|
|
Hokkaido University Collection of Scholarly and Academic Papers >
Faculty of Pharmaceutical Sciences >
Peer-reviewed Journal Articles, etc >
Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes the β-subunit of coatomer complex, β-COP
| Title: | Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes the β-subunit of coatomer complex, β-COP |
| Authors: | Hata, Shoji Browse this author | | Koyama, Suguru Browse this author | | Kawahara, Hiroyuki Browse this author | | Doi, Naoko Browse this author | | Maeda, Tatsuya Browse this author | | Toyama-Sorimachi, Noriko Browse this author | | Abe, Keiko Browse this author | | Suzuki, Koichi Browse this author | | Sorimachi, Hiroyuki Browse this author |
| Keywords: | tissue-specific caplain | | musscle-specific calpain | | cysteine protease | | crystal-structure | | appendage domain | | saccharomyces-cerevisiae | | active-site | | in-vivo | | gene |
| Issue Date: | 21-Apr-2006 |
| Publisher: | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY |
| Journal Title: | Journal of biological chemistry |
| Volume: | 281 |
| Issue: | 16 |
| Start Page: | 11214 |
| End Page: | 11224 |
| Publisher DOI: | 10.1074/jbc.M509244200 |
| Abstract: | Calpain is a Ca2+-regulated cytosolic protease. Mammals have 14 calpain genes, half of which are predominantly expressed in specific organ(s); the rest are expressed ubiquitously. A defect in calpains causes lethality/pathogenicity, indicating their physiological indispensability. nCL-2/calpain-8a was identified as a stomach-specific calpain, whose physiological functions are unclear. To elucidate these, we characterized nCL-2 in detail. Unexpectedly, nCL-2 was localized strictly to the surface mucus cells in the gastric epithelium and the mucus-secreting goblet cells in the duodenum. Yeast two-hybrid screening identified several nCL-2-intracting molecules. Of these, the -subunit of coatomer complex (-COP) occurs in the stomach pit cells and is proteolyzed by nCL-2 in vitro. Furthermore, -COP and nCL-2 co-expressed in COS7 cells co-localized in the Golgi, and Ca2+-ionophore stimulation caused the proteolysis of -COP near the linker region, resulting in the dissociation of -COP from the Golgi. These results strongly suggest novel functions for nCL-2 that involve the membrane trafficking of mucus cells via interactions with coat protein. |
| Rights: | Copyright(c)2006 by the American Society for Biochemistry and Molecular Biology |
| Relation: | http://www.jbc.org/ |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/8516 |
| Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
Submitter: 川原 裕之
|
