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Originally published In Press as doi:10.1074/jbc.M201244200 on May 1, 2002

J. Biol. Chem., Vol. 277, Issue 29, 26412-26421, July 19, 2002
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Identification and Characterization of A Novel Rat Ov-Serpin Family Member, Trespin*

Jerry E. ChipukDagger §||, LaMonica V. Stewart||**Dagger Dagger , Annalisa Ranieri**§§, Kyung SongDagger §, and David DanielpourDagger §¶¶

From the Dagger  Ireland Cancer Center Research Laboratories and § Department of Pharmacology, Case Western Reserve University/University Hospitals of Cleveland, Cleveland, Ohio 44106 and the ** Laboratory of Cell Regulation and Carcinogenesis, NCI, National Institutes of Health, Bethesda, Maryland 20892

Serpins are responsible for regulating a variety of proteolytic processes through a unique irreversible suicide substrate mechanism. To discover novel genes regulated by transforming growth factor-beta 1 (TGF-beta 1), we performed differential display reverse transcriptase-PCR analysis of NRP-152 rat prostatic epithelial cells and cloned a novel rat serpin that is transcriptionally down-regulated by TGF-beta and hence named trespin (TGF-beta -repressible serine proteinase inhibitor (trespin). Trespin is a 397-amino acid member of the ov-serpin clade with a calculated molecular mass of 45.2 kDa and 72% amino acid sequence homology to human bomapin; however, trespin exhibits different tissue expression, cellular localization, and proteinase specificity compared with bomapin. Trespin mRNA is expressed in many tissues, including brain, heart, kidney, liver, lung, prostate, skin, spleen, and stomach. FLAG-trespin expressed in HEK293 cells is localized predominantly in the cytoplasm and is not constitutively secreted. The presence of an arginine at the P1 position of trespin's reactive site loop suggests that trespin inhibits trypsin-like proteinases. Accordingly, in vitro transcribed and translated trespin forms detergent-stable and thermostable complexes with plasmin and elastase but not subtilisin A, trypsin, chymotrypsin, thrombin, or papain. Trespin interacts with plasmin at a near 1:1 stoichiometry, and immunopurified mammal-expressed trespin inhibits plasmin in a dose-dependent manner. These data suggest that trespin is a novel and functional member of the rat ov-serpin family.

* This study was supported by Cancer Center Grant P30CA43703, American Cancer Society Research Grant RG-91-022-06, and NCI, National Institutes of Health (NIH), Grant 1R01 CA3069-01 and by NIH intramural funds from the Laboratory of Cell Regulation and Carcinogenesis.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY075037.

Supported by a Research Oncology Training Grant predoctoral award to the Cancer Center from NCI, NIH.

|| These authors contributed equally to this work.

Dagger Dagger Supported by an intramural NIGMS, NIH, Pharmacology Research Associate postdoctoral fellowship. Present address: Dept. of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030.

§§ Supported by an intramural guest researcher-training award from the NIH visiting program. Present address: Dept. of Oncology and Neuroscience, University of Medicine, Chieti 66013, Italy.

¶¶ To whom correspondence should be addressed: Ireland Cancer Center Research Laboratories, Samuel Gerber Bldg., Suite 200, Lab 3, 11001 Cedar Rd., Cleveland, OH 44106. Tel.: 216-844-6959; E-mail: dxd49@po.cwru.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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