Aquaporin-3

Last updated
AQP3
Identifiers
Aliases AQP3 , AQP-3, GIL, aquaporin 3 (Gill blood group)
External IDs OMIM: 600170 MGI: 1333777 HomoloGene: 21025 GeneCards: AQP3
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 Mb Chr 4: 41.09 – 41.1 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/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]

Contents

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

Related Research Articles

<span class="mw-page-title-main">Aquaporin</span> Cellular membrane structure that selectively passes water

Aquaporins, also called water channels, are channel proteins from a larger family of major intrinsic proteins that form pores in the membrane of biological cells, mainly facilitating transport of water between cells. The cell membranes of a variety of different bacteria, fungi, animal and plant cells contain aquaporins through which water can flow more rapidly into and out of the cell than by diffusing through the phospholipid bilayer. Aquaporins have six membrane-spanning alpha helical domains with both carboxylic and amino terminals on the cytoplasmic side. Two hydrophobic loops contain conserved asparagine–proline–alanine which form a barrel surrounding a central pore-like region that contains additional protein density. Because aquaporins are usually always open and are prevalent in just about every cell type, this leads to a misconception that water readily passes through the cell membrane down its concentration gradient. Water can pass through the cell membrane through simple diffusion because it is a small molecule, and through osmosis, in cases where the concentration of water outside of the cell is greater than that of the inside. However, because water is a polar molecule this process of simple diffusion is relatively slow, and in tissues with high water permeability the majority of water passes through aquaporin.

<span class="mw-page-title-main">CD59</span> Mammalian protein found in Homo sapiens

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<span class="mw-page-title-main">Peptide transporter 1</span> Mammalian protein found in Homo sapiens

Peptide transporter 1 also known as solute carrier family 15 member 1 (SLC15A1) is a protein that in humans is encoded by SLC15A1 gene. PepT 1 is a solute carrier for oligopeptides. It functions in renal oligopeptide reabsorption and in the intestines in a proton dependent way, hence acting like a cotransporter.

<span class="mw-page-title-main">S1PR3</span> Protein and coding gene in humans

Sphingosine-1-phosphate receptor 3 also known as S1PR3 is a human gene which encodes a G protein-coupled receptor which binds the lipid signaling molecule sphingosine 1-phosphate (S1P). Hence this receptor is also known as S1P3.

<span class="mw-page-title-main">ADAM9</span> Protein-coding gene in the species Homo sapiens

Disintegrin and metalloproteinase domain-containing protein 9 is an enzyme that in humans is encoded by the ADAM9 gene.

<span class="mw-page-title-main">MEP1A</span> Protein-coding gene in the species Homo sapiens

Meprin A subunit alpha also known as endopeptidase-2 or PABA peptide hydrolase is the alpha subunit of the meprin A enzyme that in humans is encoded by the MEP1A gene. The MEP1A locus is on chromosome 6p in humans and on chromosome 17 in mice.

<span class="mw-page-title-main">HAS2</span> Protein-coding gene in the species Homo sapiens

Hyaluronan synthase 2 is an enzyme that in humans is encoded by the HAS2 gene.

<span class="mw-page-title-main">ATP2A3</span> Protein-coding gene in the species Homo sapiens

Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 is an enzyme that in humans is encoded by the ATP2A3 gene.

<span class="mw-page-title-main">FLOT2</span> Protein-coding gene in the species Homo sapiens

Flotillin-2 is a protein that in humans is encoded by the FLOT2 gene. Flotillin 2 (flot-2) is a highly conserved protein isolated from caveolae/lipid raft domains that tether growth factor receptors linked to signal transduction pathways. Flot-2 binds to PAR-1, a known upstream mediator of major signal transduction pathways implicated in cell growth and metastasis, and may influence tumour progression.

<span class="mw-page-title-main">Equilibrative nucleoside transporter 2</span> Protein-coding gene in the species Homo sapiens

Equilibrative nucleoside transporter 2 (ENT2) is a protein that in humans is encoded by the SLC29A2 gene.

<span class="mw-page-title-main">Concentrative nucleoside transporter 2</span> Protein-coding gene in the species Homo sapiens

Concentrative nucleoside transporter 2 (CNT2) is a protein that in humans is encoded by the SLC28A2 gene.

<span class="mw-page-title-main">HAS1</span> Protein-coding gene in the species Homo sapiens

Hyaluronan synthase 1 is an enzyme that in humans is encoded by the HAS1 gene.

<span class="mw-page-title-main">Concentrative nucleoside transporter 1</span> The gene that determine size of cells

Concentrative nucleoside transporter 1 (CNT1) is a protein that in humans is encoded by the SLC28A1 gene.

<span class="mw-page-title-main">Aquaporin-5</span> Protein-coding gene in the species Homo sapiens

Aquaporin-5 (AQP-5) is a protein that in humans is encoded by the AQP5 gene.

<span class="mw-page-title-main">Aquaporin-9</span> Protein-coding gene in the species Homo sapiens

Aquaporin-9 (AQP-9) is a protein that in humans is encoded by the AQP9 gene.

<span class="mw-page-title-main">RHCG</span> Protein-coding gene in the species Homo sapiens

Rh family, C glycoprotein, also known as RHCG, is a protein that in humans is encoded by the RHCG gene.

<span class="mw-page-title-main">Aquaporin-8</span> Protein-coding gene in the species Homo sapiens

Aquaporin-8 is a protein that in humans is encoded by the AQP8 gene.

<span class="mw-page-title-main">Aquaporin-7</span> Protein-coding gene in the species Homo sapiens

Aquaporin-7 (AQP-7) is a protein that in humans is encoded by the AQP7 gene.

<span class="mw-page-title-main">Ankyrin-3</span> Protein-coding gene in the species Homo sapiens

Ankyrin-3 (ANK-3), also known as ankyrin-G, is a protein from ankyrin family that in humans is encoded by the ANK3 gene.

<span class="mw-page-title-main">Mitochondrial ferritin</span> Protein-coding gene in the species Homo sapiens

Mitochondrial ferritin is a ferroxidase enzyme that in humans is encoded by the FTMT gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000165272 - Ensembl, May 2017
  2. 1 2 3 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. 1 2 3 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. 1 2 3 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. 1 2 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. 1 2 3 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