Abstract

Prostatic secretory protein of 94 amino acids (PSP94), also called beta-microseminoprotein, is a small, nonglycosylated protein, rich in cysteine residues. It was first isolated as a major protein from human seminal plasma. Subsequently, its homologous proteins were identified, and their cDNAs or genes have been cloned in primates, pigs, and rodents. The present study investigated the expression pattern of PSP94 in the normal Noble rat prostate gland by nonradioactive in situ hybridization, Northern blotting, RT-PCR, Western blotting, and immunohistochemistry. Its expression in the mouse prostate gland was also examined by in situ hybridization. The results of in situ hybridization, and Northern and Western blot analyses, showed that the expression of rat PSP94 was prostate-specific. It was highly expressed in the lateral prostatic lobe, moderate in the dorsal lobe, weak in the coagulating gland, and negative in the ventral lobe and seminal vesicle. Its specific expression in the rat prostate gland was further confirmed by RT-PCR analysis of prostatic and nonprostatic organ tissues. Its mRNA transcripts were not detected in the urinary, digestive, and respiratory tracts, male and female reproductive organs, muscles, brain, and kidney. Its molecular mass was estimated to be 14.5 kDa by Western blotting. Similar prostate-specific expression of PSP94 was also observed by in situ hybridization in the lateral lobe, but not in the dorsal and ventral lobe, of the mouse prostate gland. Rat PSP94 is a major secretory protein highly expressed and synthesized by the lateral lobe of both rat and mouse prostate glands, and moderately expressed in the dorsal lobe of the rat prostate gland.

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