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Titolo:
Engagement of endogenous ganglioside GM1a induces tyrosine phosphorylationinvolved in neuron-like differentiation of PC12 cells
Autore:
Kimura, M; Hidari, KIPJ; Suzuki, T; Miyamoto, D; Suzuki, Y;
Indirizzi:
Univ Shizuoka Pharmaceut Sci, Dept Biochem, Shizuoka 4228526, Japan Univ Shizuoka Pharmaceut Sci Shizuoka Japan 4228526 zuoka 4228526, Japan
Titolo Testata:
GLYCOBIOLOGY
fascicolo: 4, volume: 11, anno: 2001,
pagine: 335 - 343
SICI:
0959-6658(200104)11:4<335:EOEGGI>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
NERVE GROWTH-FACTOR; CHOLERA-TOXIN; B-SUBUNIT; PROTEIN-KINASES; RAT-BRAIN; COMPLEX GANGLIOSIDES; BOVINE BRAIN; RECEPTOR; DEATH; PREVENTION;
Keywords:
ERK; ganglioside GM1a; PC12 cells; tyrosine phosphorylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Suzuki, Y Univ Shizuoka Pharmaceut Sci, Dept Biochem, 52-1 Yada, Shizuoka 4228526, Japan Univ Shizuoka Pharmaceut Sci 52-1 Yada Shizuoka Japan 4228526 n
Citazione:
M. Kimura et al., "Engagement of endogenous ganglioside GM1a induces tyrosine phosphorylationinvolved in neuron-like differentiation of PC12 cells", GLYCOBIOLOG, 11(4), 2001, pp. 335-343

Abstract

Using the cholera toxin B subunit (CTB) that specifically binds to ganglioside GM1a on the plasma membrane, we investigated intracellular signaling mediated by endogenous GM1a involved in neuronal differentiation of PC12 cells. The treatment with CTB induced morphological alternations of PC12 cells, such as augmentation of the cell body, neurite extension, and branched spikes of tips of neurites. The neurite extension induced with CTB was strongly suppressed by the pretreatment of tyrosine kinase inhibitors in a dose-dependent manner. Western blotting analysis showed that CTB induced tyrosinephosphorylation of several cellular proteins with molecular masses around 120, 70, and 45-40 kDa in PC12 cells. Some of the proteins identified were extra-cellular-signal regulated kinase (ERKs) (ERK1 and ERK2), The peak activation of ERKs lasted for 60-90 min and gradually decreased thereafter. Immunoprecipitation analysis demonstrated that the intracellular events induced with CTB are not related with the activation of Trk proteins, suggesting that signals evoked by ligation of endogenous GM1a are unique and distinct from those induced with exogenous GM1a. Although the presence of a tyrosine kinase inhibitor,, genistein, at a concentration of 10 muM diminished the neurite extension of PC12 cells inducedwith CTB, ERK activation was still observed, However, pretreatment with a MEK inhibitor, PD98059, abolished the activation of ERKs induced with CTB in a dose-dependent manner and only attenuated the morphological alternations of PC12 cells. Considered together, we concluded that tyrosine phorylation induced with CTB was responsible for neuronlike differentiation of PC12 cells and that the MEK-ERK cascade is part of the biological signals mediated by endogenous ganglioside GM1a on PC12 cells.

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Documento generato il 25/01/20 alle ore 06:28:44