Glutamate activates PP125<sup>FAK</sup> through AMPA/kainate receptors in Bergmann glia
作者: Alejandro MillánPablo AguilarJ. Alfredo MéndezJosé‐Antonio Arias‐MontañoArturo Ortega
作者单位: 1Departamento de Genética y Biología Molecular, Cinvestav‐IPN, México City, Mexico México City, Mexico
2 Departamento de Fisiología, Biofísica y Neurociencias, Cinvestav‐IPN, México City, Mexico
3 Depto. Genética y Biología Molecular, Cinvestav‐IPN, Apartado Postal 14‐740, México D.F. 07000, Mexico
刊名: Journal of Neuroscience Research, 2001, Vol.66 (4), pp.723-729
来源数据库: Wiley Journal
DOI: 10.1002/jnr.10034
关键词: signal transductionfocal adhesion kinaseBergmann gliaglutamate receptors
原始语种摘要: Abstract(#br)Glial glutamate receptors are likely to play a role in plasticity, learning, and memory and in a number of neuropathologies. An enhanced glutamate‐dependent tyrosine phosphorylation has been detected in such processes. Using primary cultures of chick Bergmann glia cells and chick cerebellar slices, we addressed whether glial glutamate receptors can activate the nonreceptor tyrosine kinase pp125 focal adhesion kinase (pp125FAK). A dose‐ and time‐dependent tyrosine phosphorylation of pp125FAK was found in both preparations upon glutamate treatment. This effect was mediated through α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoaxazolepropionate (AMPA)/kainate (KA) receptors, as shown by its inhibition by the specific antagonists...
全文获取路径: Wiley  (合作)

  • sup 吃晚饭
  • adhesion 粘附
  • glutamate 谷氨酸盐酯或根
  • glial 神经胶质的
  • kinase 激酶
  • focal 焦点的
  • transduction 转导
  • ionotropic 离子移变的
  • tyrosine 酪氨酸
  • chick 雏鸡