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Abstract
We determined the cDNA and gene structures of guinea pig caltrin II, a unique member of calcium transporter inhibitor containing a whey acidic protein (WAP) motif, and 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 following castration, which was 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 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 exertion of different functions.
Key words:
Calcium
Seminal vesicles
Testosterone
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