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
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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]

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 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]}

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]

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]

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

• Adenocarcinoma not otherwise specified

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