonal antibody.
Several drugs and hormones that are known to alter fluid secretion and that
increase cAMP levels (forskolin, isoproterenol, vasoactive intestinal
peptide) or cGMP levels (atrial natriuretic peptide) or that may use
additional second messenger pathways (5-HT), increase the phosphorylation
of I1 and DARPP-32 in rat choroid plexus. In contrast, dopamine does not
alter cAMP and cGMP levels, or I1 and DARPP-32 phosphorylation. Our results
indicate that DARPP-32, known to be regulated by dopamine in a number of
tissues, can be phosphorylated in response to non-dopaminergic factors,
including hormones acting through non-cAMP-dependent pathways. Our results
also raise the possibility that inhibition of phosphatase-1, as a result of
I1 and DARPP-32 phosphorylation, might be part of a final common pathway in
the action of several factors that are known or thought to alter
cerebrospinal fluid production.
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