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.
The highest levels of acid phosphatase are found in metastasized prostate cancer. Diseases of the bone, such as Paget's disease or hyperparathyroidism, diseases of blood cells, such as sickle-cell disease or multiple myeloma or lysosomal storage diseases, such as Gaucher's disease, will show moderately increased levels.
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.
Utility in prostatic cancer
erum marker
PSAP was used to monitor and assess progression of prostate cancer until the introduction of prostate specific antigen (PSA), which has now largely displaced it. Recent work, suggesting it has a role in prognosticating intermediate and high-risk prostate cancer, has lead to renewed interest in this marker.[cite journal |author=Taira A, Merrick G, Wallner K, Dattoli M |title=Reviving the acid phosphatase test for prostate cancer |journal=Oncology (Williston Park, N.Y.) |volume=21 |issue=8 |pages=1003–10 |year=2007 |month=July |pmid=17715699 |doi= |url=] ]Immunohistochemistry
PSAP immunohistochemical staining is often used with PSA (staining), by pathologists, to help distinguish poorly differentiated carcinomas. For example, poorly differentiated prostate adenocarcinoma (prostate cancer) and urothelial carcinoma (bladder cancer) may appear similar under the microscope, but PSAP and PSA staining can help differentiate them; [cite journal |author=Genega EM, Hutchinson B, Reuter VE, Gaudin PB |title=Immunophenotype of high-grade prostatic adenocarcinoma and urothelial carcinoma |journal=Mod. Pathol. |volume=13 |issue=11 |pages=1186–91 |year=2000 |month=November |pmid=11106075 |doi=10.1038/modpathol.3880220 |url=] prostate adenocarcinoma often stains with PSA and/or PSAP, while urothelial carcinoma does not.
Presumptive test for semen
Prostatic acid phosphatase is present in semen and its presence can be used as a presumptive test for semen. [ [http://www.semenonpanties.com/AP.htm Details of Acid Phosphatase test for semen.] ] Other acid phosphatases are present in other bodily fluids, but the high concentration of PAP in semen gives a strong indication that semen is present.
HIV
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. [cite journal |author=Münch J, Rücker E, Ständker L, Adermann K, Goffinet C, Schindler M, Wildum S, Chinnadurai R, Rajan D, Specht A, Giménez-Gallego G, Sánchez PC, Fowler DM, Koulov A, Kelly JW, Mothes W, Grivel JC, Margolis L, Keppler OT, Forssmann WG, Kirchhoff F |title=Semen-Derived Amyloid Fibrils Drastically Enhance HIV Infection |journal=Cell |volume=131 |issue=6 |pages=1059–71 |year=2007 |pmid=18083097 |doi=10.1016/j.cell.2007.10.014]
Pain suppression
A study at the University of North Carolina and University of Helsinki suggested that PAP could have potent antinociceptive, antihyperalgesic, and antiallodynic effects that last longer than morphine. One dose of PAP lasted for up to three days, much longer than the five hours gained with a single dose of morphine. When in distress, nerve cells release a chemical known as adenosine triphosphate (ATP) which in turn invokes a painful sensation. ATP is broken down into AMP which PAP converts into adenosine, a molecule known to suppress pain. [ [http://www.telegraph.co.uk/earth/main.jhtml?xml=/earth/2008/10/08/scipain108.xml New pain relief that is eight times stronger than morphine] , "Daily Telegraph"] [ [http://www.neuron.org/content/article/abstract?uid=PIIS0896627308007502 Prostatic Acid Phosphatase Is an Ectonucleotidase and Suppresses Pain by Generating Adenosine] , "Neuron"]
History
PSAP was the first useful serum tumour marker and emerged in the 1940s and 1950s.ee also
*Adenocarcinoma not otherwise specified
References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Ostrowski WS, Kuciel R |title=Human prostatic acid phosphatase: selected properties and practical applications. |journal=Clin. Chim. Acta |volume=226 |issue= 2 |pages= 121–9 |year= 1994 |pmid= 7923807 |doi=
*cite journal | author=Cooper JF, Foti AG, Shank PW |title=Radioimmunochemical measurement of bone marrow prostatic acid phosphatase. |journal=J. Urol. |volume=119 |issue= 3 |pages= 392–5 |year= 1978 |pmid= 76687 |doi=
*cite journal | author=Cooper JF, Foti A, Herschman H |title=Combined serum and bone marrow radioimmunoassays for prostatic acid phosphatase. |journal=J. Urol. |volume=122 |issue= 4 |pages= 498–502 |year= 1979 |pmid= 480493 |doi=
*cite journal | author=Sharief FS, Li SS |title=Structure of human prostatic acid phosphatase gene. |journal=Biochem. Biophys. Res. Commun. |volume=184 |issue= 3 |pages= 1468–76 |year= 1992 |pmid= 1375464 |doi=
*cite journal | author=Nguyen L, Chapdelaine A, Chevalier S |title=Prostatic acid phosphatase in serum of patients with prostatic cancer is a specific phosphotyrosine acid phosphatase. |journal=Clin. Chem. |volume=36 |issue= 8 Pt 1 |pages= 1450–5 |year= 1990 |pmid= 1696855 |doi=
*cite journal | author=Kamoshida S, Tsutsumi Y |title=Extraprostatic localization of prostatic acid phosphatase and prostate-specific antigen: distribution in cloacogenic glandular epithelium and sex-dependent expression in human anal gland. |journal=Hum. Pathol. |volume=21 |issue= 11 |pages= 1108–11 |year= 1990 |pmid= 1699876 |doi=
*cite journal | author=Van Etten RL, Davidson R, Stevis PE, "et al." |title=Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. |journal=J. Biol. Chem. |volume=266 |issue= 4 |pages= 2313–9 |year= 1991 |pmid= 1989985 |doi=
*cite journal | author=Tailor PG, Govindan MV, Patel PC |title=Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone. |journal=Nucleic Acids Res. |volume=18 |issue= 16 |pages= 4928 |year= 1990 |pmid= 2395659 |doi=
*cite journal | author=Warhol MJ, Longtine JA |title=The ultrastructural localization of prostatic specific antigen and prostatic acid phosphatase in hyperplastic and neoplastic human prostates. |journal=J. Urol. |volume=134 |issue= 3 |pages= 607–13 |year= 1985 |pmid= 2411954 |doi=
*cite journal | author=Sharief FS, Lee H, Leuderman MM, "et al." |title=Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase. |journal=Biochem. Biophys. Res. Commun. |volume=160 |issue= 1 |pages= 79–86 |year= 1989 |pmid= 2712834 |doi=
*cite journal | author=Vihko P, Virkkunen P, Henttu P, "et al." |title=Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. |journal=FEBS Lett. |volume=236 |issue= 2 |pages= 275–81 |year= 1988 |pmid= 2842184 |doi=
*cite journal | author=Yeh LC, Lee AJ, Lee NE, "et al." |title=Molecular cloning of cDNA for human prostatic acid phosphatase. |journal=Gene |volume=60 |issue= 2-3 |pages= 191–6 |year= 1988 |pmid= 2965059 |doi=
*cite journal | author=Sharief FS, Li SS |title=Nucleotide sequence of human prostatic acid phosphatase ACPP gene, including seven Alu repeats. |journal=Biochem. Mol. Biol. Int. |volume=33 |issue= 3 |pages= 561–5 |year= 1994 |pmid= 7951074 |doi=
*cite journal | author=Virkkunen P, Hedberg P, Palvimo JJ, "et al." |title=Structural comparison of human and rat prostate-specific acid phosphatase genes and their promoters: identification of putative androgen response elements. |journal=Biochem. Biophys. Res. Commun. |volume=202 |issue= 1 |pages= 49–57 |year= 1994 |pmid= 8037752 |doi= 10.1006/bbrc.1994.1892
*cite journal | author=Banas B, Blaschke D, Fittler F, Hörz W |title=Analysis of the promoter of the human prostatic acid phosphatase gene. |journal=Biochim. Biophys. Acta |volume=1217 |issue= 2 |pages= 188–94 |year= 1994 |pmid= 8110833 |doi=
*cite journal | author=Ostanin K, Saeed A, Van Etten RL |title=Heterologous expression of human prostatic acid phosphatase and site-directed mutagenesis of the enzyme active site. |journal=J. Biol. Chem. |volume=269 |issue= 12 |pages= 8971–8 |year= 1994 |pmid= 8132635 |doi=
*cite journal | author=Li SS, Sharief FS |title=The prostatic acid phosphatase (ACPP) gene is localized to human chromosome 3q21-q23. |journal=Genomics |volume=17 |issue= 3 |pages= 765–6 |year= 1993 |pmid= 8244395 |doi= 10.1006/geno.1993.1403
*cite journal | author=Lindqvist Y, Schneider G, Vihko P |title=Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate. |journal=J. Biol. Chem. |volume=268 |issue= 28 |pages= 20744–6 |year= 1993 |pmid= 8407898 |doi=
*cite journal | author=Darson MF, Pacelli A, Roche P, "et al." |title=Human glandular kallikrein 2 (hK2) expression in prostatic intraepithelial neoplasia and adenocarcinoma: a novel prostate cancer marker. |journal=Urology |volume=49 |issue= 6 |pages= 857–62 |year= 1997 |pmid= 9187691 |doi=
External links
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