Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PRODUCTS OF SPHINGOLIPID CATABOLISM BLOCK ACTIVATION OF THE P21-ACTIVATED PROTEIN-KINASES IN NEUTROPHILS
Autore:
LIAN JP; HUANG RY; ROBINSON D; BADWEY JA;
Indirizzi:
BOSTON BIOMED RES INST,20 STANIFORD ST BOSTON MA 02114 BOSTON BIOMED RES INST BOSTON MA 02114 MASSACHUSETTS GEN HOSP,ARTHRITIS UNIT BOSTON MA 02114 HARVARD UNIV,SCH MED,DEPT BIOL CHEM & MOL PHARMACOL BOSTON MA 02115
Titolo Testata:
The Journal of immunology (1950)
fascicolo: 8, volume: 161, anno: 1998,
pagine: 4375 - 4381
SICI:
0022-1767(1998)161:8<4375:POSCBA>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
IGG-DEPENDENT PHAGOCYTOSIS; ACANTHAMOEBA MYOSIN-I; TUMOR-NECROSIS-FACTOR; HEAVY-CHAIN KINASE; SPHINGOMYELIN PATHWAY; CHEMOTACTIC FACTORS; RESPIRATORY BURST; FREE SPHINGOSINE; ADAPTER PROTEIN; CERAMIDE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
57
Recensione:
Indirizzi per estratti:
Citazione:
J.P. Lian et al., "PRODUCTS OF SPHINGOLIPID CATABOLISM BLOCK ACTIVATION OF THE P21-ACTIVATED PROTEIN-KINASES IN NEUTROPHILS", The Journal of immunology (1950), 161(8), 1998, pp. 4375-4381

Abstract

Neutrophils stimulated with the chemoatttractant FMLP are known to exhibit a rapid and transient activation of two p21-activated protein kinases (Paks) with molecular masses of approximately 63 and 69 kDa, Paks can be detected by their ability to undergo renaturation and catalyze the phosphorylation of a peptide substrate that corresponds to aminoacid residues 297 to 331 of the 47-kDa subunit of the nicotinamide-adenine dinucleotide phosphate-oxidase complex (p47-phox) fixed within agel. In this study, we demonstrate that N-acetylsphingosine (C-2-ceramide) and a variety of sphingoid bases (e.g., D-erythrosphingosine) block activation of the 63- and 69-kDa Paks in neutrophils. The concentrations of these lipids that were effective in blocking Pak activation were similar to those that inhibit a variety of neutrophil responses. Activation of the 63- and 69-kDa Paks was also markedly reduced in neutrophils treated with sphingomyelinase before stimulation. Moreover, we report that addition of C-2-ceramide or D-erythrosphingosine to neutrophils after stimulation with FMLP markedly enhances the rate of Pak inactivation. These effects were not mimicked by arachidonate, which is a potent disorganizing agent of neutrophil membranes, These data support and extend the proposal that sphingoid bases may establish a set point int neutrophils for positive stimuli.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 10:15:05