Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-1-14
pubmed:abstractText
125I-Neuropeptide Y (NPY) bound specifically with high affinity to rat atrial and ventricular membranes. Scatchard analysis revealed the presence of single class of binding sites in both atrial and ventricular membranes. The apparent Kd and Bmax for atrial membranes were 0.63 nM and 70 fmol/mg protein, respectively; ventricular membranes had an apparent kd of 0.39 nM and a Bmax of 283 fmol/mg protein. NPY structural homologues peptide YY (PYY) and pancreatic polypeptide (PP) bound to the ventricular membranes NPY receptor, but with several fold lower potency compared to NPY. Binding of 125I-NPY to ventricular membranes was sensitive to guanosine triphosphate (GTP) suggesting that the NPY receptor is linked to adenylate cyclase system. The receptor characterized in this system may play a crucial role in mediating the cardiac effects of NPY.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0143-4179
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-60
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Interaction of 125I-neuropeptide Y with rat cardiac membranes.
pubmed:affiliation
Department of Surgery, University of Cincinnati Medical Center, Ohio 45267.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.