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The Journal of Neuroscience, February 15, 2000, 20(4):1365-1373
Ca2+-Evoked Serotonin Secretion by Parafollicular
Cells: Roles in Signal Transduction of Phosphatidylinositol 3'-kinase,
and the  and  Isoforms of Protein Kinase C
Kuo-peing
Liu1,
Shu-chi
Hsiung1,
Mella
Adlersberg1,
Todd
Sacktor2,
Michael D.
Gershon3, and
Hadassah
Tamir1, 3
1 Division of Neuroscience, New York State Psychiatric
Institute, New York, New York 10032, 2 Department of
Pharmacology, Physiology, and Neurology State University of New York
Health Science Center, New York, New York 11203, and
3 Department of Anatomy and Cell Biology, Columbia
University, College of Physicians and Surgeons, New York, New York
10032
Parafollicular (PF) cells secrete 5-HT in response to stimulation
of a G-protein-coupled Ca2+ receptor (CaR) by
increased extracellular Ca2+
( [Ca2+]e). We tested
the hypothesis that protein kinase C (PKC) participates in
stimulus-secretion coupling. Immunoblots from membrane and cytosolic
fractions of isolated PF cells revealed conventional ( ,  I, and
 ), novel ( and  ), and atypical ( / and  ) PKCs. Only
PKC was found to have been translocated to the membrane fraction
when secretion of 5-HT was evoked by
[Ca2+]e or phorbol esters. Although
phorbol downregulation caused PKC to disappear, secretion was only
partially inhibited. A similar reduction of
[Ca2+]e-evoked secretion was
produced by inhibitors of conventional and/or novel PKCs (Gö
6976, calphostin C, and pseudoA), and these compounds did not inhibit
secretion at all when applied to phorbol-downregulated cells. In
contrast, the phorbol downregulation-resistant component of secretion
was abolished by pseudoZ, which inhibits the atypical PKC.
Stimulation of PF cells with
[Ca2+]e increased the activity of
immunoprecipitated PKC (but not PKC/), and the activity of
this PKC was inhibited by pseudoZ. PF cells were found to express
regulatory (p85) and catalytic (p110 and p110) subunits of
phosphatidylinositol 3'-kinase (PI3'-kinase). [Ca2+]e increased the activity of
immunoprecipitated PI3'-kinase; moreover, PI3'-kinase inhibitors
(wortmannin and LY294002) antagonized secretion. We suggest that
PKC isoforms mediate secretion of 5-HT by PF cells in response to
stimulation of the CaR. PKC involvement can be accounted for by PKC
and an isoform sensitive to inhibition by pseudoZ, probably PKC,
which is activated via PI3'-kinase.
Key words:
Ca2+ receptor; serotonin secretion; protein kinase C; protein kinase C; phosphatidylinositol
3'-kinase; thyroid parafollicular cell
Copyright © 2000 Society for Neuroscience 0270-6474/00/2041365-09$05.00/0
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