Aquaporin-3

Protein-coding gene in the species Homo sapiens
AQP3
Identifiers
AliasesAQP3, AQP-3, GIL, aquaporin 3 (Gill blood group)
External IDsOMIM: 600170 MGI: 1333777 HomoloGene: 21025 GeneCards: AQP3
Gene location (Human)
Chromosome 9 (human)
Chr.Chromosome 9 (human)[1]
Chromosome 9 (human)
Genomic location for AQP3
Genomic location for AQP3
Band9p13.3Start33,441,156 bp[1]
End33,447,596 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for AQP3
Genomic location for AQP3
Band4|4 A5Start41,092,722 bp[2]
End41,098,183 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • parotid gland

  • human penis

  • palpebral conjunctiva

  • vulva

  • oral cavity

  • nipple

  • trachea

  • bronchus

  • bronchial epithelial cell

  • renal medulla
Top expressed in
  • lip

  • olfactory epithelium

  • yolk sac

  • esophagus

  • mucous cell of stomach

  • conjunctival fornix

  • cornea

  • pyloric antrum

  • kidney

  • morula
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • water channel activity
  • glycerol channel activity
  • transporter activity
  • channel activity
  • urea transmembrane transporter activity
Cellular component
  • cytoplasm
  • integral component of membrane
  • membrane
  • cell-cell junction
  • plasma membrane
  • basolateral plasma membrane
  • nucleus
Biological process
  • positive regulation of immune system process
  • excretion
  • response to vitamin D
  • response to retinoic acid
  • water transport
  • urea transport
  • odontogenesis
  • response to calcium ion
  • renal water homeostasis
  • regulation of keratinocyte differentiation
  • renal water absorption
  • glycerol transport
  • cellular response to oxygen-glucose deprivation
  • cellular response to hypoxia
  • transmembrane transport
  • urea transmembrane transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

360

11828

Ensembl

ENSG00000165272

ENSMUSG00000028435

UniProt

Q92482

Q8R2N1

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

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]

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

Clinical significance

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

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000165272 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028435 – 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. ^ 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

  • Bietz S, Montilla I, Külzer S, et al. (2009). "Recruitment of human aquaporin 3 to internal membranes in the Plasmodium falciparum infected erythrocyte". Mol. Biochem. Parasitol. 167 (1): 48–53. doi:10.1016/j.molbiopara.2009.04.006. PMID 19393693.
  • Bahamontes-Rosa N, Tena-Tomás C, Wolkow J, et al. (2008). "Genetic conservation of the GIL blood group determining aquaporin 3 gene in African and Caucasian populations". Transfusion. 48 (6): 1164–8. doi:10.1111/j.1537-2995.2008.01683.x. PMID 18435676. S2CID 5795042.
  • Wang S, Amidi F, Beall M, et al. (2006). "Aquaporin 3 expression in human fetal membranes and its up-regulation by cyclic adenosine monophosphate in amnion epithelial cell culture". J. Soc. Gynecol. Investig. 13 (3): 181–5. doi:10.1016/j.jsgi.2006.02.002. PMID 16638588. S2CID 30438043.
  • Ben Y, Chen J, Zhu R, et al. (2008). "Upregulation of AQP3 and AQP5 induced by dexamethasone and ambroxol in A549 cells". Respiratory Physiology & Neurobiology. 161 (2): 111–8. doi:10.1016/j.resp.2007.12.007. PMID 18280225. S2CID 25006640.
  • Yasui H, Kubota M, Iguchi K, et al. (2008). "Membrane trafficking of aquaporin 3 induced by epinephrine". Biochem. Biophys. Res. Commun. 373 (4): 613–7. doi:10.1016/j.bbrc.2008.06.086. PMID 18601899.
  • Horie I, Maeda M, Yokoyama S, et al. (2009). "Tumor necrosis factor-alpha decreases aquaporin-3 expression in DJM-1 keratinocytes". Biochem. Biophys. Res. Commun. 387 (3): 564–8. doi:10.1016/j.bbrc.2009.07.077. PMID 19619514.
  • Bellemère G, Von Stetten O, Oddos T (2008). "Retinoic acid increases aquaporin 3 expression in normal human skin". J. Invest. Dermatol. 128 (3): 542–8. doi:10.1038/sj.jid.5701047. PMID 17943189.
  • Cohly HH, Isokpehi R, Rajnarayanan RV (2008). "Compartmentalization of aquaporins in the human intestine". Int J Environ Res Public Health. 5 (2): 115–9. doi:10.3390/ijerph5020115. PMC 2694936. PMID 18678926.
  • Lee TC, Ho IC, Lu WJ, Huang JD (2006). "Enhanced expression of multidrug resistance-associated protein 2 and reduced expression of aquaglyceroporin 3 in an arsenic-resistant human cell line". J. Biol. Chem. 281 (27): 18401–7. doi:10.1074/jbc.M601266200. PMID 16672223.
  • Hara-Chikuma M, Verkman AS (2008). "Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing". J. Mol. Med. 86 (2): 221–31. doi:10.1007/s00109-007-0272-4. PMID 17968524. S2CID 24532416.
  • Hara-Chikuma M, Takahashi K, Chikuma S, et al. (2009). "The expression of differentiation markers in aquaporin-3 deficient epidermis". Arch. Dermatol. Res. 301 (3): 245–52. doi:10.1007/s00403-009-0927-9. PMC 3582396. PMID 19184071.
  • Wang J, Tanji N, Kikugawa T, et al. (2007). "Expression of aquaporin 3 in the human prostate". Int. J. Urol. 14 (12): 1088–92, discussion 1092. doi:10.1111/j.1442-2042.2007.01901.x. PMID 18036046. S2CID 34913820.
  • Higuchi S, Kubota M, Iguchi K, et al. (2007). "Transcriptional regulation of aquaporin 3 by insulin". J. Cell. Biochem. 102 (4): 1051–8. doi:10.1002/jcb.21350. PMID 17471492. S2CID 7045806.
  • Tancharoen S, Matsuyama T, Abeyama K, et al. (2008). "The role of water channel aquaporin 3 in the mechanism of TNF-alpha-mediated proinflammatory events: Implication in periodontal inflammation". J. Cell. Physiol. 217 (2): 338–49. doi:10.1002/jcp.21506. PMID 18543247. S2CID 900588.
  • Richardson SM, Knowles R, Marples D, et al. (2008). "Aquaporin expression in the human intervertebral disc". J. Mol. Histol. 39 (3): 303–9. doi:10.1007/s10735-008-9166-1. PMID 18247144. S2CID 24136257.
  • Avril-Delplanque A, Casal I, Castillon N, et al. (2005). "Aquaporin-3 expression in human fetal airway epithelial progenitor cells". Stem Cells. 23 (7): 992–1001. doi:10.1634/stemcells.2004-0197. PMID 16043462. S2CID 31421283.
  • Kida H, Miyoshi T, Manabe K, et al. (2005). "Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line". J. Membr. Biol. 208 (1): 55–64. doi:10.1007/s00232-005-0819-7. PMID 16596446. S2CID 11479553.
  • Liu YL, Matsuzaki T, Nakazawa T, et al. (2007). "Expression of aquaporin 3 (AQP3) in normal and neoplastic lung tissues". Hum. Pathol. 38 (1): 171–8. doi:10.1016/j.humpath.2006.07.015. PMID 17056099.

External links

  • GIL blood group system at BGMUT Blood Group Antigen Gene Mutation Database at NCBI, NIH
  • Human AQP3 genome location and AQP3 gene details page in the UCSC Genome Browser.
  • v
  • t
  • e
Ligand-gated
Voltage-gated
Constitutively active
Proton-gated
Voltage-gated
Calcium-activated
Inward-rectifier
Tandem pore domain
Voltage-gated
Miscellaneous
Cl: Chloride channel
H+: Proton channel
M+: CNG cation channel
M+: TRP cation channel
H2O (+ solutes): Porin
Cytoplasm: Gap junction
By gating mechanism
Ion channel class
see also disorders