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Titolo:
Toxins affecting cell signalling and alteration of cytoskeletal structure
Autore:
Toivola, DM; Eriksson, JE;
Indirizzi:
Vet Adm Palo Alto Hlth Care Syst, Div Gastroenterol, Palo Alto, CA 94305 USA Vet Adm Palo Alto Hlth Care Syst Palo Alto CA USA 94305 lto, CA 94305 USA Stanford Univ, Sch Med, Palo Alto, CA 94305 USA Stanford Univ Palo Alto CA USA 94305 iv, Sch Med, Palo Alto, CA 94305 USA Turku Ctr Biotechnol, FIN-20521 Turku, Finland Turku Ctr Biotechnol Turku Finland FIN-20521 l, FIN-20521 Turku, Finland
Titolo Testata:
TOXICOLOGY IN VITRO
fascicolo: 4-5, volume: 13, anno: 1999,
pagine: 521 - 530
SICI:
0887-2333(199908/10)13:4-5<521:TACSAA>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
THREONINE PROTEIN PHOSPHATASES; CYCLIC PEPTIDE TOXIN; KERATIN INTERMEDIATE FILAMENTS; ISOLATED RAT HEPATOCYTES; MICROCYSTIN-LR; OKADAIC ACID; CATALYTIC SUBUNIT; TUMOR PROMOTION; CALYCULIN-A; IN-VIVO;
Keywords:
microcystin; protein phosphatase inhibitor; cytoskeleton; keratin; liver toxicity; algal toxin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
86
Recensione:
Indirizzi per estratti:
Indirizzo: Toivola, DM Vet Adm Palo Alto Hlth Care Syst, Div Gastroenterol, Palo Alto, CA 94305 USA Vet Adm Palo Alto Hlth Care Syst Palo Alto CA USA 94305 5 USA
Citazione:
D.M. Toivola e J.E. Eriksson, "Toxins affecting cell signalling and alteration of cytoskeletal structure", TOX VITRO, 13(4-5), 1999, pp. 521-530

Abstract

Many natural toxins act by modifying key functions of the phosphorylation-based signalling machinery. Microcystins comprise a good example of highly specific, signalling-targeted toxicants. These liver-specific cyanobacterial peptide toxins act as potent inhibitors of serine:threonine (ser:thr) protein phosphatases, in particular type-1 (PPI) and type-2A (PP2A). PP1 and PP2A regulate the phosphorylation of a large number of key elements in various signalling processes. Furthermore, they are crucial in maintaining cytoskeletal integrity. Consequently, microcystins disrupt the liver structure by abrogating cytoskeletal regulation. Microcystin-induced protein phosphatase inhibition in liver cells leads to rapid reorganization of all three major cytoskeletal components, microfilaments, microtubules and intermediate filaments (IFs). The inhibited dephosphorylation induces an especially marked phosphorylation of the liver IF proteins, keratins 8 and 18. The elevatedphosphorylation of these proteins causes disassembly and reorganization ofkeratin filaments, indicating that their assembly state iii vivo is regulated by a continuous phosphate turnover. In this review on microcystin-induced cellular effects, we attempt to illustrate the potentially grave consequences when phosphorylation processes are disturbed by toxicants. The aim isalso to show how such signalling-targeted toxicants can be used as biochemical tools to establish the biological roles of specific signalling or regulatory processes. (C) 1999 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 09:00:55