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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1989-10-24
|
| pubmed:databankReference | |
| pubmed:abstractText |
Atrial natriuretic peptide (ANP) binds directly to a plasma membrane form of guanylate cyclase (GC-A), stimulating the production of the second messenger cyclic GMP. We show that a second guanylate cyclase/receptor (GC-B) exists, with distinctly different specificities for various natriuretic peptides. A cDNA clone encoding GC-B was isolated by low-stringency screening of a rat brain cDNA library using GC-A cDNA as a probe. The deduced amino acid sequence of GC-B is 78% identical with GC-A within the intracellular region, but 43% identical within the extracellular domain. Cyclic GMP concentrations in cells transfected with GC-A were half-maximally elevated at 3 nM ANP, 25 nM brain natriuretic peptide (BNP), and 65 nM atriopeptin 1, while 25 microM ANP, 6 microM BNP, and greater than 100 microM atriopeptin 1 were required for half-maximal stimulation of GC-B. The potencies of natriuretic peptides on GC-A and GC-B activity are therefore markedly different; furthermore, despite the specificity of GC-B for BNP, the relatively high BNP concentration required to elicit a response suggests the possible presence of a more potent, unidentified natural ligand.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Atrial Natriuretic Factor,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Atrial Natriuretic Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0092-8674
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
22
|
| pubmed:volume |
58
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1155-62
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:2570641-Amino Acid Sequence,
pubmed-meshheading:2570641-Animals,
pubmed-meshheading:2570641-Atrial Natriuretic Factor,
pubmed-meshheading:2570641-Base Sequence,
pubmed-meshheading:2570641-Brain,
pubmed-meshheading:2570641-Cell Line,
pubmed-meshheading:2570641-Cell Membrane,
pubmed-meshheading:2570641-Cloning, Molecular,
pubmed-meshheading:2570641-DNA,
pubmed-meshheading:2570641-Genes,
pubmed-meshheading:2570641-Genetic Variation,
pubmed-meshheading:2570641-Guanylate Cyclase,
pubmed-meshheading:2570641-Molecular Sequence Data,
pubmed-meshheading:2570641-Multigene Family,
pubmed-meshheading:2570641-Nucleic Acid Hybridization,
pubmed-meshheading:2570641-Rats,
pubmed-meshheading:2570641-Receptors, Atrial Natriuretic Factor,
pubmed-meshheading:2570641-Receptors, Cell Surface,
pubmed-meshheading:2570641-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2570641-Transfection
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
The primary structure of a plasma membrane guanylate cyclase demonstrates diversity within this new receptor family.
|
| pubmed:affiliation |
Howard Hughes Medical Institute, Vanderbilt University Medical Center, Nashville, Tennessee 37232.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|