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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3-5
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pubmed:dateCreated |
1989-11-21
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pubmed:abstractText |
The original concept that cyclic GMP is one of the mediators of the hormone-dependent process of steroidogenesis has been strengthened by the characterization of a 180-kDa protein from rat adrenocortical carcinoma and rat and mouse testes. This protein appears to have an unusual characteristic of containing both the atrial natriuretic factor (ANF)-binding and guanylate cyclase activities, and appears to be intimately involved in the ANF-dependent steroidogenic signal transduction. In rat adrenal glands we now demonstrate: 1) the direct presence of a 180-kDa ANF-binding protein in GTP-affinity purified membrane fraction as evidenced by affinity cross-linking technique and by the Western blot analysis of the partially purified enzyme; 2) that the enzyme is biochemically and immunologically different from the soluble guanylate cyclase as there is no antigenic cross-reactivity of 180-kDa guanylate cyclase antibody with soluble guanylate cyclase; 3) in contrast to the soluble guanylate cyclase, the particulate enzyme is not stimulated by nitrite-generating compounds and hemin; and 4) protein kinase C inhibits both the basal and ANF-dependent guanylate cyclase activity and phosphorylates the 180-kDa guanylate cyclase. These results reveal the presence of a 180-kDa protein in rat adrenal glands and support the contention that: (a) this protein contains both the guanylate cyclase and ANF receptor; (b) the 180-kDa enzyme is coupled with the ANF-dependent cyclic GMP production; (c) the 180-kDa enzyme is biochemically distinct from the nonspecific soluble guanylate cyclase; and (d) there is a protein kinase C-dependent negative regulatory loop for the operation of ANF-dependent cyclic GMP signal pathway which acts via the phosphorylation of 180-kDa guanylate cyclase.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Atrial Natriuretic Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Azides,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Hemin,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitroprusside,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Atrial Natriuretic Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Azide,
http://linkedlifedata.com/resource/pubmed/chemical/atrial natriuretic peptide, rat
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pubmed:status |
MEDLINE
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pubmed:issn |
0039-128X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
437-60
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2572076-Adrenal Cortex Neoplasms,
pubmed-meshheading:2572076-Adrenal Glands,
pubmed-meshheading:2572076-Animals,
pubmed-meshheading:2572076-Antibodies,
pubmed-meshheading:2572076-Atrial Natriuretic Factor,
pubmed-meshheading:2572076-Azides,
pubmed-meshheading:2572076-Cyclic GMP,
pubmed-meshheading:2572076-Guanylate Cyclase,
pubmed-meshheading:2572076-Hemin,
pubmed-meshheading:2572076-Hemoglobins,
pubmed-meshheading:2572076-Nitroprusside,
pubmed-meshheading:2572076-Phosphorylation,
pubmed-meshheading:2572076-Protein Kinase C,
pubmed-meshheading:2572076-Rabbits,
pubmed-meshheading:2572076-Rats,
pubmed-meshheading:2572076-Receptors, Atrial Natriuretic Factor,
pubmed-meshheading:2572076-Receptors, Cell Surface,
pubmed-meshheading:2572076-Sodium Azide
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pubmed:articleTitle |
Purification and characterization of the 180-kDa membrane guanylate cyclase containing atrial natriuretic factor receptor from rat adrenal gland and its regulation by protein kinase C.
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pubmed:affiliation |
Section of Regulatory Biology, Cleveland Clinic Research Institute, OH 44195-5068.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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