An inward rectifier K+current modulates in neuroblastoma cells tyrosine phosphorylation of pp125 FAK and associated proteins: role in neuritogenesis.

Bianchi, L.; Arcangeli, Annarosa; Bartolini, P.; Mugnai, Gabriele; Wanke, E.; Olivotto, Massimo

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The relationships between the integrin-mediated activation of inward rectifyier K+ channels (KIR), the phosphorylation of pp125FAK and the rescue of neuritogenesis were studied in 41A3 mouse neuroblastoma cells. Neuritogenesis, elicited by adhesion to FN-enriched substrata, was reversibly impaired by pretreating these cells with the tyrosine kinase inhibitor Herbimycin A. This impairment mimicked that operated by Cs+ ions, which selectively inhibited the integrin-mediated activation of KIR channels. Various phosphotyrosine containing cellular proteins underwent a marked increase upon cell adhesion to FN-coated dishes. This increase was significantly reduced by Cs+ addition. Immunoprecipitation of pp125FAK revealed that the phosphorylation of this kinase and several associated proteins was significantly and reversibly inhibited by Cs+, indicating that integrin-mediated activation of KIR channels is a limiting step upstream to the phosphorylation of pp125FAK in the commitment to neuritogenesis

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Titolo:	An inward rectifier K+current modulates in neuroblastoma cells tyrosine phosphorylation of pp125 FAK and associated proteins: role in neuritogenesis.
Autori di Ateneo:	L. BIANCHI ARCANGELI, ANNAROSA P. BARTOLINI MUGNAI, GABRIELE E. WANKE OLIVOTTO, MASSIMO mostra contributor esterni nascondi contributor esterni
Autori:	L. BIANCHI; ARCANGELI, ANNAROSA; P. BARTOLINI; MUGNAI, GABRIELE; E. WANKE; OLIVOTTO, MASSIMO
Data di pubblicazione:	1995
Rivista:	BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume:	210
Pagina iniziale:	823
Pagina finale:	829
Abstract:	The relationships between the integrin-mediated activation of inward rectifyier K+ channels (KIR), the phosphorylation of pp125FAK and the rescue of neuritogenesis were studied in 41A3 mouse neuroblastoma cells. Neuritogenesis, elicited by adhesion to FN-enriched substrata, was reversibly impaired by pretreating these cells with the tyrosine kinase inhibitor Herbimycin A. This impairment mimicked that operated by Cs+ ions, which selectively inhibited the integrin-mediated activation of KIR channels. Various phosphotyrosine containing cellular proteins underwent a marked increase upon cell adhesion to FN-coated dishes. This increase was significantly reduced by Cs+ addition. Immunoprecipitation of pp125FAK revealed that the phosphorylation of this kinase and several associated proteins was significantly and reversibly inhibited by Cs+, indicating that integrin-mediated activation of KIR channels is a limiting step upstream to the phosphorylation of pp125FAK in the commitment to neuritogenesis
Handle:	http://hdl.handle.net/2158/310704
Appare nelle tipologie:	1a - Articolo su rivista

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