Linked Life Data

10189064

Source:http://linkedlifedata.com/resource/pubmed/id/10189064

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-5-17
pubmed:abstractText
This study characterized rat lung membrane arginine vasopressin (AVP) receptors in detail. Specific binding of [3H]AVP to rat lung membranes was dependent upon time, temperature and membrane protein concentration. Scatchard plot analysis of equilibrium binding data revealed the existence of a single class of high-affinity binding sites with a Kd of 0.45 nM and a Bmax of 76.6 fmol/mg protein. Competitive inhibition of [3H]AVP binding showed that neurohypophysial hormones as well as their synthetic analogues displaced [3H]AVP in a concentration-dependent manner. The order of potencies for the native peptides was: AVP > lysine vasopressin = arginine vasotocin > oxytocin. Furthermore, potent V1A receptor antagonists, d(CH2)5Tyr(Me)AVP and dPTyr(Me)AVP, showed high affinity for lung membranes. In contrast, the V2 receptor agonist, dDAVP, and the specific oxytocin receptor agonist, [Thr4,Gly7]oxytocin, did not affect AVP binding. These results suggest that the lung contains the V1A receptor subtype. The lung membrane AVP receptor characterized in this study may play an important role in mediating the physiological effects of AVP in the lung.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0143-4179
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
281-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Characterization of vasopressin receptor in rat lung.
pubmed:affiliation
Institute for Drug Discovery Research, Yamanouchi Pharmaceutical Co. Ltd, Ibaraki, Japan. tahara@yamanouchi.co.jp
pubmed:publicationType
Journal Article, Comparative Study