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Titolo:
A novel mitogen-activated protein kinase phosphatase is an important negative regulator of lipopolysaccharide-mediated c-Jun N-terminal kinase activation in mouse macrophage cell lines
Autore:
Matsuguchi, T; Musikacharoen, T; Johnson, TR; Kraft, AS; Yoshikai, Y;
Indirizzi:
Nagoya Univ, Sch Med, Dis Mechanism & Control Res Inst, Lab Host Def & Germfree Life,Showa Ku, Nagoya, Aichi 4668550, Japan Nagoya Univ Nagoya AichiJapan 4668550 a Ku, Nagoya, Aichi 4668550, Japan Univ Colorado, Hlth Sci Ctr, Dept Med Oncol, Denver, CO 80262 USA Univ Colorado Denver CO USA 80262 r, Dept Med Oncol, Denver, CO 80262 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 20, volume: 21, anno: 2001,
pagine: 6999 - 7009
SICI:
0270-7306(200110)21:20<6999:ANMPKP>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
DUAL-SPECIFICITY PHOSPHATASES; SIGNAL-TRANSDUCTION PATHWAY; COLONY-STIMULATING FACTOR; TOLL-LIKE RECEPTOR-2; BACTERIAL LIPOPOLYSACCHARIDE; TYROSINE-PHOSPHATASE; TRANSCRIPTIONAL ACTIVATION; CATALYTIC ACTIVATION; MURINE MACROPHAGES; MOLECULAR-CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
58
Recensione:
Indirizzi per estratti:
Indirizzo: Matsuguchi, T Nagoya Univ, Sch Med, Dis Mechanism & Control Res Inst, Lab Host Def & Germfree Life,Showa Ku, 65 Tsurumai Cho, Nagoya, Aichi 4668550, Japan Nagoya Univ 65 Tsurumai Cho Nagoya Aichi Japan 4668550 Japan
Citazione:
T. Matsuguchi et al., "A novel mitogen-activated protein kinase phosphatase is an important negative regulator of lipopolysaccharide-mediated c-Jun N-terminal kinase activation in mouse macrophage cell lines", MOL CELL B, 21(20), 2001, pp. 6999-7009

Abstract

We have isolated a cDNA homologous to known dual-specificity phosphatases from a mouse macrophage cDNA library and termed it MKP-M (for mitogen-activated protein kinase phosphatase isolated from macrophages). Three other presumed splice variant isoforms have also been identified for MKP-M. The longest and most abundant mRNA contains an open reading frame corresponding to 677 amino acids and produces an 80-kDa protein. The deduced amino acid sequence of MKP-M is most similar to those of hVH-5 (or mouse M3/6) and VHP1, aCaenorhabditis elegans tyrosine phosphatase. It includes an N-terminal rhodanase homology domain, the extended active-site sequence motif (V/L)X(V/I)HCXAG(I/V)SRSXT(I/V)XXAY(L/I)M (where X is any amino acid), and a C-terminal PEST sequence. Northern blot analysis revealed a dominant MKP-M mRNA species of approximately 5.5 kb detected ubiquitously among all tissues examined. MKP-M was constitutively expressed in mouse macrophage cell lines, and its expression levels were rapidly increased by lipopolysaccharide (LPS) stimulation but not by tumor necrosis factor alpha (TNF-alpha), gamma interferon, interleukin-2 (IL-2), or IL-15 stimulation. Immunocytochemical analysisshowed MKP-M to be present within cytosol. When expressed in COS7 cells, MKP-M blocks activation of mitogen-activated protein kinases with the selectivity c-jun N-terminal kinase (JNK) much greater than p38 = extracellular signal-regulated kinase. Furthermore, expression of a catalytically inactiveform of MKP-M in a mouse macrophage cell line increased the intensity and duration of JNK activation and TNF-alpha secretion after LPS stimulation, suggesting that MKP-M is at least partially responsible for the desensitization of LPS-mediated JNK activation and cytokine secretion in macrophages.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/04/20 alle ore 23:13:49