Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1988-8-31
pubmed:abstractText
Receptor binding of fish neuropeptide urotensin II (UII) was characterized in membranes isolated from major rat arteries. Monoiodinated UII radioligand (125I-UII) was prepared and purified using high-pressure liquid chromatography (HPLC). The contractile potency of iodinated UII (I-UII) on rat thoracic aorta strips was somewhat lower than that of native UII. The binding of 125I-UII to the membrane preparations of rat thoracic aorta was saturable, specific and time-dependent. Scatchard analysis indicated a single population of binding sites with an apparent dissociation constant of 5.9 x 10(-9) M. The calculated maximal number of binding sites was about 155 fmol/mg protein. The specific binding to the membrane preparations from the abdominal aorta and mesenteric artery was about 27 and 8%, respectively, of those in the thoracic aorta, which corresponds to the order of contractile potency of UII on rat blood vessels: thoracic aorta greater than abdominal aorta greater than mesenteric artery. The displacement of 125I-UII binding by the UII peptide or its fragments (UII-(5-12), UII-(6-12) and UII-(6-11] were also comparable to their contractile effects on rat thoracic aorta strips (UII greater than UII-(5-12) greater than UII-(6-12) much greater than UII-(6-11]. These results suggest that the fish neuropeptide, UII, can induce contraction of rat vascular tissue by interacting with its functional receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-2999
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
149
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
61-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Functional receptors for fish neuropeptide urotensin II in major rat arteries.
pubmed:affiliation
Department of Pharmacology and Therapeutics, Faculty of Medicine, University of Calgary, Alberta, Canada.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't