rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
Pt 3
|
pubmed:dateCreated |
2001-1-26
|
pubmed:abstractText |
The role of pituitary adenylate cyclase-activating polypeptide (PACAP) in catecholamine secretion from dissociated adrenal chromaffin cells of the guinea-pig was investigated using amperometry, the patch clamp technique and immunochemistry. Pretreatment of adrenal chromaffin cells with 0.3-10 nM PACAP for 2 min resulted in enhancement of nicotine- and muscarine-induced secretions in either the presence of external Ca2+ ions or nominally Ca2+-free solution, with no change in basal secretion or the holding current at -60 mV in most of the cells tested. Pretreatment with PACAP augmented the muscarine-induced non-selective cation current, but did not affect the muscarine-induced outward current or nicotine-induced current. PACAP-induced enhancement of nicotine- and muscarine-induced secretions was suppressed by the simultaneous application of PACAP and the protein kinase inhibitors 100 microM HA1004 or 2 microM H89. Application of forskolin enhanced both muscarine- and nicotine-induced secretions, whereas application of a phorbol ester augmented the nicotine-induced secretion, but suppressed the muscarine-induced secretion in a reversible manner. Immunohistochemical analysis of adrenal medullae revealed that PACAP-like immunoreactivity was present in nerve fibres surrounding putative chromaffin cells. PAC1R-like immunoreactivity was distributed diffusely in the plasma membrane, whereas nicotinic ACh receptor-like immunoreactivity was concentrated at the plasma membrane near the nucleus, where the synapses were mainly localized. These observations suggest that PACAP in the guinea-pig adrenal medulla functions as a neuromodulator to facilitate ACh-induced secretion through a cAMP-protein kinase A-dependent pathway.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Nov
|
pubmed:issn |
0022-3751
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
1
|
pubmed:volume |
528
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
473-87
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11060125-Adrenal Medulla,
pubmed-meshheading:11060125-Animals,
pubmed-meshheading:11060125-Catecholamines,
pubmed-meshheading:11060125-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:11060125-Electric Conductivity,
pubmed-meshheading:11060125-Enzyme Activation,
pubmed-meshheading:11060125-Female,
pubmed-meshheading:11060125-Guinea Pigs,
pubmed-meshheading:11060125-Immunochemistry,
pubmed-meshheading:11060125-Neuropeptides,
pubmed-meshheading:11060125-Neurotransmitter Agents,
pubmed-meshheading:11060125-Osmolar Concentration,
pubmed-meshheading:11060125-Pituitary Adenylate Cyclase-Activating Polypeptide,
pubmed-meshheading:11060125-Protein Kinase C,
pubmed-meshheading:11060125-Receptors, Cholinergic
|
pubmed:year |
2000
|
pubmed:articleTitle |
Pituitary adenylate cyclase-activating polypeptide may function as a neuromodulator in guinea-pig adrenal medulla.
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pubmed:affiliation |
Departments of Physiology and Anatomy, Fukuoka University School of Medicine, Fukuoka 814-0180, Japan. minoue@fukuoka-u.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|