Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
T21/DP107, a synthetic leucine zipper-like domain of the HIV-1 envelope gp41, attracts and activates human phagocytes by using G-protein-coupled formyl peptide receptors
Autore:
Su, SB; Gao, JL; Gong, WH; Dunlop, NM; Murphy, PM; Oppenheim, JJ; Wang, JM;
Indirizzi:
NCI,ederick,ck Canc Res & Dev Ctr, Div Basic Sci, Mol Immunoregulat Lab, Fr NCI Frederick MD USA 21702 Ctr, Div Basic Sci, Mol Immunoregulat Lab, Fr NCI,pporterick Canc Res & Dev Ctr, Sci Applicat Int Corp, Intramural Res Su NCI Frederick MD USA 21702 Ctr, Sci Applicat Int Corp, Intramural Res Su NIH, NIAID, Host Def Lab, Bethesda, MD 20892 USA NIH Bethesda MD USA 20892 IH, NIAID, Host Def Lab, Bethesda, MD 20892 USA
Titolo Testata:
JOURNAL OF IMMUNOLOGY
fascicolo: 10, volume: 162, anno: 1999,
pagine: 5924 - 5930
SICI:
0022-1767(19990515)162:10<5924:TASLZD>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNODEFICIENCY-VIRUS TYPE-1; LIPOXIN A(4) RECEPTOR; SERUM AMYLOID-A; CHEMOATTRACTANT RECEPTORS; CHEMOTACTIC RECEPTOR; HUMAN MONOCYTES; STABLE ANALOGS; FORMYLPEPTIDE; GLYCOPROTEIN; NEUTROPHILS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Wang, JM NCI,dgrederick Canc Res & Dev Ctr, Div Basic Sci, Mol Immunoregulat Lab, Bl NCI Bldg 560,Room 31-19 Frederick MD USA 21702 unoregulat Lab, Bl
Citazione:
S.B. Su et al., "T21/DP107, a synthetic leucine zipper-like domain of the HIV-1 envelope gp41, attracts and activates human phagocytes by using G-protein-coupled formyl peptide receptors", J IMMUNOL, 162(10), 1999, pp. 5924-5930

Abstract

A leucine zipper-like domain, T21/DP107, located in the amino terminus of the ectodomain of gp41, is crucial to the formation of fusogenic configuration of the HIV-1 envelope protein gp41. We report that the synthetic T21/DP107 segment is a potent stimulant of migration and calcium mobilization in human monocytes and neutrophils, The activity of T21/DP107 on phagocytes was pertussis toxin-sensitive, suggesting this peptide uses Gi-coupled seven-transmembrane receptor(s), Since the bacterial chemotactic peptide fMLP partially desensitized the calcium-mobilizing activity of T21/DP107 in phagocytes, we postulated that T21/DP107 might preferentially use a lower affinityfMLP receptor. By using cells transfected to express cloned prototype chemotactic N-formyl peptide receptor (FPR) or its variant, FPR-like 1 (FPRL1),we demonstrate that T21/DP107 activates both receptors but has a much higher efficacy for FPRL1, In addition, T21/DP107 at nM concentrations induced migration of FPRL1-transfected human embryonic kidney 293 cells. In contrast, fMLP did not induce significant chemotaxis of the same cells at a concentration as high as 50 mu M Although a lipid metabolite, lipoxin A4, was a high-affinity ligand for FPRL1, it was not reported to induce Ca2+ mobilization or chemotaxis in FPRL1-transfected cells. Therefore, T21/DP107 is a first chemotactic peptide agonist identified thus far for FPRL1. Our results suggest that this peptide domain of the HIV-1 gp41 may have the potential toactivate host innate immune response by interacting with FPR and FPRL1 on phagocytes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 22:00:57