aquaporin 2

アクアポリン2

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AQP2

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/09/01 11:47:49」(JST)

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Aquaporin 2 (collecting duct)
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4NEF, 4OJ2
Identifiers
Symbols	AQP2 ; AQP-CD; WCH-CD
External IDs	OMIM: 107777 MGI: 1096865 HomoloGene: 20137 IUPHAR: 689 GeneCards: AQP2 Gene
Gene ontology Molecular function • water transmembrane transporter activity • glycerol transmembrane transporter activity • water channel activity • glycerol channel activity Cellular component • Golgi apparatus • plasma membrane • integral component of plasma membrane • membrane • basolateral plasma membrane • apical plasma membrane • transport vesicle membrane • recycling endosome • extracellular exosome Biological process • renal water homeostasis • renal water transport • water transport • excretion • cellular water homeostasis • glycerol transport • ion transmembrane transport • cellular response to water deprivation • transmembrane transport • cellular response to copper ion • cellular response to mercury ion • metanephric collecting duct development Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	359	11827
Ensembl	ENSG00000167580	ENSMUSG00000023013
UniProt	P41181	P56402
RefSeq (mRNA)	NM_000486	NM_009699
RefSeq (protein)	NP_000477	NP_033829
Location (UCSC)	Chr 12: 49.95 – 49.96 Mb	Chr 15: 99.58 – 99.58 Mb
PubMed search	[1]	[2]

AQP2 is found in the apical cell membranes of the kidney's collecting duct principal cells and in intracellular vesicles located throughout the cell.

Regulation

It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its being removed from the blood by the kidney. Aquaporin 2 is in kidney epithelial cells and usually lies dormant in intracellular vesicle membranes, but when it is needed vasopressin binds to the cell surface vasopressin receptor, activating a signaling pathway that causes the aquaporin 2 containing vesicles to fuse with the plasma membrane so the aquaporin 2 can be used by the cell.

This aquaporin is regulated in two ways by the peptide hormone vasopressin:

• short-term regulation (minutes) through trafficking of AQP2 vesicles to the apical region where they fuse with the apical plasma membrane
• long-term regulation (days) through an increase in AQP2 gene expression.

This aquaporin is also regulated by food intake. Fasting reduces expression of this aquaporin independently of vasopressin.

Clinical significance

Mutations in this channel are associated with nephrogenic diabetes insipidus, which can be autosomal dominant or recessive. Mutations in the vasopressin receptor cause a similar X-linked phenotype.

Lithium, which is often used to treat bipolar disorder, can cause acquired diabetes insipidus (characterized by the excretion of large volumes of dilute urine) by decreasing the expression of the AQP2 gene.

The expression of the AQP2 gene is increased during conditions associated with water retention such as pregnancy and congestive heart failure.

See also

• Aquaporin

References

Further reading

• Bichet DG (2006). "Nephrogenic diabetes insipidus". Advances in chronic kidney disease 13 (2): 96–104. doi:10.1053/j.ackd.2006.01.006. PMID 16580609. 
• Bouley R, Hasler U, Lu HAJ, Nunes P, Brown D (2008). "Bypassing vasopressin signaling pathways in nephrogenic diabetes insipidus". Sem. Nephrol. 28 (3): 266–78. doi:10.1016/j.semnephrol.2008.03.010. PMC 2494582. PMID 18519087. 
• Robben JH, Knoers NV, Deen PM (2006). "Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus". Am. J. Physiol. Renal Physiol. 291 (2): F257–70. doi:10.1152/ajprenal.00491.2005. PMID 16825342. 
• Sasaki S, Fushimi K, Saito H et al. (1994). "Cloning, characterization, and chromosomal mapping of human aquaporin of collecting duct". J. Clin. Invest. 93 (3): 1250–6. doi:10.1172/JCI117079. PMC 294077. PMID 7510718. 
• Deen PM, Weghuis DO, Sinke RJ et al. (1994). "Assignment of the human gene for the water channel of renal collecting duct Aquaporin 2 (AQP2) to chromosome 12 region q12→q13". Cytogenet. Cell Genet. 66 (4): 260–2. doi:10.1159/000133707. PMID 7512890. 
• Uchida S, Sasaki S, Fushimi K, Marumo F (1994). "Isolation of human aquaporin-CD gene". J. Biol. Chem. 269 (38): 23451–5. PMID 7522228. 
• van Lieburg AF, Verdijk MA, Knoers VV et al. (1994). "Patients with autosomal nephrogenic diabetes insipidus homozygous for mutations in the aquaporin 2 water-channel gene". Am. J. Hum. Genet. 55 (4): 648–52. PMC 1918308. PMID 7524315. 
• Saito F, Sasaki S, Chepelinsky AB et al. (1994). "Human AQP2 and MIP genes, two members of the MIP family, map within chromosome band 12q13 on the basis of two-color FISH". Cytogenet. Cell Genet. 68 (1–2): 45–8. doi:10.1159/000133885. PMID 7525161. 
• Nielsen S, Chou CL, Marples D et al. (1995). "Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane". Proc. Natl. Acad. Sci. U.S.A. 92 (4): 1013–7. doi:10.1073/pnas.92.4.1013. PMC 42627. PMID 7532304. 
• Brown D (2003). "The ins and outs of aquaporin 2 trafficking". Am. J. Physiol. Renal Physiol. 284 (5): F893–901. doi:10.1152/ajprenal.00387.2002. PMID 12676734. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Deen PM, Verdijk MA, Knoers NV et al. (1994). "Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine". Science 264 (5155): 92–5. doi:10.1126/science.8140421. PMID 8140421. 
• Oksche A, Möller A, Dickson J et al. (1996). "Two novel mutations in the aquaporin-2 and the vasopressin V2 receptor genes in patients with congenital nephrogenic diabetes insipidus". Hum. Genet. 98 (5): 587–9. doi:10.1007/s004390050264. PMID 8882880. 
• Mulders SM, Knoers NV, Van Lieburg AF et al. (1997). "New mutations in the AQP2 gene in nephrogenic diabetes insipidus resulting in functional but misrouted water channels". J. Am. Soc. Nephrol. 8 (2): 242–8. PMID 9048343. 
• Ma T, Yang B, Umenishi F, Verkman AS (1997). "Closely spaced tandem arrangement of AQP2, AQP5, and AQP6 genes in a 27-kilobase segment at chromosome locus 12q13". Genomics 43 (3): 387–9. doi:10.1006/geno.1997.4836. PMID 9268644. 
• Canfield MC, Tamarappoo BK, Moses AM et al. (1998). "Identification and characterization of aquaporin-2 water channel mutations causing nephrogenic diabetes insipidus with partial vasopressin response". Hum. Mol. Genet. 6 (11): 1865–71. doi:10.1093/hmg/6.11.1865. PMID 9302264. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Vargas-Poussou R, Forestier L, Dautzenberg MD et al. (1998). "Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12 families with congenital nephrogenic diabetes insipidus". J. Am. Soc. Nephrol. 8 (12): 1855–62. PMID 9402087. 
• Kuwahara M (1998). "Aquaporin-2, a vasopressin-sensitive water channel, and nephrogenic diabetes insipidus". Intern. Med. 37 (2): 215–7. doi:10.2169/internalmedicine.37.215. PMID 9550615. 
• Mulders SM, Bichet DG, Rijss JP et al. (1998). "An aquaporin-2 water channel mutant which causes autosomal dominant nephrogenic diabetes insipidus is retained in the Golgi complex". J. Clin. Invest. 102 (1): 57–66. doi:10.1172/JCI2605. PMC 509065. PMID 9649557. 
• Goji K, Kuwahara M, Gu Y et al. (1998). "Novel mutations in aquaporin-2 gene in female siblings with nephrogenic diabetes insipidus: evidence of disrupted water channel function". J. Clin. Endocrinol. Metab. 83 (9): 3205–9. doi:10.1210/jc.83.9.3205. PMID 9745427. 
• Saito T, Ishikawa S, Ito T et al. (1999). "Urinary excretion of aquaporin-2 water channel differentiates psychogenic polydipsia from central diabetes insipidus". J. Clin. Endocrinol. Metab. 84 (6): 2235–7. doi:10.1210/jc.84.6.2235. PMID 10372737. 

External links

• GeneReviews/NCBI/NIH/UW entry on Nephrogenic Diabetes Insipidus
• Aquaporin 2 at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

• 1. 腎性尿崩症の臨床症状および原因 clinical manifestations and causes of nephrogenic diabetes insipidus
• 2. 低カリウム血症誘発性腎機能障害 hypokalemia induced renal dysfunction
• 3. 抗利尿ホルモン不適合分泌（SIADH）症候群の病態生理および病因 pathophysiology and etiology of the syndrome of inappropriate antidiuretic hormone secretion siadh
• 4. リチウムの腎毒性 renal toxicity of lithium
• 5. 多尿および尿崩症の診断 diagnosis of polyuria and diabetes insipidus

English Journal

• Exogenous Vasopressin-Induced Hyponatremia in Patients With Vasodilatory Shock: Two Case Reports and Literature Review.

• Salazar M, Hu BB, Vazquez J, Wintz RL, Varon J.SourceDepartment of Pharmacy Practice, Lerma Rangel College of Pharmacy, Texas A&M Health Science Center, Kingsville, TX, USA.
• Journal of intensive care medicine.J Intensive Care Med.2013 Oct 7. [Epub ahead of print]
• Vasopressin has gained wide support as an adjunct vasopressor in patients with septic shock. This agent exerts its vasoconstriction effects through smooth muscle V1 receptors and also has antidiuretic activity via renal V2 receptors. This interaction with the renal V2 receptors results in the integr
• PMID 24106070

• Renal β-intercalated cells maintain body fluid and electrolyte balance.

• Gueutin V, Vallet M, Jayat M, Peti-Peterdi J, Cornière N, Leviel F, Sohet F, Wagner CA, Eladari D, Chambrey R.AbstractInactivation of the B1 proton pump subunit (ATP6V1B1) in intercalated cells (ICs) leads to type I distal renal tubular acidosis (dRTA), a disease associated with salt- and potassium-losing nephropathy. Here we show that mice deficient in ATP6V1B1 (Atp6v1b1-/- mice) displayed renal loss of NaCl, K+, and water, causing hypovolemia, hypokalemia, and polyuria. We demonstrated that NaCl loss originated from the cortical collecting duct, where activity of both the epithelial sodium channel (ENaC) and the pendrin/Na+-driven chloride/bicarbonate exchanger (pendrin/NDCBE) transport system was impaired. ENaC was appropriately increased in the medullary collecting duct, suggesting a localized inhibition in the cortex. We detected high urinary prostaglandin E2 (PGE2) and ATP levels in Atp6v1b1-/- mice. Inhibition of PGE2 synthesis in vivo restored ENaC protein levels specifically in the cortex. It also normalized protein levels of the large conductance calcium-activated potassium channel and the water channel aquaporin 2, and improved polyuria and hypokalemia in mutant mice. Furthermore, pharmacological inactivation of the proton pump in β-ICs induced release of PGE2 through activation of calcium-coupled purinergic receptors. In the present study, we identified ATP-triggered PGE2 paracrine signaling originating from β-ICs as a mechanism in the development of the hydroelectrolytic imbalance associated with dRTA. Our data indicate that in addition to principal cells, ICs are also critical in maintaining sodium balance and, hence, normal vascular volume and blood pressure.
• The Journal of clinical investigation.J Clin Invest.2013 Oct 1;123(10):4219-4231. doi: 10.1172/JCI63492. Epub 2013 Sep 24.
• Inactivation of the B1 proton pump subunit (ATP6V1B1) in intercalated cells (ICs) leads to type I distal renal tubular acidosis (dRTA), a disease associated with salt- and potassium-losing nephropathy. Here we show that mice deficient in ATP6V1B1 (Atp6v1b1-/- mice) displayed renal loss of NaCl, K+,
• PMID 24051376

• Quantitative apical membrane proteomics reveals vasopressin-induced actin dynamics in collecting duct cells.

• Loo CS, Chen CW, Wang PJ, Chen PY, Lin SY, Khoo KH, Fenton RA, Knepper MA, Yu MJ.SourceInstitute of Biochemistry and Molecular Biology, National Taiwan University College of Medicine, Taipei 10051, Taiwan.
• Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2013 Oct 1. [Epub ahead of print]
• In kidney collecting duct cells, filamentous actin (F-actin) depolymerization is a critical step in vasopressin-induced trafficking of aquaporin-2 to the apical plasma membrane. However, the molecular components of this response are largely unknown. Using stable isotope-based quantitative protein ma
• PMID 24085853

Japanese Journal

• Developmental Ability of Vitrified Mouse Oocytes Expressing Water Channels

• YAMAJI Yohei,SEKI Shinsuke,MATSUKAWA Kazutsugu,KOSHIMOTO Chihiro,KASAI Magosaburo,EDASHIGE Keisuke
• The Journal of reproduction and development 57(3), 403-408, 2011-06-01
• NAID 10029050757

• 低温下でのイネの水吸収とアクアポリン(セミナー「生物のストレス受容のメカニズム-分子レベルから細胞レベルまで-」)

• 村井(羽田野) 麻理,櫻井(石川) 淳子,桑形 恒男,林 秀洋,アハメド アリファ,長管 輝義
• 低温生物工学会誌 57(1), 7-12, 2011-04-15
• Ability of plants to regulate the hydraulic conductivity inside the plant is crucial for sound growth and survival under adverse environment. In this manuscript, we demonstrated that low-root-temperat …
• NAID 110008671114

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