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Androgen-Dependent Expression, Gene Structure, and Molecular Evolution of Guinea Pig Caltrin II, a WAP-Motif Protein¹

Molecular Cellular Pathology Research Unit,³ RIKEN, Wako-shi, Saitama 351-0198, Japan Department of Biological Sciences,⁴ Tokyo Institute of Technology, Midori-ku, Yokohama 226-8501, Japan

We determined the cDNA and gene structures of guinea pig caltrin II, a unique member of the calcium transporter inhibitors containing a whey acidic protein (WAP) motif, and we established that it is a secretory protein with a potential 21-amino acid signal peptide in its N-terminus. Northern blot analysis and in situ hybridization histochemistry indicated that the expression of caltrin II is restricted to luminal epithelial cells in the seminal vesicles. Its message levels markedly decreased either after castration (and were restored by simultaneous administration of testosterone) or after treatment of the animals with estradiol, suggesting that the expression of caltrin II is androgen-dependent. Recombinant caltrin II had an elastase-inhibitor activity. Comparison of sequence between the caltrin II and related genes and their molecular evolutionary analyses revealed that caltrin II and seminal vesicle secretory proteins (SVPs) appear to be evolved from a common ancestor gene that is made by the fusion of semenogelin and trappin genes. Caltrin II and SVPs lost the transglutaminase substrate domain and the WAP motif, respectively, within a single exon, resulting in the exertion of different functions.

¹ Supported in part by Grants-in-Aid for Scientific Research (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 the Chemical Biology Research Project from RIKEN (to S.K.). Y.F. was supported by a Research Fellowship for Young Scientists from the Japan Society for the Promotion of Science. The nucleotide sequences reported in the present study have been submitted to the DDBJ/GenBank/EMBL Data Bank with accession numbers AB042257 and AB161363.

² Correspondence: Shigehisa Hirose, Department of Biological Sciences, Tokyo Institute of Technology, 4259-B-19 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan. FAX: 81-45-924-5824; shirose{at}bio.titech.ac.jp

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