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Originally published In Press as doi:10.1074/jbc.M501678200 on March 18, 2005

J. Biol. Chem., Vol. 280, Issue 21, 20204-20215, May 27, 2005
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Identification, Evolution, and Regulation of Expression of Guinea Pig Trappin with an Unusually Long Transglutaminase Substrate Domain*{boxs}

Yutaka Furutani{ddagger}§, Akira Kato§, Azzania Fibriani§, Taku Hirata§, Ryoji Kawai§, Ju-Hong Jeon||, Yasuhisa Fujii**, In-Gyu Kim||, Soichi Kojima{ddagger}, and Shigehisa Hirose§{ddagger}{ddagger}

From the {ddagger}Molecular Cellular Pathology Research Unit, RIKEN, Wako-shi, Saitama 351-0198, Japan, the §Department of Biological Sciences, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8501, Japan, the ||Department of Biochemistry and Molecular Biology, Aging and Apoptosis Research Center, Seoul National University College of Medicine, Seoul 110-799, Korea, and the **Department of Urology and Reproductive Medicine, Tokyo Medical and Dental University Graduate School, Bunkyo-ku, Tokyo 113-8519, Japan

Trappins are found in human, bovine, hippopotamus, and members of the pig family, but not in rat and mouse. To clarify the evolution of the trappin genes and the functional significance of their products, we isolated the trappin gene in guinea pig, a species belonging to a rodent family distinct from rat and mouse. Guinea pig trappin was confirmed to encode the same domain structure as trappin, consisting of a signal sequence, an extra large transglutaminase substrate domain, and a whey acidic protein motif. Northern blot analysis and in situ hybridization histochemistry as well as immunohistochemistry demonstrated that guinea pig trappin is expressed solely in the secretory epithelium of the seminal vesicle and that its expression is androgen-dependent. We confirmed that guinea pig trappin is cross-linked by prostate transglutaminase and that the whey acidic protein motif derived from guinea pig trappin has an inhibitory activity against leukocyte elastase. Genome sequence analysis showed that guinea pig trappin belongs to the family of REST (rapidly evolving seminal vesicle transcribed) genes.


Received for publication, February 14, 2005

* This work was supported in part by grants-in-aid for scientific research, the 21st Century Centers of Excellence (COE) Program (to S. H.), and the Special Coordination Fund for the Promotion of Science and Technology (to S. K.) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan and by a chemical biology research project from RIKEN (to S. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{boxs} The on-line version of this article (available at http://www.jbc.org) contains Supplemental Figs. S1 and S2.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number(s) AB058645 and AB161364.

Supported by a research fellowship for young scientists from the Japan Society for the Promotion of Science.

{ddagger}{ddagger} To whom correspondence should be addressed: Dept. of Biological Sciences, Tokyo Inst. of Technology, 4259-B19 Nagatsuta-cho, Midoriku, Yokohama 226-8501, Japan. Tel: 81-45-924-5726; Fax: 81-45-924-5824; E-mail: shirose{at}bio.titech.ac.jp.


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