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EnglishThe 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
http://hdl.handle.net/2158/310704| Titolo: | An inward rectifier K+current modulates in neuroblastoma cells tyrosine phosphorylation of pp125 FAK and associated proteins: role in neuritogenesis. |
| Autori di Ateneo: | |
| Autori: | L. BIANCHI; ARCANGELI, ANNAROSA; P. BARTOLINI; MUGNAI, GABRIELE; E. WANKE; OLIVOTTO, MASSIMO |
| Anno di registrazione: | 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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