ISSN:
1573-5168
Keywords:
signal transduction
;
cyclic AMP
;
protein kinase A
;
protein kinase C
;
[Ca2+]i
;
voltage-sensitive Ca2+ channels
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract The mechanisms of pituitary adenylate cyclase activating polypeptide (PACAP) action on goldfish growth hormone (GH) release were investigated by examining GH release responses from dispersed goldfish pituitary cells to a synthetic mammalian (m)PACAP38 peptide. It was established that GH release stimulated by 2-h exposure to mPACAP38 was concentration-dependent, attenuated by the PACAP receptor antagonist mPACAP6−38, and subject to neuroendocrine modulation by somatostatin. Maximal mPACAP38-stimulated GH release was not additive to the responses elicited by either the adenylate cyclase activator forskolin or the cyclic (c)AMP analog 8-bromo-cAMP. The GH responses to mPACAP38, forskolin and 8-bromo-cAMP, either alone or in combination, were abolished by H89, a protein kinase A (PKA) inhibitor. SQ22536, an adenylate cyclase inhibitor, attenuated forskolin- and mPACAP38-stimulated GH release. In contrast, mPACAP38-stimulated GH release were additive to the responses to two protein kinase C (PKC) activators and unaffected by two PKC inhibitors. These results suggest that the stimulatory action of PACAP on GH secretion is mediated through a cAMP- / PKA-dependent mechanism, whereas the involvement of PKC appears unlikely. The ability of mPACAP38 to further enhance maximal GnRH (PKC)-dependent GH release, but not dopamine D1 agonist (PKA)-dependent GH secretion, is consistent with this hypothesis. A possible involvement of Ca2+ in PACAP action is also suggested. Two inhibitors of voltage-sensitive Ca2+ channel reduced the GH responses to mPACAP38 in static incubation; conversely, mPACAP38 increased intracellular [Ca2+] in identified, single goldfish somatotropes.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1007837708880
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