Prostatic acid phosphatase (PAP), also prostatic specific acid phosphatase (PSAP), is an
enzyme produced by the
prostate. It may be found in increased amounts in men who have
prostate cancer or other diseases.
Certain
medications can cause temporary increases or decreases in acid phosphatase levels. Manipulation of the prostate gland through massage,
biopsy or
rectal exam before a test may increase the level.
Its physiological function may be associated with the liquefaction process of
semen.[5]
Use in prostatic cancer prognosis
Serum marker
PAP was used to monitor and assess progression of
prostate cancer until the introduction of
prostate specific antigen (PSA), which has now largely displaced it. Subsequent work, suggested that it has a role in
prognosticating intermediate and high-risk prostate cancer, and led to renewed interest in it as a
biomarker.[6]
PAP may play an important role in the transmission of
HIV. Researchers at the
University of Ulm in
Germany found that PAP forms fibers made of
amyloid. They called the fibers
semen-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]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Page 1135-1136 in: Walter F. Boron (2003). Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. p. 1300.
ISBN978-1-4160-2328-9.
^
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.
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.
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