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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1991-4-2
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pubmed:abstractText |
PACAP (pituitary adenylate-cyclase-activating peptide)-binding receptors were investigated in membranes from the rat pancreatic acinar cell line, AR 4-2J, the rat hippocampus and the human neuroblastoma cell line NB-OK, by 125I-PACAP(1-27) (amino acid residues 1-27 of N-terminal amidated PACAP) binding and adenylate cyclase activation. The relative binding of 125I-PACAP(1-27) to the receptor, and ability to activate adenylate cyclase were PACAP greater than or equal to PACAP(1-27) greater than PACAP(2-38) greater than PACAP(1-9)-VIP(10-28)(PACAP-VIP) greater than PACAP(2-27) greater than [Ser9,Tyr13]VIP greater than [Tyr13]VIP greater than or equal to [Ser9]VIP greater than or equal to VIP(1-23)-PACAP(24-27)(VIP-PACAP) greater than VIP (vasoactive intestinal peptide). The N-terminal moiety of PACAP(1-27) was more important than the three amino acids at the C-terminus for 125I-PACAP(1-27)-binding site recognition. For rat pancreatic 125I-VIP-binding sites tested with 125I-VIP, the order of binding affinity was PACAP = PACAP(1-27) greater than or equal to VIP = [Ser9]VIP = [Tyr13]VIP = [Ser9,Try13]VIP greater than or equal to PACAP-VIP greater than or equal to VIP-PACAP greater than PACAP(2-38) = PACAP(2-27). Pancreatic 125I-VIP-binding sites, when compared to 125I-PACAP(1-27)-binding sites, showed little specificity and only weak coupling, so that PACAP and VIP-PACAP acted only as partial VIP agonists on adenylate cyclase.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADCYAP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adcyap1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Pituitary Adenylate...,
http://linkedlifedata.com/resource/pubmed/chemical/Vasoactive Intestinal Peptide
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
30
|
pubmed:volume |
195
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
535-41
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1997328-Adenylate Cyclase,
pubmed-meshheading:1997328-Amino Acid Sequence,
pubmed-meshheading:1997328-Animals,
pubmed-meshheading:1997328-Binding Sites,
pubmed-meshheading:1997328-Cell Membrane,
pubmed-meshheading:1997328-Chimera,
pubmed-meshheading:1997328-Enzyme Activation,
pubmed-meshheading:1997328-Hippocampus,
pubmed-meshheading:1997328-Humans,
pubmed-meshheading:1997328-Molecular Sequence Data,
pubmed-meshheading:1997328-Neuroblastoma,
pubmed-meshheading:1997328-Neurons,
pubmed-meshheading:1997328-Neuropeptides,
pubmed-meshheading:1997328-Pancreatic Neoplasms,
pubmed-meshheading:1997328-Pituitary Adenylate Cyclase-Activating Polypeptide,
pubmed-meshheading:1997328-Rats,
pubmed-meshheading:1997328-Tumor Cells, Cultured,
pubmed-meshheading:1997328-Vasoactive Intestinal Peptide
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pubmed:year |
1991
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pubmed:articleTitle |
Structural requirements for the binding of the pituitary adenylate-cyclase-activating peptide to receptors and adenylate-cyclase activation in pancreatic and neuronal membranes.
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pubmed:affiliation |
Department of Biochemistry and Nutrition, Medical School, Université Libre de Bruxelles, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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