N-Methyl-D-aspartate (NMDA) at a subtoxic concentration (100 mM) promotes neuronal survival against glutamate-mediated excitotoxicity via a brain-derived neurotrophic factor (BDNF) autocrine loop in cultured cerebellar granule cells. The signal transduction mechanism(s) underlying NMDA neuroprotecti
Transcriptional regulation through glutamate receptors: Involvement of tyrosine kinases
✍ Scribed by Esther López-Bayghen; Adán Aguirre; Arturo Ortega
- Publisher
- John Wiley and Sons
- Year
- 2003
- Tongue
- English
- Weight
- 340 KB
- Volume
- 74
- Category
- Article
- ISSN
- 0360-4012
No coin nor oath required. For personal study only.
✦ Synopsis
Glutamate receptors play a key role in neuronal plasticity, learning and memory, and in several neuropathologies. Short-term and long-term changes in synaptic efficacy are triggered by glutamate. Although an enhanced glutamate-dependent tyrosine phosphorylation has been described in several systems, its role in membrane-to-nuclei signaling is unclear. Taking advantage of the fact that the gene encoding the chick kainate-binding protein undergoes a glutamate-dependent transcriptional regulation via an activator protein-1 (AP-1) site, we evaluated the involvement of tyrosine kinases in this process. We describe here the participation of receptor and non-receptor tyrosine kinases in the signaling cascade triggered by glutamate. Our results suggest that in Bergmann glia cells, glutamate receptors transactivate receptor tyrosine kinases, favoring the idea of a complex network of signals activated by this excitatory neurotransmitter that results in regulation of gene expression.
📜 SIMILAR VOLUMES
## Abstract We previously identified functional __N__‐methyl‐d‐aspartate (NMDA) glutamate receptors in mature osteoclasts and demonstrated that they are involved in bone resorption in vitro. In the present work, we studied the expression of NMDA receptors (NMDAR) by osteoclast precursors and their
## Abstract The tyrosine kinase Syk is associated with CD18, the β‐subunit of the leukocyte adhesion molecules of the β~2~ integrin family (CD11/CD18), and becomes activated upon β~2~ integrin‐mediated adhesion. In this study, we elucidated the role of Syk in polarization and site‐directed migratio
## Abstract The discoidin domain receptor 1 (DDR1) is a receptor tyrosine kinase that is highly expressed in breast carcinoma cells. Upon binding to collagen, DDR1 undergoes autophosphorylation followed by limited proteolysis to generate a tyrosine phosphorylated C‐terminal fragment (CTF). Although
## Abstract By using pharmacological and molecular approaches, we previously showed that the G‐protein‐coupled, extracellular calcium (Ca)‐sensing receptor (CaR) regulates a large‐conductance (∼140 pS), Ca^2+^‐activated K^+^ channel [I~K(Ca)~; CAKC] in U87 astrocytoma cells. Here we show that eleva