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Titolo:
Mitotic aberrations induced by carbaryl reflect tyrosine kinase inhibitionwith coincident up-regulation of serine threonine protein phosphatase activity: implications for coordination of karyokinesis and cytokinesis
Autore:
Renglin, A; Harmala-Brasken, AS; Eriksson, JE; Onfelt, A;
Indirizzi:
Univ Stockholm, Wallenberg Lab, S-10691 Stockholm, Sweden Univ Stockholm Stockholm Sweden S-10691 g Lab, S-10691 Stockholm, Sweden Abo Akad Univ, Turku Ctr Biotechnol, Turku, Finland Abo Akad Univ Turku Finland Univ, Turku Ctr Biotechnol, Turku, Finland Turku Univ, Turku, Finland Turku Univ Turku FinlandTurku Univ, Turku, Finland Abo Akad Univ, Dept Biochem & Pharm, FIN-20520 Turku, Finland Abo Akad Univ Turku Finland FIN-20520 & Pharm, FIN-20520 Turku, Finland
Titolo Testata:
MUTAGENESIS
fascicolo: 3, volume: 14, anno: 1999,
pagine: 327 - 333
SICI:
0267-8357(199905)14:3<327:MAIBCR>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHINESE-HAMSTER CELLS; SISTER CHROMATID SEPARATION; MAMMALIAN-CELLS; SPINDLE DISTURBANCES; OKADAIC ACID; MICROTUBULE DYNAMICS; PHOSPHORYLATION; MITOSIS; INDUCTION; MICROINJECTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Onfelt, A Univ Stockholm, Wallenberg Lab, S-10691 Stockholm, Sweden Univ Stockholm Stockholm Sweden S-10691 0691 Stockholm, Sweden
Citazione:
A. Renglin et al., "Mitotic aberrations induced by carbaryl reflect tyrosine kinase inhibitionwith coincident up-regulation of serine threonine protein phosphatase activity: implications for coordination of karyokinesis and cytokinesis", MUTAGENESIS, 14(3), 1999, pp. 327-333

Abstract

The insecticide carbaryl and its metabolite 1-naphthol cause partial uncoupling of karyokinesis and cytokinesis in V79 Chinese hamster fibroblasts; karyokinesis is blocked in metaphase, the microtubules of the spindle depolymerize and the chromosomes and spindle remnants become displaced to the periphery of the cell. A high frequency of these disturbed cells elongate and a smaller fraction initiate a cleavage furrow. Here, we attempt to determine the potential targets for carbaryl and 1-naphthol in cytokinesis-specificsignalling, led by the fact that the potential protein phosphatase inhibitor 1-naphthyl phosphate was previously identified in treated cells. We found that the typical cytological pattern induced by carbaryl and 1-naphthol could be obtained with tyrphostins, specific tyrosine kinase inhibitors, indicating that the carbaryl-induced effects could be due to tyrosine kinase inhibition. This was confirmed by tyrosine kinase assays showing that carbaryl, 1-naphthol and 2-naphthol were equally efficient at inhibiting tyrosinekinase activity as tyrphostin B44(-). As tyrosine kinases can act as regulatory factors in determining dephosphorylation rates, the activities of type-1 (PP1) and type-2A (PP2A) serine/threonine protein phosphatases were also determined. There was a clear up-regulation of the overall PP1/PP2A activities in cells treated with carbaryl, 1-naphthol or tyrphostin B44(-), Thisstimulation was shown to be indirect because these compounds had no effecton the activity of purified human PP1 in the test tube. 2-Naphthol, which has been found to be less efficient with regard to displacement of chromatin, did not cause up-regulation, but a significant decrease in PP1/PP2A activity. We suggest that a net decrease in tyrosine kinase activity in combination with a net increase in PP1/PP2A activity is a precondition for cell elongation and cytokinesis in mammalian cells and that the corresponding enzymes are targets in the network of activities serving to coordinate karyokinesis and cytokinesis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 12:33:41