Extracellular proteases in epilepsy.

Abstract

During the last decade, multiple data have been obtained, pointing to an involvement of extracellular, including extrasynaptic, proteolysis in epilepsy pathogenesis. The most productive avenues of investigations have been analyses of seizure-evoked gene and protein expression patterns, both hypothesis-driven and unbiased (e.g., DNA microarrays), complemented by functional analyses in animal models, as well as expression and gene polymorphism studies carried out on human tissue In result, serine proteases (e.g., tPA, thrombin, trypsin-like proteases, etc.), metalloproteinases, natural protease inhibitors, as well as complement components, and reelin have been identified as a novel molecular system, emerging as a key factor in the development of epilepsy, in addition to well known contribution of ion channels and signal transduction pathways. The extracellular location of the enzymes makes them particularly attractive potential targets for future pharmacological therapeutic interventions.

• Authors: Katarzyna Lukasiuk, Grzegorz M Wilczynski, Leszek Kaczmarek
• Journal: Epilepsy research (Epilepsy Res) Vol. 96 Issue 3 Pg. 191-206 (Oct 2011) ISSN: 1872-6844 [Electronic] Netherlands
• PMID: 21893397 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
• Copyright: Copyright © 2011 Elsevier B.V. All rights reserved.

Chemical References

• Ion Channels
• Reelin Protein
• Peptide Hydrolases
• RELN protein, human

Topics

• Animals
• Cell Membrane (enzymology)
• Epilepsy (enzymology, pathology)
• Extracellular Space (metabolism)
• Humans
• Ion Channels (metabolism)
• Peptide Hydrolases (metabolism)
• Reelin Protein
• Signal Transduction (physiology)