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Titolo:
Integrins stimulate phosphorylation of neurofilament NF-M subunit KSP repeats through activation of extracellular regulated-kinases (Erk1/Erk2) in cultured motoneurons and transfected NIH 3T3 cells
Autore:
Li, BS; Daniels, MP; Pant, HC;
Indirizzi:
NINDS, Neurochem Lab, NIH, Bethesda, MD 20892 USA NINDS Bethesda MD USA 20892 S, Neurochem Lab, NIH, Bethesda, MD 20892 USA NHLBI, Lab Biochem Genet, NIH, Bethesda, MD USA NHLBI Bethesda MD USANHLBI, Lab Biochem Genet, NIH, Bethesda, MD USA
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 3, volume: 76, anno: 2001,
pagine: 703 - 710
SICI:
0022-3042(200102)76:3<703:ISPONN>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASES; SIGNAL-TRANSDUCTION; NEURITE OUTGROWTH; PERIPHERAL-NERVE; SPINAL-CORD; MAMMALIAN NEUROFILAMENTS; ADHESION MOLECULES; AXONAL-TRANSPORT; GROWTH-FACTOR; TAIL DOMAIN;
Keywords:
fibronectin; integrin; laminin; MAPK; motoneuron; neurofilament;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Pant, HC NINDS, Neurochem Lab, NIH, Bldg 36,Rm 4D20,9000 Rockville Pike, Bethesda, MD 20892 USA NINDS Bldg 36,Rm 4D20,9000 Rockville Pike Bethesda MDUSA 20892 A
Citazione:
B.S. Li et al., "Integrins stimulate phosphorylation of neurofilament NF-M subunit KSP repeats through activation of extracellular regulated-kinases (Erk1/Erk2) in cultured motoneurons and transfected NIH 3T3 cells", J NEUROCHEM, 76(3), 2001, pp. 703-710

Abstract

Integrin-mediated interactions of cells with components of the extracellular matrix (ECM) regulate cell survival, cell proliferation, cell differentiation and cell migration through activation of multiple intracellular signal transduction pathways. In this study, we have demonstrated that integrin-matrix interactions promote KSP tail-domain phosphorylation of neurofilament medium molecular weight subunits (NF-M)in cultured rat spinal cord motoneurons and NF-M transfected NIH 3T3 cells. We found that laminin and fibronectin induce NF-M tail-domain phosphorylation in motoneurons and NIH 3T3 cells transfected with NF-M, respectively. This phosphorylation was selectively inhibited by PD98059, a specific MEK1 inhibitor. This suggests that laminin and fibronectin-induced MEK1 activation and the downstream targets Erk1 and Erk2 are involved in NF-M KSP tail-domain phosphorylation. This pathwayappears to represent one of the mechanisms whereby integrin-extracellular matrix interactions are involved in phosphorylation of the NF-M KSP tail domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 08:37:33