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Titolo:
IDENTIFICATION OF C-C CHEMOKINE RECEPTOR-1 (CCR1) AS THE MONOCYTE HEMOFILTRATE C-C CHEMOKINE (HCC)-1 RECEPTOR
Autore:
TSOU CL; GLADUE RP; CARROLL LA; PARADIS T; BOYD JG; NELSON RT; NEOTE K; CHARO IF;
Indirizzi:
UNIV CALIF SAN FRANCISCO,GLADSTONE INST CARDIOVASC DIS,CARDIOVASC RESINST,POB 419100 SAN FRANCISCO CA 94141 UNIV CALIF SAN FRANCISCO,DAIICHI RES CTR SAN FRANCISCO CA 94141 UNIV CALIF SAN FRANCISCO,DEPT MED SAN FRANCISCO CA 94141 PFIZER INC GROTON CT 06340
Titolo Testata:
The Journal of experimental medicine
fascicolo: 3, volume: 188, anno: 1998,
pagine: 603 - 608
SICI:
0022-1007(1998)188:3<603:IOCCR(>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHEMOATTRACTANT PROTEIN-1 RECEPTOR; MOLECULAR-CLONING; SIGNAL-TRANSDUCTION; FUNCTIONAL LIGAND; CELL-LINE; CHEMOTAXIS; EXPRESSION; I-309;
Keywords:
HEMOFILTRATE C-C CHEMOKINE; C-C CHEMOKINE RECEPTOR 1; CHEMOKINE; CHEMOTAXIS; MACROPHAGE INFLAMMATORY PROTEIN 1-ALPHA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
C.L. Tsou et al., "IDENTIFICATION OF C-C CHEMOKINE RECEPTOR-1 (CCR1) AS THE MONOCYTE HEMOFILTRATE C-C CHEMOKINE (HCC)-1 RECEPTOR", The Journal of experimental medicine, 188(3), 1998, pp. 603-608

Abstract

Hemofiltrate C-C chemokine (HCC)-1 is a recently cloned C-C chemokinethat is structurally similar to macrophage inflammatory protein (MIP)-1 alpha. Unlike most chemokines, it is constitutively secreted by tissues and is present at high concentrations in normal human plasma. Also atypical for chemokines, HCC-1 is reported not to be chemotactic forleukocytes. In this paper, we have investigated the chemokine receptor usage and downstream signaling pathways of HCC-1. Cross-desensitization experiments using THP-1 cells suggested that HCC-1 and MIP-1 alphaactivated the same receptor. Experiments using a panel of cloned chemokine receptors revealed that HCC-1 specifically activated C-C chemokine receptor (CCR)1, but not closely related receptors, including CCR5. HCC-1 competed with MIP-1 alpha for binding to CCR1-transfected cells, but with a markedly reduced affinity (IC50 = 93 nM versus 1.3 nM forMIP-1 alpha). Similarly, HCC-1 was less potent than MIP-1 alpha in inducing inhibition of adenylyl cyclase in CCR1-transfected cells. HCC-1induced chemotaxis of freshly isolated human monocytes, THP-1 cells, and CCR1-transfected cells, and the optimal concentration for cell migration (100 nM) was similar to 100-fold lower than that of MIP-1 alpha(1 nM). These data demonstrate that HCC-1 is a chemoattractant and identify CCR1 as a functional HCC-1 receptor on human monocytes.

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Documento generato il 24/09/20 alle ore 05:25:40