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Titolo:
MEK-1/2 inhibition prevents 5-lipoxygenase translocation in N-formylpeptide-challenged human neutrophils
Autore:
Boden, SE; Bertsche, T; Ammon, HPT; Safayhi, H;
Indirizzi:
Univ Tubingen, Inst Pharmaceut Sci, Dept Pharmacol, D-72076 Tubingen, Germany Univ Tubingen Tubingen Germany D-72076 rmacol, D-72076 Tubingen, Germany
Titolo Testata:
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
fascicolo: 10, volume: 32, anno: 2000,
pagine: 1069 - 1074
SICI:
1357-2725(200010)32:10<1069:MIP5TI>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIVATED PROTEIN-KINASE; TYROSINE PHOSPHORYLATION; LEUKOTRIENE SYNTHESIS; MAP KINASE; RELEASE; INFLUX; STORES; ACID;
Keywords:
5-lipoxygenase; MEK (mitogen-activated protein kinase kinase); fMLP (N-formylmethionyl-leucyl-phenylalanine; PD098059; U0126; SB203580;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Safayhi, H Univ Tubingen, Inst Pharmaceut Sci, Dept Pharmacol, Morgenstelle 8, D-72076 Tubingen, Germany Univ Tubingen Morgenstelle 8 Tubingen Germany D-72076 Germany
Citazione:
S.E. Boden et al., "MEK-1/2 inhibition prevents 5-lipoxygenase translocation in N-formylpeptide-challenged human neutrophils", INT J BIO C, 32(10), 2000, pp. 1069-1074

Abstract

In order to elucidate the role of mitogen-activated protein kinase kinase (MEK-1/2) in 5-lipoxygenase (5-LO) activation we studied the N-formyl-methionyl-leucyl-phenylalanine (fMLP)-induced 5-LO translocation in human blood neutrophils (PMNs). In non-primed, Ca2+-repleted PMNs, fMLP consistently stimulated MEK-1/2 phosphorylation, but induced 5-LO translocation and product formation (430 +/- 128 pmol; SEM, n = 13) only in 13 of 18 PMN preparations from different healthy donors. In fMLP-responsive cells, the MEK-1/2 inhibitor PD098059 (50 muM) attenuated MEK phosphorylation and abolished 5-LO activation at the translocation step. The fMLP-mediated 5-LO product formation was also sensitive to MEK inhibition by U0126 and to p38 inhibition by SB203580. But in contrast to PD098059, U0126 at 10 muM and SB203580 at 20-50 muM impaired 5-LO activity in the cell-free assay setting, suggesting direct actions of higher concentrations of U0126 and SB203580 on 5-LO apart from MEK and p38 inhibition, respectively. These data show that fMLP initiates 5-LO product formation in non-primed, Ca2+-repleted human blood PMNs fromhealthy donors, and that MEK signaling is pivotal, but not sufficient for 5-LO activation in response to the receptor agonist fMLP. (C) 2000 ElsevierScience Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 22:52:48