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Aquaporin-3

From Wikipedia, the free encyclopedia
(Redirected fromAquaporin 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;OMA:AQP3 - orthologs
Gene location (Human)
Chromosome 9 (human)
Chr.Chromosome 9 (human)[1]
Chromosome 9 (human)
Genomic location for AQP3
Genomic location for AQP3
Band9p13.3Start33,441,156bp[1]
End33,447,596bp[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 A5Start41,092,722bp[2]
End41,098,183bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • nasal epithelium

  • gingival epithelium

  • mucosa of pharynx

  • epithelium of nasopharynx

  • parotid gland

  • human penis

  • palpebral conjunctiva

  • vulva

  • oral cavity

  • nipple
Top expressed in
  • lip

  • olfactory epithelium

  • transitional epithelium of urinary bladder

  • yolk sac

  • esophagus

  • right kidney

  • mucous cell of stomach

  • skin of external ear

  • conjunctival fornix

  • cornea
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
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 humanAQP3 gene.[5] It is found in the basolateral cell membrane of principalcollecting duct cells and provides a pathway for water to exit these cells.[6] Aquaporin-3 is also permeable toglycerol,ammonia,urea, andhydrogen 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, aquaporin-3 is unresponsive to the antidiuretic hormonevasopressin, unlikeaquaporin-2.[8] This protein is also a determinant for the GIL blood group system.[9]

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

Clinical significance

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

Aquaporin 3 is expressed more inatopic eczema.[11]

Recent studies indicate that aquaporin 3 is overexpressed in many types of malignancies such asmelanoma[7] andprimary 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 ascell 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. ^abcGRCh38: Ensembl release 89: ENSG00000165272Ensembl, May 2017
  2. ^abcGRCm38: 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. ^abcMarlar 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. ^abcOliveira 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. ^abUniversity, 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. ^abcShimada 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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External links

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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 alsodisorders
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