AQP2

アクアポリン2 aquaporin 2

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/08/15 00:56:16」(JST)

wiki en

[Wiki en表示]

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. リチウムの腎毒性 renal toxicity of lithium
• 2. 小児における高ナトリウム血症 hypernatremia in children

English Journal

• Localisation and expression of aquaporin subtypes in epithelial ovarian tumours.

• Yang JH, Yu YQ, Yan CX.SourceDepartment of Gynaecology, Second Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, China.
• Histology and histopathology.Histol Histopathol.2011 Sep;26(9):1197-205.
• To characterise AQP subtype localisation and expression in epithelial ovarian tumours, immunohistochemistry was used to assess the localisation and expression of AQP1-9 in 30 benign tumour cases, 30 borderline tumour cases, 50 malignant tumour cases and 20 normal ovarian tissue cases. Multiple AQP s
• PMID 21751151

• Different effects of CsA and FK506 on aquaporin-2 abundance in rat primary cultured collecting duct cells.

• Rinschen MM, Klokkers J, Pavenstadt H, Neugebauer U, Schlatter E, Edemir B.SourceMedizinische Klinik und Poliklinik D, Experimentelle Nephrologie, Universitat Munster, Domagkstrase 3a, 48149, Munster, Germany.
• Pflugers Archiv : European journal of physiology.Pflugers Arch.2011 Jul 20. [Epub ahead of print]
• Calcineurin (Cn) inhibitors (CnI) such as cyclosporine A (CsA) and FK506 are nephrotoxic immunosuppressant drugs, which decrease tubular function. Here, we examined the direct effect of CnI on aquaporin-2 (AQP2) expression in rat primary cultured inner medullary collecting duct cells. CsA (0.5-5?μ
• PMID 21773745

Japanese Journal

• 使用経験 トルバプタン投与例における尿中AQP2の意義 (肝性浮腫 : 病態・診断・薬物療法)

• 細川 貴範,黒崎 雅之,泉 並木
• Fluid management renaissance 4(15増刊), 103-107, 2014-11
• NAID 40020284810

• 腎性尿崩症 : 多飲・多尿の鑑別診断 (特集 日常診療で遭遇する小児腎泌尿器疾患とトピックス) -- (尿細管疾患・囊胞性腎疾患)

• 三浦 健一郎
• 小児科診療 77(6), 749-755, 2014-06
• NAID 40020099385

• バソプレシン／バソトシンの浸透圧調節作用からみた脊椎動物の環境適応と進化

• 今野 紀文
• 比較生理生化学 31(2), 68-74, 2014
• … この水を保持する作用は，V2受容体を介した水チャネル（AQP2）の発現促進によって発揮されるが，この仕組み（VP/VT-V2受容体-AQP2系）はこれまで両生類以降の動物群でしか見つかっておらず，原始的な両生類の陸上進出に伴って獲得されたと考えられてきた。 …
• NAID 130004501991

Related Links

• 2012生理学特論 水チャネル - 明治薬科大学 薬学部／大学院

AQP2小胞小胞 管腔膜 癒合の管腔膜への癒合 37 AQP2小胞の管腔膜への癒合 • シナプ胞似るプス小胞に似る • v‐SNARE（小胞）とt‐SNARE（管腔膜） • v‐SNARE：VAMP‐2, synaptobrevin • t‐SNARE: SNAP‐23, syntaxin3 ...

• AQP2 抗体(N-20) | Santa Cruz Biotech

AQP2 Antibody (N-20) is a goat polyclonal IgG provided at 200 µg/ml epitope mapping at the N-terminus of AQP2 of human origin recommended for detection of AQP0, AQP1, AQP2, AQP4, AQP5 and AQP6 of mouse, rat and human ...

Related Pictures

---

★リンクテーブル★

リンク元	「アクアポリン2」「aquaporin 2」
関連記事	「AQP」

「アクアポリン2」

　　[★]

英

aquaporin-2, AQP-2 AQP2

関

アクアポリン、バソプレシン

概念

• 血管側の細胞膜に存在するV2受容体にAVPが結合すると、Gs蛋白、アデニル酸シクラーゼ、プロテインキナーゼAを介し、AQP2に作用する。細胞質内に存在するAQP2粒子は尿細管の管腔側細胞膜上へ移動し、それを通して水再吸収・尿濃縮作用が発現する。

(1)

• Aquaporin-2 (AQP-2)は集合管でAVPに調整される水チャネル。
• 約3%のAQP-2が尿に排泄されている。
• 尿のAQP-2レベルは血清AVPと正の相関がある。
• 尿AQP-2レベルはAVPに依存した水代謝にまつわる疾患の診断において有用な指標である。

(2)

• バソプレッシンの作用で管腔側細胞膜にエキソサイトーシスされたAQP2 は、その一部が尿中に排泄される。健常者および中枢性尿崩症の患者では、バソプレッシンを投与することで尿中に排泄されるAQP2が増加するが、先天性腎性尿崩症の患者では、バソプレッシンを投与しても尿中に排泄されるAQP2 は増加しない。つまりバソプレッシンを投与して尿中のAQP2 排泄量の変化を調べることで、バソプレッシンが集合管に作用しているか否かを知ることができる。

参考文献

• 1. Ishikawa S., Urinary excretion of aquaporin-2 in pathological states of water metabolism., Ann Med. 2000 Mar;32(2):90-3.

• PMID 10766399

• 2. 松崎利行；―綜説―細胞膜水チャネル，アクアポリン 腎臓を中心にして；日医大医会誌2009; 5（2）

http://www.nms.ac.jp/jmanms/pdf/005020118.pdf

「aquaporin 2」

　　[★]

アクアポリン2

関

AQP2

「AQP」

　　[★] アクアポリン aquaporin