Biochemical characteristics of the proteins secreted by dog prostate, a review.
Proteins secreted by dog prostate differ from those of other species and in particular from those of man, both in terms of quantity and quality. These differences can be observed in the electrophoretic pattern of proteins in polyacrylamide gels and in enzymes such as phosphatases, glycohydrolases and proteases. For instance, canine acid phosphatase, although quite similar biochemically to the human enzyme, is about one hundred fold less concentrated in both prostatic tissue and seminal plasma than in the human. By contrast, arginine esterase, which is virtually absent in human prostatic secretion, comprises more than 90% of total proteins secreted by dog prostate. The most recent data on each of these enzymes, enzyme classes and proteins will be reviewed. Despite recent advancement of knowledge on the biochemistry of these constituents, their biological function as well as their contribution to the pathogenesis of prostatic diseases still remain a matter of speculation. For both of these aspects, dog appears to be a particularly interesting model.
D000135:Acid Phosphatase / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D005959:Glucosidases / Q000378:metabolism; D008297:Male; D010447:Peptide Hydrolases / Q000378:metabolism; D011467:Prostate / Q000201:enzymology / Q000378:metabolism*; D011471:Prostatic Neoplasms / Q000201:enzymology; D011506:Proteins / Q000378:metabolism*; D012661:Semen / Q000201:enzymology; D013379:Substrate Specificity
D011506:Proteins; D000135:Acid Phosphatase; D005959:Glucosidases; D010447:Peptide Hydrolases