Prostatic acid phosphatase

ACP3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1CVI, 1ND5, 1ND6, 2HPA, 2L3H, 2L77, 2L79, 3PPD, 2MG0
Identifiers
Aliases	ACP3 , 5'-NT, TM-PAP, ACP-3, acid phosphatase 3, acid phosphatase, prostate, ACPP
External IDs	OMIM: 171790; MGI: 1928480; HomoloGene: 55552; GeneCards: ACP3; OMA:ACP3 - orthologs
EC number	3.1.3.5
Gene location (Human) Chr. Chromosome 3 (human) [1] Band 3q22.1 Start 132,317,369 bp [1] End 132,368,298 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9|9 F1 Start 104,165,450 bp [2] End 104,214,947 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in prostate sperm human penis urethra monocyte oral cavity skin of thigh germinal epithelium vulva gingival epithelium Top expressed in lacrimal gland molar lumbar spinal ganglion submandibular gland skin of external ear lip Paneth cell hair follicle parotid gland granulocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function 5'-nucleotidase activity acid phosphatase activity thiamine phosphate phosphatase activity phosphatase activity lysophosphatidic acid phosphatase activity identical protein binding hydrolase activity protein binding protein homodimerization activity Cellular component integral component of membrane membrane vesicle membrane filopodium intracellular anatomical structure extracellular region lysosomal membrane lysosome extracellular exosome nucleus extracellular space plasma membrane azurophil granule membrane Biological process regulation of sensory perception of pain adenosine metabolic process nucleotide metabolic process positive regulation of adenosine receptor signaling pathway purine nucleobase metabolic process thiamine metabolic process dephosphorylation neutrophil degranulation protein homotetramerization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 55 56318 Ensembl ENSG00000014257 ENSMUSG00000032561 UniProt P15309 Q8CE08 RefSeq (mRNA) NM_001099 NM_001134194 NM_001292037 NM_019807 NM_207668 RefSeq (protein) NP_001090 NP_001127666 NP_001278966 NP_062781 NP_997551 Location (UCSC) Chr 3: 132.32 – 132.37 Mb Chr 9: 104.17 – 104.21 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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.

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]

Immunohistochemistry

PAP 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 PAP and PSA staining can help differentiate them; ^[7] prostate adenocarcinoma often stains with PSA and/or PAP, while urothelial carcinoma does not.^{[ citation needed ]}

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. ^[8]

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 (adenosine monophosphate), which PAP converts into adenosine, a molecule known to suppress pain. ^{[9] [10]}

History

PAP was the first useful serum tumour marker and emerged in the 1940s and 1950s. ^[6]

See also

• Adenocarcinoma not otherwise specified

References

1. GRCh38: Ensembl release 89: ENSG00000014257 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032561 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Page 1135-1136 in: Walter F. Boron (2003). Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. p. 1300. ISBN   978-1-4160-2328-9.
6. Taira 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. PMID   17715699.
7. Genega EM, Hutchinson B, Reuter VE, Gaudin PB (November 2000). "Immunophenotype of high-grade prostatic adenocarcinoma and urothelial carcinoma". Mod. Pathol. 13 (11): 1186–91. doi: 10.1038/modpathol.3880220 . PMID   11106075.
8. 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 (2007). "Semen-Derived Amyloid Fibrils Drastically Enhance HIV Infection". Cell. 131 (6): 1059–71. doi: 10.1016/j.cell.2007.10.014 . PMID   18083097. S2CID   7921205.
9. New pain relief that is eight times stronger than morphine, Daily Telegraph
10. Zylka MJ, Sowa NA, Taylor-Blake B, et al. (October 2008). "Prostatic acid phosphatase is an ectonucleotidase and suppresses pain by generating adenosine". Neuron. 60 (1): 111–22. doi:10.1016/j.neuron.2008.08.024. PMC   2629077 . PMID   18940592.

Further reading

• 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. PMID   7923807.
• 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. PMID   76687.
• 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. PMID   480493.
• Sharief FS, Li SS (1992). "Structure of human prostatic acid phosphatase gene". Biochem. Biophys. Res. Commun. 184 (3): 1468–76. doi:10.1016/S0006-291X(05)80048-8. PMID   1375464.
• Nguyen L, Chapdelaine A, Chevalier S (1990). "Prostatic acid phosphatase in serum of patients with prostatic cancer is a specific phosphotyrosine acid phosphatase". Clin. Chem. 36 (8 Pt 1): 1450–5. doi: 10.1093/clinchem/36.8.1450 . PMID   1696855.
• 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. PMID   1699876.
• Van Etten RL, Davidson R, Stevis PE, et al. (1991). "Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase". J. Biol. Chem. 266 (4): 2313–9. doi: 10.1016/S0021-9258(18)52245-6 . PMID   1989985.
• Tailor PG, Govindan MV, Patel PC (1990). "Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone". Nucleic Acids Res. 18 (16): 4928. doi:10.1093/nar/18.16.4928. PMC   331993 . PMID   2395659.
• 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. PMID   2411954.
• Sharief FS, Lee H, Leuderman MM, et al. (1989). "Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase". Biochem. Biophys. Res. Commun. 160 (1): 79–86. doi:10.1016/0006-291X(89)91623-9. PMID   2712834.
• Vihko P, Virkkunen P, Henttu P, et al. (1988). "Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase". FEBS Lett. 236 (2): 275–81. Bibcode:1988FEBSL.236..275V. doi: 10.1016/0014-5793(88)80037-1 . PMID   2842184. S2CID   8445782.
• 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. PMID   2965059.
• 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. PMID   7951074.
• 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. PMID   8037752.
• 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. PMID   8110833.
• Ostanin K, Saeed A, Van Etten RL (1994). "Heterologous expression of human prostatic acid phosphatase and site-directed mutagenesis of the enzyme active site". J. Biol. Chem. 269 (12): 8971–8. doi: 10.1016/S0021-9258(17)37063-1 . PMID   8132635.
• Li SS, Sharief FS (1993). "The prostatic acid phosphatase (ACPP) gene is localized to human chromosome 3q21-q23". Genomics. 17 (3): 765–6. doi:10.1006/geno.1993.1403. PMID   8244395.
• Quintero IB, Araujo CL, Pulkka AE, Wirkkala RS, Herrala AM, Eskelinen EL, Jokitalo E, Hellström PA, Tuominen HJ, Hirvikoski PP, Vihko PT (2007). "Prostatic acid phosphatase is not a prostate specific target" (PDF). Cancer Res. 67 (14): 6549–54. doi: 10.1158/0008-5472.CAN-07-1651 . PMID   17638863.
• Lindqvist Y, Schneider G, Vihko P (1993). "Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate". J. Biol. Chem. 268 (28): 20744–6. doi: 10.1016/S0021-9258(19)36845-0 . PMID   8407898.
• 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. PMID   9187691.

External links

• prostatic+acid+phosphatase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)