Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Protein phosphatase 2A inhibitors, phoslactomycins. Effects on the cytoskeleton in NIH/3T3 cells
Autore:
Usui, T; Marriott, G; Inagaki, M; Swarup, G; Osada, H;
Indirizzi:
RIKEN, Inst Phys & Chem Res, Antibiot Lab, Wako, Saitama 3510198, Japan RIKEN Wako Saitama Japan 3510198 tibiot Lab, Wako, Saitama 3510198, Japan Aichi Canc Ctr, Res Inst, Dept Biochem, Aichi, Japan Aichi Canc Ctr Aichi Japan nc Ctr, Res Inst, Dept Biochem, Aichi, Japan Max Planck Inst Biochem, D-8000 Munich, Germany Max Planck Inst Biochem Munich Germany D-8000 em, D-8000 Munich, Germany Ctr Cellular & Mol Biol, Hyderabad 500007, Andhra Pradesh, India Ctr Cellular & Mol Biol Hyderabad Andhra Pradesh India 500007 desh, India
Titolo Testata:
JOURNAL OF BIOCHEMISTRY
fascicolo: 5, volume: 125, anno: 1999,
pagine: 960 - 965
SICI:
0021-924X(199905)125:5<960:PP2IPE>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANTIFUNGAL ANTIBIOTICS PHOSLACTOMYCINS; COLONY-STIMULATING FACTORS; FAMILY INDUCE PRODUCTION; MARROW STROMAL CELLS; ACTIN POLYMERIZATION; OKADAIC ACID; MICROBIAL METABOLITES; TYROSINE-PHOSPHATASE; CALYCULIN-A; HEAD DOMAIN;
Keywords:
actin; protein phosphatase 1; protein phosphatase 2A; site-specific phosphorylated antibodies; vimentin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Osada, H RIKEN,198,t Phys & Chem Res, Antibiot Lab, Hirosawa 2-1, Wako, Saitama 3510 RIKEN Hirosawa 2-1 Wako Saitama Japan 3510198 Wako, Saitama 3510
Citazione:
T. Usui et al., "Protein phosphatase 2A inhibitors, phoslactomycins. Effects on the cytoskeleton in NIH/3T3 cells", J BIOCHEM, 125(5), 1999, pp. 960-965

Abstract

Protein phosphorylation is a key regulatory mechanism of the organization and dynamics of the actin cytoskeleton during cell motility, differentiation, and cytokinesis. The level of protein phosphorylation is dependent on the relative activities of both protein kinases and protein phosphatases, In this paper, we examined the effect of phoslactomycins (PLMs) on the regulation of the cytoskeleton of NIH/3T3 fibroblasts. Treatment of cells with PLM-F (10 mu M) induced actin filament depolymerization after 4 h, This effectwas reversible and actin filaments were reformed 1 h after removal of the inhibitors. lis PLM-F had no effect at all on polymerization of purified actin in vitro, it is thought that PLMs induce actin depolymerization throughan indirect mechanism. An in vitro assay showed PLMs inhibited protein phosphatase 2A at lower concentrations (IC50 4.7 mu M) than protein phosphatase 1, An in situ phosphorylation assay also revealed that PLM-F treatment stimulated the phosphorylation of intracellular vimentin, These results suggest that phoslactomycins are protein phosphatase 2A-specific inhibitors and that protein phosphatase 2A is involved in regulation of the organization of the actin cytoskeleton.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 16:10:50