2000 Fiscal Year Final Research Report Summary
Trappins, a new family of proteins that have an anchoring sequence-Localization, function, and evolution
| Project/Area Number |
09680615
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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 |
Functional biochemistry
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| Research Institution | TOKYO INSTITUTE OF TECHNOLOGY |
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Principal Investigator |
YOKO Suzuki Tokyo Institute of Technology Graduate School of Bioscience and Biotechnology Research Assistant Professor, 大学院・生命理工学研究科, 教務職員 (30179270)
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| Project Period (FY) |
1997 – 2000
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| Keywords | Crosslinking / Transglutaminase / Trappin / Cementoin / Elafin / Gene conversion / Evolution / Proteinase inhibitor |
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| Research Abstract |
Trappin-2 (SKALP/elafin), an elastase inhibitor, belongs to a unique family of proteinase inhibitors that are covalently anchored at the site of action through their transglutaminase substrate domain and are collectively called trappins. The transglutaminase substrate domain is therefore called "cementoin moiety". Currently, human, porcine, and bovine trappin-2(SKALP/elafin) have been characterized. Previously, our group showed that porcine trappin-2 (SKALP/elafin) occurs mainly in the trachea and large intestine. To determine the localization of trappin-2 (SKALP/elafin) at the cellular level, I performed in situ hybridization and immunohistochemistry using the porcine trachea and large intestine and found that trappin-2 (SKALP/elafin) is produced in the goblet cells of the trachea epithelium and of thelarge intestinal crypt. These locations suggest that trappin-2 (SKALP/elafin) is secreted intothe luminal surface of the trachea and crypts of Lieberkuhn and plays a protective role against destructive bacterial proteinases. Evolution of trappin family, genes was also clarified.Analysis of gene structure revealed that the genes for trappins have evolved by exon shuffling between the REST and SLPI genes and that the intron sequences have been homogenized by gene conversion.
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