Aquaporin 3 (AQP-3) is the protein product of the human AQP3 gene.[5] It is found in the basolateral cell membrane of principal collecting duct cells and provides a pathway for water to exit these cells.[6] Aquaporin-3 is also permeable to glycerol, ammonia, urea, and hydrogen peroxide. It is expressed in various tissues including the skin, respiratory tract, and kidneys as well as various types of cancers.[7] In the kidney, aquaproin-3 is unresponsive to the antidiuretic hormone vasopressin, unlike aquaporin-2.[8] This protein is also a determinant for the GIL blood group system.[9]

AQP3
Identifiers
AliasesAQP3, AQP-3, GIL, aquaporin 3 (Gill blood group)
External IDsOMIM: 600170; MGI: 1333777; HomoloGene: 21025; GeneCards: AQP3; OMA:AQP3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004925
NM_001318144

NM_016689

RefSeq (protein)

NP_001305073
NP_004916

NP_057898

Location (UCSC)Chr 9: 33.44 – 33.45 MbChr 4: 41.09 – 41.1 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Suberoylanilide hydroxamic acid (SAHA) (a HDAC inhibitor) increases expression of aquaporin-3 in normal skin cells (keratinocytes).[10]

Clinical significance

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Aquaporin 3 levels are often lower in psoriasis than in healthy skin.[10]

Aquaporin 3 is expressed more in atopic eczema.[11]

Recent studies indicate that aquaporin 3 is overexpressed in many types of malignancies such as melanoma[7] and primary effusion lymphomas[12] as well as cancers of the lung, colon, stomach, esophagus, mouth, liver, and pancreatic duct.[5][12] Based on these as well as cell culture studies, it is suggested that this overexpression contributes to the growth and spread of at least some of these cancers and therefore may be a therapeutic target for the treatment of these cancers.[5][7][12]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000165272Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028435Ensembl, 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. ^ a b c Marlar S, Jensen HH, Login FH, Nejsum LN (October 2017). "Aquaporin-3 in Cancer". International Journal of Molecular Sciences. 18 (10): 2106. doi:10.3390/ijms18102106. PMC 5666788. PMID 28991174.
  6. ^ Sasaki S, Ishibashi K, Marumo F (1998). "Aquaporin-2 and -3: representatives of two subgroups of the aquaporin family colocalized in the kidney collecting duct". Annu. Rev. Physiol. 60: 199–220. doi:10.1146/annurev.physiol.60.1.199. PMID 9558461.
  7. ^ a b c Oliveira Pinho J, Matias M, Gaspar MM (October 2019). "Emergent Nanotechnological Strategies for Systemic Chemotherapy against Melanoma". Nanomaterials. 9 (10): 1455. doi:10.3390/nano9101455. PMC 6836019. PMID 31614947.
  8. ^ Dibas AI, Mia AJ, Yorio, T (1998). "Aquaporins (Water Channels): Role in Vasopressin-Activated Water Transport". Proc. Soc. Exp. Biol. Med. 219 (3): 183–99. doi:10.3181/00379727-219-44332. PMID 9824541. S2CID 28952956.
  9. ^ Roudier N, Ripoche P, Gane P, Le Pennec PY, Daniels G, Cartron JP, Bailly P (2002). "AQP3 deficiency in humans and the molecular basis of a novel blood group system, GIL". J. Biol. Chem. 277 (48): 45854–9. doi:10.1074/jbc.M208999200. PMID 12239222.
  10. ^ a b University, Medical College of Georgia at Augusta. "Cancer therapy shows promise for psoriasis treatment". medicalxpress.com.
  11. ^ Olsson M, Broberg A, Jernãs M, et al. (2006). "Increased expression of aquaporin 3 in atopic eczema". Allergy. 61 (9): 1132–7. doi:10.1111/j.1398-9995.2006.01151.x. PMID 16918518. S2CID 7873440.
  12. ^ a b c Shimada K, Hayakawa F, Kiyoi H (November 2018). "Biology and management of primary effusion lymphoma". Blood. 132 (18): 1879–1888. doi:10.1182/blood-2018-03-791426. PMID 30154110.

Further reading

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