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dc.contributor.author | Inouye, Kuniyo | en |
dc.contributor.author | Yasumoto, Makoto | en |
dc.contributor.author | Tsuzuki, Satoshi | en |
dc.contributor.author | Mochida, Seiya | en |
dc.contributor.author | Fushiki, Tohru | en |
dc.contributor.alternative | 井上, 國世 | ja |
dc.date.accessioned | 2010-10-18T08:03:42Z | - |
dc.date.available | 2010-10-18T08:03:42Z | - |
dc.date.issued | 2010-04 | - |
dc.identifier.issn | 0021-924X | - |
dc.identifier.uri | http://hdl.handle.net/2433/128777 | - |
dc.description.abstract | Matriptase is a transmembrane serine protease that is strongly expressed in epithelial cells. The single-chain zymogen of matriptase is considered to have inherent activity, leading to its own activation (i.e. conversion to the disulphide-linked-two-chain form by cleavage after Thr-Lys-Gln-Ala-Arg614). Also, there is growing evidence that the activation of zymogen occurs at the cell surface and in relation to the acidification and lowering of ionic strength within cell-surface microenvironments. The present study aimed to provide evidence for the involvement of zymogen activity in its activation in physiologically relevant cellular contexts. For this purpose, the activity of a pseudozymogen form of recombinant matriptase (HL-matriptase zymogen) was examined using acetyl-l-Lys-l-Thr-l-Lys-l-Gln-l-Leu-l-Arg-4-methyl-coumaryl-7-amide as a substrate. HL-matriptase zymogen exhibited optimal activity toward the substrate pH approximately 6.0. The substrate hydrolysis at the pH value was hardly detected when NaCl was present at a concentration of 145 mM. In a buffer of pH 6.0 containing 5 mM NaCl, the activity of HL-matriptase zymogen was only approximately 30-times lower than that of the respective two-chain form. These findings suggest that the in vivo activation of matriptase zymogen occurs via a mechanism involving the zymogen activity. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Oxford University Press on behalf of the Japanese Biochemical Society | en |
dc.rights | © The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. | en |
dc.rights | この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 | ja |
dc.rights | This is not the published version. Please cite only the published version. | en |
dc.subject.mesh | Amino Acid Chloromethyl Ketones/metabolism | en |
dc.subject.mesh | Amino Acid Motifs | en |
dc.subject.mesh | Animals | en |
dc.subject.mesh | Enteropeptidase | en |
dc.subject.mesh | Enzyme Activation | en |
dc.subject.mesh | Enzyme Precursors/chemistry | en |
dc.subject.mesh | Enzyme Precursors/genetics | en |
dc.subject.mesh | Enzyme Precursors/metabolism | en |
dc.subject.mesh | Hydrogen-Ion Concentration | en |
dc.subject.mesh | Kinetics | en |
dc.subject.mesh | Muscle Hypotonia | en |
dc.subject.mesh | Oligopeptides/chemistry | en |
dc.subject.mesh | Oligopeptides/metabolism | en |
dc.subject.mesh | Osmolar Concentration | en |
dc.subject.mesh | Protein Structure, Tertiary | en |
dc.subject.mesh | Rats | en |
dc.subject.mesh | Recombinant Fusion Proteins/chemistry | en |
dc.subject.mesh | Recombinant Fusion Proteins/metabolism | en |
dc.subject.mesh | Serine Endopeptidases/chemistry | en |
dc.subject.mesh | Serine Endopeptidases/genetics | en |
dc.subject.mesh | Serine Endopeptidases/metabolism | en |
dc.subject.mesh | Substrate Specificity | en |
dc.title | The optimal activity of a pseudozymogen form of recombinant matriptase under the mildly acidic pH and low ionic strength conditions. | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.ncid | AA00694073 | - |
dc.identifier.jtitle | Journal of biochemistry | en |
dc.identifier.volume | 147 | - |
dc.identifier.issue | 4 | - |
dc.identifier.spage | 485 | - |
dc.identifier.epage | 492 | - |
dc.relation.doi | 10.1093/jb/mvp190 | - |
dc.textversion | author | - |
dc.identifier.pmid | 19919953 | - |
dcterms.accessRights | open access | - |
出現コレクション: | 学術雑誌掲載論文等 |
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