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rdf:type |
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lifeskim:mentions |
umls-concept:C0002313,
umls-concept:C0006556,
umls-concept:C0009015,
umls-concept:C0017262,
umls-concept:C0018557,
umls-concept:C0185117,
umls-concept:C0300926,
umls-concept:C0596235,
umls-concept:C0597357,
umls-concept:C1948027,
umls-concept:C2911684
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pubmed:issue |
1-2
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pubmed:dateCreated |
1991-10-3
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pubmed:databankReference |
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pubmed:abstractText |
The serine protease alpha-thrombin (thrombin) potently stimulates G-protein-coupled signaling pathways and DNA synthesis in CCL39 hamster lung fibroblasts. To clone a thrombin receptor cDNA, selective amplification of mRNA sequences displaying homology to the transmembrane domains of G-protein-coupled receptor genes was performed by polymerase chain reaction. Using reverse transcribed poly(A)+ RNA from CCL39 cells and degenerate primers corresponding to conserved regions of several phospholipase C-coupled receptors, three novel putative receptor sequences were identified. One corresponds to an mRNA transcript of 3.4 kb in CCL39 cells and a relatively abundant cDNA. Microinjection of RNA transcribed in vitro from this cDNA in Xenopus oocytes leads to the expression of a functional thrombin receptor. The hamster thrombin receptor consists of 427 amino acid residues with 8 hydrophobic domains, including one at the extreme N-terminus that is likely to represent a signal peptide. A thrombin consensus cleavage site is present in the N-terminal extracellular region of the receptor sequence followed by a negatively charged cluster of residues present in a number of proteins that interact with the anion-binding exosite of thrombin.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
288
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
123-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1652467-Amino Acid Sequence,
pubmed-meshheading:1652467-Animals,
pubmed-meshheading:1652467-Base Sequence,
pubmed-meshheading:1652467-Blotting, Northern,
pubmed-meshheading:1652467-Calcium,
pubmed-meshheading:1652467-Cloning, Molecular,
pubmed-meshheading:1652467-Cricetinae,
pubmed-meshheading:1652467-Cricetulus,
pubmed-meshheading:1652467-GTP-Binding Proteins,
pubmed-meshheading:1652467-Humans,
pubmed-meshheading:1652467-Molecular Sequence Data,
pubmed-meshheading:1652467-Oocytes,
pubmed-meshheading:1652467-Polymerase Chain Reaction,
pubmed-meshheading:1652467-Receptors, Cell Surface,
pubmed-meshheading:1652467-Receptors, Thrombin,
pubmed-meshheading:1652467-Recombinant Proteins,
pubmed-meshheading:1652467-Sequence Alignment,
pubmed-meshheading:1652467-Type C Phospholipases,
pubmed-meshheading:1652467-Xenopus
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pubmed:year |
1991
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pubmed:articleTitle |
cDNA cloning and expression of a hamster alpha-thrombin receptor coupled to Ca2+ mobilization.
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pubmed:affiliation |
Transgene, S.A., Strasbourg, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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