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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1986-10-23
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pubmed:abstractText |
We measured 125I-secretin binding to membranes prepared from rat fundic glands and compared the abilities of natural and synthetic secretin (SN) analogs to inhibit 125I-secretin binding and to activate the cAMP generating system in glandular and subcellular preparations from the fundus and antrum. The natural peptides structurally related to porcine secretin (pSN) included: chicken secretin (cSN), vasoactive intestinal peptide (VIP), porcine peptide with N-terminal histidine and C-terminal isoleucine amide (PHI), helodermin, growth hormone releasing factors isolated from the rat hypothalamus (rhGRF-43, rhGRF-29) or from a human pancreatic tumour (hpGRF-40). These peptides inhibited the binding of 125I-secretin to rat fundic membranes: pSN greater than cSN greater than PHI, VIP and activated the cAMP generating system in fundic glands, according to the following order of potency; pSN greater than cSN greater than PHI, VIP greater than rhGRF-29 greater than rhGRF-43. Porcine peptide with N-terminal tyrosine and C-terminal tyrosine (PYY), GIP, SOM and hpGRF-40 were inactive. Structural requirements for secretin receptor activity were evaluated with four synthetic secretin analogs corresponding to porcine secretin substituted at the N-terminal end by sequence portion of VIP, GIP, GLU and SOM: Ala4-Val5-SN(VIP-SN); Tyr1-Ala2-Glu3-SN (GIP-SN); Gln3-SN (GLU-SN) and Phe1-Phe1-Trp3-Lys4-SN (SOM-SN). The relative potencies of the analogs in fundic and antral preparations were: pSN greater than VIP-SN greater than VIP, GIP-SN greater than GLU-SN greater than SOM-SN for 125I-secretin displacement and cAMP production (glandular cAMP generation and adenylate cyclase activation).(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Gastrointestinal Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Secretin,
http://linkedlifedata.com/resource/pubmed/chemical/secretin receptor
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pubmed:status |
MEDLINE
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pubmed:issn |
0196-9781
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
7 Suppl 1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
155-63
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:3018694-Adenylate Cyclase,
pubmed-meshheading:3018694-Amino Acid Sequence,
pubmed-meshheading:3018694-Animals,
pubmed-meshheading:3018694-Cyclic AMP,
pubmed-meshheading:3018694-Gastric Fundus,
pubmed-meshheading:3018694-Gastric Mucosa,
pubmed-meshheading:3018694-Kinetics,
pubmed-meshheading:3018694-Male,
pubmed-meshheading:3018694-Pyloric Antrum,
pubmed-meshheading:3018694-Rats,
pubmed-meshheading:3018694-Rats, Inbred Strains,
pubmed-meshheading:3018694-Receptors, Cell Surface,
pubmed-meshheading:3018694-Receptors, G-Protein-Coupled,
pubmed-meshheading:3018694-Receptors, Gastrointestinal Hormone,
pubmed-meshheading:3018694-Secretin,
pubmed-meshheading:3018694-Structure-Activity Relationship
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pubmed:year |
1986
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pubmed:articleTitle |
Secretin receptor activity in rat gastric glands. Binding studies, cAMP generation and pharmacology.
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pubmed:publicationType |
Journal Article,
Review
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