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Titolo:
PURIFICATION AND IDENTIFICATION OF A MAJOR ACTIVATOR FOR P38 FROM OSMOTICALLY SHOCKED CELLS - ACTIVATION OF MITOGEN-ACTIVATED PROTEIN-KINASE-6 BY OSMOTIC SHOCK, TUMOR-NECROSIS-FACTOR-ALPHA, AND H2O2
Autore:
MORIGUCHI T; TOYOSHIMA F; GOTOH Y; IWAMATSU A; IRIE K; MORI E; KUROYANAGI N; HAGIWARA M; MATSUMOTO K; NISHIDA E;
Indirizzi:
KYOTO UNIV,INST VIRUS RES,DEPT MOL BIOL & GENET,SAKYO KU KYOTO 60601 JAPAN KYOTO UNIV,INST VIRUS RES,DEPT MOL BIOL & GENET,SAKYO KU KYOTO 60601 JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL,KANAZAWA KU YOKOHAMA KANAGAWA 236 JAPAN NAGOYA UNIV,FAC SCI,DEPT MOL BIOL,CHIKUSA KU NAGOYA AICHI 46401 JAPAN NAGOYA UNIV,SCH MED,DEPT ANAT,SHOWA KU NAGOYA AICHI 466 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 43, volume: 271, anno: 1996,
pagine: 26981 - 26988
SICI:
0021-9258(1996)271:43<26981:PAIOAM>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
SIGNAL-TRANSDUCTION PATHWAY; C-JUN; MAMMALIAN-CELLS; HEAT-SHOCK; STRESS; PHOSPHORYLATION; YEAST; CASCADE; THREONINE; TYROSINE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
T. Moriguchi et al., "PURIFICATION AND IDENTIFICATION OF A MAJOR ACTIVATOR FOR P38 FROM OSMOTICALLY SHOCKED CELLS - ACTIVATION OF MITOGEN-ACTIVATED PROTEIN-KINASE-6 BY OSMOTIC SHOCK, TUMOR-NECROSIS-FACTOR-ALPHA, AND H2O2", The Journal of biological chemistry, 271(43), 1996, pp. 26981-26988

Abstract

A stress-activated, serine/threonine kinase, p38 (also known as HOG1 or MPK2) belongs to a subgroup of mitogen-activated protein kinase (MAPK) superfamily molecules, An activity to activate p38 (p38 activator activity) as well as p38 activity itself were greatly stimulated by hyperosmolar media in mouse lymphoma L5178Y cells, The activator activity has been purified by sequential chromatography. A 36-kDa polypeptidethat was coeluted with the activity in the final chromatography step was identified as MAPK kinase 6 (MAPKK6) by protein microsequencing analysis, Monoclonal and polyclonal antibodies raised against recombinant MAPKK6 recognized specifically the 36-kDa MAPKK6 protein but did notcross react with MKK3 proteins. The use of these anti-MAPKK6 antibodies revealed that two major peaks of the p38 activator activity in the first chromatography step reside in the activated MAPKK6, Using a genetic screen in yeast, we isolated MKK3b, an alternatively spliced form of MKK3. Like MKK3 and MAPKK6, MKK3b was shown to be a specific activator for p38 and was activated by osmotic shock when expressed in COS7 cells, Immunoblotting analysis revealed that MAPKK6 is expressed highly in HeLa and KB cells and scarcely in PC12 cells, whereas MKK3 and MKK3b are expressed in all cells examined, Immunodepletion of MAPKK6 from the extracts obtained from L5178Y cells and KB cells exposed to hyperosmolar media depleted them of almost all of the p38 activator activity, indicating that MAPKK6 is a major activator for p38 in an osmosensing pathway in these cells. In addition, MAPKK6 was activated stronglyby tumor necrosis factor-alpha, H2O2, and okadaic acid and moderatelyby cycloheximide in KB cells. Thus, there are at least three members of p38 activator, MKK3, MKK3b, and MAPKK6, and MAPKK6 may function as a major activator for p38 when expressed.

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Documento generato il 23/01/21 alle ore 03:40:54