Linked Life Data

8179608

Source:http://linkedlifedata.com/resource/pubmed/id/8179608

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-6-3
pubmed:abstractText
We have demonstrated specific adenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) receptors at heart cell surfaces. Optimal Ap4A binding requires receptor activation. Other Investigators have demonstrated that Ap5A and Ap6A act as vasopressors. We now compare the binding of Ap4A, Ap5A and Ap6A on heart membranes to determine if all three ligands bind to the same receptor and their relative avidities. Anti-Ap4A receptor antibodies inhibit the binding of all three ligands. SDS-PAGE analysis of Ap4A, Ap5A and Ap6A cross-linked to membranes reveals that all three are attached to a 30 kDa peptide. The specific activity for binding to unactivated membranes is similar for all three ligands. However, after receptor activation there is a 3.4x increase in Ap4A binding and a 32.5x decrease in the KD; values remain unchanged for Ap5A and Ap6A. These data indicate that Ap4A, Ap5A and Ap6A bind to the same receptor on cardiac membranes but receptor activation enhances only Ap4A binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
200
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
749-55
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Adenylated dinucleotide binding to the adenosine 5',5'''-P1,P4-tetraphosphate mouse heart receptor.
pubmed:affiliation
Department of Biological Sciences, Clemson University, SC 29634-1903.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, Non-U.S. Gov't