Linked Life Data

8094102

Source:http://linkedlifedata.com/resource/pubmed/id/8094102

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-3-11
pubmed:abstractText
Secretin is thought to cause choleresis by acting on a receptor expressed by bile duct epithelial cells. In this study, the receptor was characterized using a new preparation of intrahepatic bile duct plasma membranes. Hyperplastic biliary trees were obtained from 3-week bile duct-ligated rats. The biliary trees were homogenized, filtered, and subjected to an aqueous two-phase partition technique to yield highly purified plasma membranes (confirmed by a 14-fold enrichment in gamma-glutamyl transpeptidase activity and a 10-fold enrichment in 125I-secretin binding). 125I-secretin bound saturably with high affinity and in a dose-dependent fashion (Kd = 1.3 +/- 0.1 nM, Bmax = 273 +/- 23 fmole/mg) to purified plasma membranes. The binding characteristics of secretin were most consistent with a single site receptor model. Competitive binding studies indicated that the secretin-related peptides glucagon, peptide histidine isoleucine, gastric inhibitory peptide, and growth hormone releasing factor did not inhibit binding. Vasoactive intestinal peptide (1 microM) reduced maximal binding by 19 +/- 1%. The GTP analogs guanylylimidodiphosphate and guanosine 5'-O-[3-thiotriphosphate] (1 microM) inhibited binding by 16 +/- 2 and 13 +/- 1%, respectively. In conclusion, secretin binds to a specific, high-affinity receptor in intrahepatic bile duct epithelium that is coupled to a G-protein-linked signal transduction system.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-4804
pubmed:author
pubmed:issnType
Print
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8094102-Animals, pubmed-meshheading:8094102-Bile Ducts, Intrahepatic, pubmed-meshheading:8094102-Binding, Competitive, pubmed-meshheading:8094102-Cell Fractionation, pubmed-meshheading:8094102-Cell Membrane, pubmed-meshheading:8094102-Epithelium, pubmed-meshheading:8094102-Guanosine 5'-O-(3-Thiotriphosphate), pubmed-meshheading:8094102-Guanylyl Imidodiphosphate, pubmed-meshheading:8094102-Kinetics, pubmed-meshheading:8094102-Male, pubmed-meshheading:8094102-Rats, pubmed-meshheading:8094102-Rats, Sprague-Dawley, pubmed-meshheading:8094102-Receptors, G-Protein-Coupled, pubmed-meshheading:8094102-Receptors, Gastrointestinal Hormone, pubmed-meshheading:8094102-Secretin, pubmed-meshheading:8094102-Vasoactive Intestinal Peptide, pubmed-meshheading:8094102-gamma-Glutamyltransferase
pubmed:year
1993
pubmed:articleTitle
Secretin receptors in a new preparation of plasma membranes from intrahepatic biliary epithelium.
pubmed:affiliation
Department of Surgery, Duke University Medical Center, Durham, North Carolina 27710.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.