Prostatic acid phosphatase (PAP), alsoprostatic specific acid phosphatase (PSAP), is anenzyme produced by theprostate. It may be found in increased amounts in men who haveprostate cancer or other diseases.
Certainmedications can cause temporary increases or decreases in acid phosphatase levels. Manipulation of the prostate gland through massage,biopsy orrectal exam before a test may increase the level.
Its physiological function may be associated with the liquefaction process ofsemen.[5]
PAP was used to monitor and assess progression ofprostate cancer until the introduction ofprostate specific antigen (PSA), which has now largely displaced it. Subsequent work, suggested that it has a role inprognosticating intermediate and high-risk prostate cancer, and led to renewed interest in it as abiomarker.[6]
PAP may play an important role in the transmission ofHIV. Researchers at theUniversity of Ulm inGermany found that PAP forms fibers made ofamyloid. They called the fiberssemen-derived enhancer of virus infection (SEVI) and showed that they capture HIV virions promoting their attachment to target cells. The association of PAP with HIV may increase the ability of the virus to infect human cells "by several orders of magnitude." PAP may be a future target of efforts to combat the spread of HIV infection.[8]
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^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
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^abTaira A, Merrick G, Wallner K, Dattoli M (July 2007). "Reviving the acid phosphatase test for prostate cancer".Oncology (Williston Park, N.Y.).21 (8):1003–10.PMID17715699.
Ostrowski WS, Kuciel R (1994). "Human prostatic acid phosphatase: selected properties and practical applications".Clin. Chim. Acta.226 (2):121–9.doi:10.1016/0009-8981(94)90209-7.PMID7923807.
Cooper JF, Foti AG, Shank PW (1978). "Radioimmunochemical measurement of bone marrow prostatic acid phosphatase".J. Urol.119 (3):392–5.doi:10.1016/S0022-5347(17)57499-6.PMID76687.
Cooper JF, Foti A, Herschman H (1979). "Combined serum and bone marrow radioimmunoassays for prostatic acid phosphatase".J. Urol.122 (4):498–502.doi:10.1016/S0022-5347(17)56480-0.PMID480493.
Kamoshida S, Tsutsumi Y (1990). "Extraprostatic localization of prostatic acid phosphatase and prostate-specific antigen: distribution in cloacogenic glandular epithelium and sex-dependent expression in human anal gland".Hum. Pathol.21 (11):1108–11.doi:10.1016/0046-8177(90)90146-V.PMID1699876.
Warhol MJ, Longtine JA (1985). "The ultrastructural localization of prostatic specific antigen and prostatic acid phosphatase in hyperplastic and neoplastic human prostates".J. Urol.134 (3):607–13.doi:10.1016/S0022-5347(17)47311-3.PMID2411954.
Yeh LC, Lee AJ, Lee NE, et al. (1988). "Molecular cloning of cDNA for human prostatic acid phosphatase".Gene.60 (2–3):191–6.doi:10.1016/0378-1119(87)90227-7.PMID2965059.
Sharief FS, Li SS (1994). "Nucleotide sequence of human prostatic acid phosphatase ACPP gene, including seven Alu repeats".Biochem. Mol. Biol. Int.33 (3):561–5.PMID7951074.
Virkkunen P, Hedberg P, Palvimo JJ, et al. (1994). "Structural comparison of human and rat prostate-specific acid phosphatase genes and their promoters: identification of putative androgen response elements".Biochem. Biophys. Res. Commun.202 (1):49–57.doi:10.1006/bbrc.1994.1892.PMID8037752.
Banas B, Blaschke D, Fittler F, Hörz W (1994). "Analysis of the promoter of the human prostatic acid phosphatase gene".Biochim. Biophys. Acta.1217 (2):188–94.doi:10.1016/0167-4781(94)90033-7.PMID8110833.
Darson MF, Pacelli A, Roche P, et al. (1997). "Human glandular kallikrein 2 (hK2) expression in prostatic intraepithelial neoplasia and adenocarcinoma: a novel prostate cancer marker".Urology.49 (6):857–62.doi:10.1016/S0090-4295(97)00108-8.PMID9187691.
1cvi: CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE
1nd5: Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design
1nd6: Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design
2hpa: STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE
