rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1992-6-2
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pubmed:databankReference |
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pubmed:abstractText |
A cDNA of 1650 base pairs was isolated by screening an HL-60 granulocyte library with an N-formyl peptide receptor (NFPR) cDNA probe under low stringency conditions. The cDNA encodes a protein of 351 amino acids tentatively named FPR2, with a calculated molecular weight of 39 kDa. Sequence analysis revealed that FPR2 is 69% identical in sequence to the human NFPR and shares extensive homology to several other chemoattractant receptors. FPR2 expressed in transfected cells mediated formyl peptide-stimulated calcium mobilization at micromolar concentrations of ligand. FPR2 messenger is detected in granulocytic HL-60 cells, but not in undifferentiated HL-60 cells. These findings suggest that FPR2 is a novel receptor for formyl peptide ligand and a new member of the chemoattractant receptor gene family.
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pubmed:grant |
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Probes,
http://linkedlifedata.com/resource/pubmed/chemical/N-Formylmethionine...,
http://linkedlifedata.com/resource/pubmed/chemical/Poly A,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Formyl Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
|
pubmed:issn |
0006-291X
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
30
|
pubmed:volume |
184
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pubmed:geneSymbol |
FPR2
|
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
582-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1374236-Amino Acid Sequence,
pubmed-meshheading:1374236-Animals,
pubmed-meshheading:1374236-Base Sequence,
pubmed-meshheading:1374236-Cell Line,
pubmed-meshheading:1374236-Cloning, Molecular,
pubmed-meshheading:1374236-DNA, Neoplasm,
pubmed-meshheading:1374236-DNA Probes,
pubmed-meshheading:1374236-Granulocytes,
pubmed-meshheading:1374236-Humans,
pubmed-meshheading:1374236-Leukemia, Promyelocytic, Acute,
pubmed-meshheading:1374236-Mice,
pubmed-meshheading:1374236-Molecular Sequence Data,
pubmed-meshheading:1374236-Molecular Weight,
pubmed-meshheading:1374236-Multigene Family,
pubmed-meshheading:1374236-N-Formylmethionine Leucyl-Phenylalanine,
pubmed-meshheading:1374236-Poly A,
pubmed-meshheading:1374236-Polymerase Chain Reaction,
pubmed-meshheading:1374236-Protein Conformation,
pubmed-meshheading:1374236-RNA,
pubmed-meshheading:1374236-RNA, Messenger,
pubmed-meshheading:1374236-Receptors, Formyl Peptide,
pubmed-meshheading:1374236-Receptors, Immunologic,
pubmed-meshheading:1374236-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1374236-Transfection
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pubmed:year |
1992
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pubmed:articleTitle |
Isolation of a cDNA that encodes a novel granulocyte N-formyl peptide receptor.
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pubmed:affiliation |
Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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