Literature DB >> 1720736

Seizure-induced protein tyrosine phosphorylation in rat brain regions.

R S Jope1, G V Johnson, M S Baird.   

Abstract

Phosphorylation of protein tyrosines is an important modulatory process for cell signaling and other cellular functions. Rat brain regions were examined for altered protein phosphotyrosines, using Western blot analysis and microwave irradiation to limit postmortem alterations, after administration of two convulsants: lithium plus pilocarpine or kainic acid (KA). Most phosphotyrosine proteins were unaltered by these treatments, but there was a large, specific increase in the tyrosine phosphorylation of a 40-Kd protein. This increase was evident in all three regions examined: cerebral cortex, hippocampus, and striatum; it occurred abruptly with onset of generalized status epilepticus (SE) and remained elevated for at least 90 min. Most of the tyrosine phosphorylated 40-Kd protein was in the cytosolic fraction. These results demonstrate a large, specific effect of chemically induced seizures on a single phosphotyrosine protein in rat brain.

Entities:  

Mesh:

Substances:

Year:  1991        PMID: 1720736     DOI: 10.1111/j.1528-1157.1991.tb05530.x

Source DB:  PubMed          Journal:  Epilepsia        ISSN: 0013-9580            Impact factor:   5.864


  1 in total

1.  Anesthesia and post-mortem interval profoundly influence the regulatory serine phosphorylation of glycogen synthase kinase-3 in mouse brain.

Authors:  Xiaohua Li; Ari B Friedman; Myoung-Sun Roh; Richard S Jope
Journal:  J Neurochem       Date:  2005-02       Impact factor: 5.372

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.