Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-5-4
pubmed:abstractText
There has been considerable difficulty in defining distinct adrenomedullin (AM) binding sites and function in vivo. However, a rat adrenomedullin receptor (rAMR) and a putative human adrenomedullin receptor (hAMR) have recently been reported. We attempted to confirm and extend the pharmacological characterization of these cloned receptors. COS-7 cells transfected with rAMR or epitope tagged rAMR display abundant rAMR mRNA expression and cell-surface receptor localization. Specific 125I-AM binding is detected in transfected cells; however, similar levels of binding are also detected in cells transfected with vector DNA alone. This AM binding site fails to mediate any changes in cAMP in response to AM. In contrast, Swiss 3T3 cells, expressing specific endogenous AM receptors, display AM binding and functional cAMP responses. Transfection studies performed with the putative hAMR yield similar results. These data suggest that the proposed rAMR and hAMR do not represent authentic adrenomedullin receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
244
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
832-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Expression of the rat adrenomedullin receptor or a putative human adrenomedullin receptor does not correlate with adrenomedullin binding or functional response.
pubmed:affiliation
Department of Molecular Sciences, Pfizer Inc., Groton, Connecticut 06340, USA. Scott_P_Kennedy@Groton.Pfizer.Com
pubmed:publicationType
Journal Article, Comparative Study