Analysis of mechanism and development of regulation approach in liver fibrosis via transglutaminase
| Project/Area Number |
26860500
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Gastroenterology
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| Research Institution | Nagoya University |
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Principal Investigator |
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| Project Period (FY) |
2014-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2015: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2014: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | トランスグルタミナーゼ / タンパク質架橋化酵 / 肝線維化 / 肝硬変 / サイトケラチン18 / タンパク質架橋化酵素 / ALDH2 / Cytokeratin-18 / 線維化 |
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| Outline of Final Research Achievements |
Transglutaminase is a family of enzymes that catalyzes cross-linking reactions among proteins and has been thought to contribute to the fibrotic diseases via crosslinking-mediated stabilization of ECMs and activation of TGF-beta in several tissues such as liver, kidney and lung. Despite these accumulating evidences to implicate transglutaminase as a key enzyme in the fibrosis process, a causative role for the enzyme still has not been established.
We demonstrated that both TG1 and TG2 activities were enhanced in mouse liver fibrosis by bile duct ligation (BDL). To elucidate the detail mechanism by which transglutaminase contributes to the diseases, we identified the several proteins incorporated with biotinylated substrate peptides for TG1 and TG2. Among the identified several substrates, we found that cytokeratin 18 (CK18) was one of crosslinked proteins by both TG1 and TG2 only in mouse liver after the BDL surgery.
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Report
(3 results)
Research Products
(9 results)
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[Journal Article] Biochemical Characterization of Medaka (Oryzias latipes) Transglutaminases, OlTGK1 and OlTGK2, as Orthologues of Human Keratinocyte-Type Transglutaminase.2015
Author(s)
Kikuta A, Furukawa E, Ogawa R, Suganuma N, Saitoh M, Nishimaki T, Katsumura T, Oota H, Kawamoto T, Tatsukawa H, Hashimoto H, Hitomi K.
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Journal Title
PLoS One.
Volume: 10
Issue: 12
Pages: 1-13
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research / Acknowledgement Compliant
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