Aquaporin 3 is found in the basolateral cell membrane of principal collecting duct cells and provide a pathway for water to exit these cells.[1] In kidney, AQP3 gene expression is not regulated by vasopressin (ADH).[2] This protein is also a determinant for the GIL blood group system.[3] [edit] See also [edit] References - ^ 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.
- ^ 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. PMID 9824541. http://www.ebmonline.org/cgi/content/abstract/219/3/183.
- ^ 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.
[edit] 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.
- 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.
- 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.
- 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.
- Olsson M, Broberg A, Jernås 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.
- 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. 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.
- 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. 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
[edit] External links | Membrane transport protein: ion channels | | | Ca2+: Calcium channel | | | | L-type/ Cavα ( 1.1, 1.2, 1.3, 1.4) · N-type/ Cavα2.2 · P-type/ Cavα( 2.1) · Q-type/ Cavα2.1 · R-type/ Cavα2.3 · T-type/ Cavα( 3.1, 3.2, 3.3) α2δ-subunits ( 1, 2) · β-subunits ( β1, β2, β3, β4) · γ-subunits ( γ1, γ2, γ3, γ4) Cation channels of sperm ( 1, 2, 3, 4) · Two-pore channel ( 1, 2) | | | Ligand-gated | | | | | | Na+: Sodium channel | | | | Navα ( 1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 7A) · Navβ ( 1, 2, 3, 4) | | | Constitutively active | | | | | | K+: Potassium channel | | | | Kvα1-6 ( 1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.10) · ( 2.1, 2.2) · ( 3.1, 3.2, 3.3, 3.4) · ( 4.1, 4.2, 4.3) · ( 5.1) · ( 6.1, 6.2, 6.3, 6.4) Kvα7-12 ( 7.1, 7.2, 7.3, 7.4, 7.5) · ( 8.1, 8.2) · ( 9.1, 9.2, 9.3) · ( 10.1, 10.2) · ( 11.1/hERG, 11.2, 11.3) · ( 12.1, 12.2, 12.3) Kvβ ( 1, 2, 3) · KCNIP ( 1, 2, 3, 4) · minK/ISK · minK/ISK-like · MiRP ( 1, 2, 3) · Shaker gene | | | | BK channel ( α1, β1, β2, β3, β4) · SK channel ( SK1, SK2, SK3, SK4) · KCa ( 1.1, 2.1, 2.2, 2.3, 3.1, 4.1, 4.2, 5.1) | | | | Kir ( 1.1, 2.1, 2.2, 2.3, 2.4) · GIRK/ Kir ( 3.1, 3.2, 3.3, 3.4) · Kir ( 4.1, 4.2, 5.1, 6.1, 6.2, 7.1) | | | | K2P ( 1, 2, 3, 4, 5, 6, 7, 9, 10, 12, 13, 15, 16, 17, 18) | | | | | Other | | | | | TRPA ( 1) · TRPC ( 1, 2, 3, 4, 4AP, 5, 6, 7) · TRPM ( 1, 2, 3, 4, 5, 6, 7, 8) · TRPML ( 1, 2, 3) · TRPP ( 1, 2) · TRPV ( 1, 2, 3, 4, 5, 6) | | | | ANO1 · Bestrophin ( 1, 2) · CFTR · CLCA ( 1, 2, 3, 4) · CLCN ( 1, 2, 3, 4, 5, 6, 7, KA, KB) · CLIC ( 1, 2, 3, 4, 5, 6, L1) · CLNS ( 1A, 1B) | | | | | | | | | | | General | | | | | | | | | |