http://purl.uniprot.org/citations/17646163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17646163 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17646163 | http://www.w3.org/2000/01/rdf-schema#comment | "Calpains constitute a family of intracellular Ca(2+)-regulated cysteine proteases that are indispensable in the regulation of a wide variety of cellular functions. The improper activation of calpain causes lethality or various disorders, such as muscular dystrophies and tumor formation. nCL-2/calpain 8 is predominantly expressed in the stomach, where it appears to be involved in membrane trafficking in the gastric surface mucus cells (pit cells). Although the primary structure of nCL-2 is quite similar to that of the ubiquitous m-calpain large subunit, the enzymatic properties of nCL-2 have never been reported. Here, to characterize nCL-2, the recombinant protein was prepared using an Escherichia coli expression system and purified to homogeneity. nCL-2 was stably produced as a soluble and active enzyme without the conventional calpain regulatory subunit (30K). Purified nCL-2 showed Ca(2+)-dependent activity, with half-maximal activity at about 0.3 mM Ca(2+), similar to that of m-calpain, whereas its optimal pH and temperature were comparatively low. Immunoprecipitation analysis revealed that nCL-2 exists in both monomeric and homo-oligomeric forms, but not as a heterodimer with 30K or 30K-2, and that the oligomerization occurs through domains other than the 5EF-hand domain IV, most probably through domain III, suggesting a novel regulatory system for nCL-2."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m703168200"xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m703168200"xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/author | "Hata S."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/author | "Hata S."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/author | "Doi N."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/author | "Doi N."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/author | "Sorimachi H."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/author | "Sorimachi H."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/author | "Kitamura F."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/author | "Kitamura F."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/pages | "27847-27856"xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/pages | "27847-27856"xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/title | "Stomach-specific calpain, nCL-2/calpain 8, is active without calpain regulatory subunit and oligomerizes through C2-like domains."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/title | "Stomach-specific calpain, nCL-2/calpain 8, is active without calpain regulatory subunit and oligomerizes through C2-like domains."xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/volume | "282"xsd:string |
http://purl.uniprot.org/citations/17646163 | http://purl.uniprot.org/core/volume | "282"xsd:string |
http://purl.uniprot.org/citations/17646163 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17646163 |
http://purl.uniprot.org/citations/17646163 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17646163 |