CHARACTERIZATION OF RHESUS-MONKEY PROSTATE-SPECIFIC ANTIGEN CDNA

Using a RT-PCR approach, we obtained two overlapping cDNA clones conta ining the entire 1.5 kb sequence of rhesus monkey prostate specific an tigen (rmPSA). The sequence obtained revealed an open reading frame of 261 amino acids. One potential N-glycosylation site was identified at Asn-78. The calculated molecular mass for the unglycosylated mature p rotein was 26 147 Da. Extensive amino acid homology (89%) was observed between rmPSA and its human counterpart. These results demonstrate th at rhesus monkey and man prostate share a major biochemical component, and suggest that this animal species might be useful to answer specif ic questions related to human prostatic function and pathology.