title: 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: Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur St, 02-093 Warsaw, Poland. k.lukasiuk@nencki.gov.pl
authors: Katarzyna
authors: K
authors: Lukasiuk
authors: Grzegorz M
authors: GM
authors: Wilczynski
authors: Leszek
authors: L
authors: Kaczmarek
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000201:enzymology*; D004827:Epilepsy / Q000201:enzymology* / Q000473:pathology; D005110:Extracellular Space / Q000378:metabolism*; D006801:Humans; D007473:Ion Channels / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D000091042:Reelin Protein; D015398:Signal Transduction / Q000502:physiology*
chemical_list: D007473:Ion Channels; D000091042:Reelin Protein; D010447:Peptide Hydrolases; C000717127:RELN protein, human