D-Ephedrinephosphate, DEP: a new substrate with specificity for prostatic acid phosphatase (PAP).
This report describes the synthesis and physical (including spectral) properties of a new substrate, D-ephedrinephosphate, DEP1, which is histochemically highly specific for a secreted non-lysosomal prostatic acid phosphatase, PAP. This specificity is in contrast to other substrates which are nonspecific, i.e., which demonstrate acid phosphatases that originate from various cell types and are mainly lysosomal. When this substrate is used for light and electron microscopic histochemistry in a modified Gomori medium, PAP is demonstrated mainly in secretory granules and in the Golgi apparatus (and its related vacuoles) of prostatic epithelial cells of several species of mammals including man. This corroborates our previous suggestion that PAP is not a lysosomal enzyme as are many of the other acid phosphatases. This high degree of specificity of DEP for PAP supports the usefulness of this compound in the histochemical and biochemical characterization of PAP, and in the diagnosis of localized or disseminated prostatic disease.
D000135:Acid Phosphatase / Q000032:analysis* / Q000378:metabolism; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D003594:Cytoplasmic Granules / Q000201:enzymology; D004285:Dogs; D004809:Ephedrine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism; D004848:Epithelium / Q000201:enzymology; D005994:Glycerophosphates / Q000378:metabolism; D006056:Golgi Apparatus / Q000201:enzymology; D006651:Histocytochemistry; D006801:Humans; D008297:Male; D009943:Organophosphorus Compounds / Q000138:chemical synthesis; D011467:Prostate / Q000201:enzymology*; D051381:Rats; D013379:Substrate Specificity
D005994:Glycerophosphates; D009943:Organophosphorus Compounds; D000135:Acid Phosphatase; D004809:Ephedrine