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Prostatic acid phosphatase

From Wikipedia, the free encyclopedia
(Redirected from ACPP)
ACP3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesACP3, 5'-NT, TM-PAP, ACP-3, acid phosphatase 3, acid phosphatase, prostate, ACPP
External IDsOMIM: 171790; MGI: 1928480; HomoloGene: 55552; GeneCards: ACP3; OMA:ACP3 - orthologs
EC number3.1.3.5
Orthologs
SpeciesHumanMouse
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 MbChr 9: 104.17 – 104.21 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

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Serum marker

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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

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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

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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

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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

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

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000014257 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b 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

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