TESSP-1: a novel serine protease gene expressed in the spermatogonia and spermatocytes of adult mouse testes.

A cDNA encoding a novel type of serine protease, designated testis-specific serine protease 1 (TESSP-1), was cloned using mRNA isolated from the adult mouse testis. The open reading frame of this cDNA codes for a protein of 322 amino acids, which includes a hydrophobic signal peptide of 18 amino acids and an N-terminal activation peptide of 34 amino acids. The protein has an additional hydrophobic amino acid sequence at the C-terminus. Expression of the TESSP-1 gene was restricted to the testis. TESSP-1 mRNA expression initiated in the mouse testis at 2 weeks after birth, and its level increased steadily with sexual maturation of the animal. In situ hybridization analysis revealed that TESSP-1 mRNA was expressed in type B spermatogonia and spermatocytes at stages between preleptotene and pachytene. The testis contained at least five distinct forms of TESSP-1 transcript, which presumably resulted from alternative splicing of the mRNA, but only one of these transcripts encodes a complete, functional enzyme. Expression experiments using COS-7 cells showed that TESSP-1 was synthesized as a glycoprotein with N-glycosylated carbohydrates. Tests also showed that the C-terminal hydrophobic region of TESSP-1 was important upon its binding to the membrane by anchoring through glycosylphosphatidylinositol (GPI).

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