Linked Life Data

7912431

Source:http://linkedlifedata.com/resource/pubmed/id/7912431

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-7-26
pubmed:abstractText
The ability to assess the importance of VIP in different physiological processes is limited by the lack of specific potent antagonists. In the present study, we have adopted two different approaches used successfully with other peptides in an attempt to identify new VIP receptor antagonists. One involves the formation of pseudopeptides by insertion of reduced peptide bonds in the NH2-terminus from position 2 to 8 of VIP. The other methodology involves the formation of a COOH-terminal chimeric analogue by combining VIP(6-28) and PACAP(28-38). The ability of each of these peptides to function as an antagonist was compared with reported VIP antagonists. All of the peptides inhibited [125I]VIP binding to VIP receptors on guinea pig pancreatic acini. For the pseudopeptides the affinities were: [psi 3-4]VIP (0.2 microM) = 4 x [psi 4-5]VIP = 8 x [psi 8-9]VIP = 14 x [psi 6-7]VIP, [psi 2-3]VIP = 25 x [psi 5-6]VIP. Each nonpseudopeptide analogue also inhibited VIP binding with relative potencies of VIP(6-28)-PACAP(28-38) (1 microM) = 2.5 x [4-Cl-D-Phe6,Leu17]VIP, VIP(10-28), neurotensin(6-11)-VIP(7-28) = 6 x [Ac-Tyr1,D-Phe2]GRF. All pseudopeptides were agonists with relative potencies: [psi 3-4]VIP > [psi 6-7], [psi 4-5]VIP > [psi 5-6] > [psi 8- 9]VIP > [psi 2-3]VIP. The reported VIP receptor antagonist, neurotensin(6-11)-VIP(7-28), was also an agonist.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0196-9781
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-100
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
A chimeric VIP-PACAP analogue but not VIP pseudopeptides function as VIP receptor antagonists.
pubmed:affiliation
Digestive Diseases Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.