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Titolo:
Activation of lipoxin A(4) receptors by aspirin-triggered lipoxins and select peptides evokes ligand-specific responses in inflammation
Autore:
Chiang, N; Fierro, IM; Gronert, K; Serhan, CN;
Indirizzi:
Brigham & Womens Hosp, Ctr Expt Therapeut & Reperfus Injury, Dept Anesthesiol Perioperat & Pain Med, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 Pain Med, Boston, MA 02115 USA Harvard Univ, Sch Med, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 vard Univ, Sch Med, Boston, MA 02115 USA
Titolo Testata:
JOURNAL OF EXPERIMENTAL MEDICINE
fascicolo: 7, volume: 191, anno: 2000,
pagine: 1197 - 1207
SICI:
0022-1007(20000403)191:7<1197:AOLARB>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
STABLE ANALOGS; STIMULATED NEUTROPHILS; BINDING; CELLS; IDENTIFICATION; CHEMOTAXIS; PROTEIN; INHIBITION; NETWORKS; IMPACT;
Keywords:
inhibitory receptors; antiinflammation; resolution; leukocytes; MHC binding peptide;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Serhan, CN Brigham & Womens Hosp, Ctr Expt Therapeut & Reperfus Injury, Dept Anesthesiol Perioperat & Pain Med, 75 Francis St, Boston, MA 02115 USA Brigham & Womens Hosp 75 Francis St Boston MA USA 02115 115 USA
Citazione:
N. Chiang et al., "Activation of lipoxin A(4) receptors by aspirin-triggered lipoxins and select peptides evokes ligand-specific responses in inflammation", J EXP MED, 191(7), 2000, pp. 1197-1207

Abstract

Lipoxin (LX) A(4) and aspirin-triggered LX (ATL) are endogenous lipids that regulate leukocyte trafficking via specific LXA(4) receptor (ALXRs) and mediate antiinflammation and resolution ATL analogues dramatically inhibitedhuman neutrophil (polymorphonuclear leukocyte [PMN]) responses evoked by apotent necrotactic peptide derived from mitochondria as well as a rogue synthetic chemotactic peptide. These bioactive lipid analogues and small peptides each selectively competed for specific H-3-LXA(4) binding with recombinant human ALXR, and its N-glycosylation proved essential for peptide but not LXA(4) recognition. Chimeric receptors constructed from receptors with opposing functions, namely ALXR and leukotriene B-4 receptors (BLTs), revealed that the seventh transmembrane segment and adjacent regions of ALXR are essential for LXA(4) recognition, and additional regions of ALXR are required for high affinity binding of the peptide ligands. Together, these findings are the first to indicate that a single Seven-transmembrane receptor sanswitch recognition as well as function with certain chemotactic peptides to inhibitory with ATL and LX (lipid ligands). Moreover, they suggest that ALXR activation by LX or ATL can protect the host from potentially deleterious PMN responses associated with innate immunity as well as direct effectorresponses in tissue injury by recognition of peptide fragments.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 19:50:19