2001 Fiscal Year Final Research Report Summary
Studies on activating mechanisms oftransglutaminase in epidermis
| Project/Area Number |
12660074
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | Nagoya University |
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Principal Investigator |
HITOMI Kiyotaka Nagoya University GraduateSchool of Bioagricultural Sciences Dept of Applied Biological Sciences, 大学院・生命農学研究科, 助教授 (00202276)
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| Co-Investigator(Kenkyū-buntansha) |
MAKI Masatoshi Nagoya University GraduateSchool of Bioagricultural Sciences Department of Applied Biological Sciences, 大学院・生命農学研究科, 教授 (40183610)
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| Project Period (FY) |
2000 – 2001
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| Keywords | Transglutaminase / Epidermis / Proteasea |
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| Research Abstract |
Transglutaminases catalyze the posttranslational modification of proteins by the formation of isopeptide bond either within or between polypeptide chains. This reaction is calcium ion-dependent found in various tissues and cells from mammals to bacteria. In human, nine isozymes with similar primary structure have been discovered so far. Among them, Tgases 1 and 3 are involved in the formation ofcornified envelop by cross-linking various structural proteins. Both enzymes are synthesized as immature proteins and activated during differentiation. The zymogen form enzymes are limitedly proteolyzed for activation. In this study, using recombinant proteins produced and purified in baculos, the responsible proteases for activation were investigated. In respect to the Tgase 1, calpain could proteolyze zymogen form. The proteolyzed molecule was enhanced at the sensitivity of Ca for transglutaminase activity. Furthermore, we also investigated the tissue distribution of Tgase 3 using RT-POR (reverse transcription polymerase chain reaction). In addition to skin and mouse forestomach, Tgase 3 was expressed also in brain, spleen, and testis.
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Research Products
(10 results)
