• transporter activity • glycerol transmembrane transporter activity • water transmembrane transporter activity • water channel activity • protein binding • channel activity
Cellular component
• integral component of membrane • recycling endosome • Golgi apparatus • membrane • plasma membrane • transport vesicle membrane • basolateral plasma membrane • apical plasma membrane • extracellular exosome • cytoplasmic vesicle membrane • cytoplasmic vesicle • integral component of plasma membrane
Biological process
• cellular response to mercury ion • excretion • water transport • ion transmembrane transport • renal water transport • renal water homeostasis • cellular response to copper ion • metanephric collecting duct development • cellular response to water deprivation • glycerol transport • transport • transmembrane transport • protein homotetramerization
Sources:Amigo / QuickGO
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
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
AQP2 is found in the apical cell membranes of the kidney's collecting duct principal cells and in intracellular vesicles located throughout the cell.
Contents
1Regulation
2Clinical significance
3See also
4References
5Further reading
6External links
Regulation
It is the only aquaporin regulated by vasopressin.[5]
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. When it is needed, vasopressin binds to the cell surface vasopressin receptor thereby 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.[6]
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
^ abcGRCh38: Ensembl release 89: ENSG00000167580 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000023013 - Ensembl, May 2017
^"Human PubMed Reference:".
^"Mouse PubMed Reference:".
^Dibas AI, Mia AJ, Yorio T (December 1998). "Aquaporins (water channels): role in vasopressin-activated water transport". Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine. 219 (3): 183–99. doi:10.3181/00379727-219-44332. PMID 9824541.
^Lodish H, Berk A, Kaiser CA, Krieger M, Scott MP, Bretscher A, Ploegh H, Matsudaira P (2008). Molecular Cell Biology (6th ed.). New York: Freeman. p. 445. ISBN 978-0-7167-7601-7.
Bouley R, Hasler U, Lu HA, Nunes P, Brown D (May 2008). "Bypassing vasopressin receptor signaling pathways in nephrogenic diabetes insipidus". Seminars in Nephrology. 28 (3): 266–78. doi:10.1016/j.semnephrol.2008.03.010. PMC 2494582. PMID 18519087.
Robben JH, Knoers NV, Deen PM (August 2006). "Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus". American Journal of Physiology. Renal Physiology. 291 (2): F257–70. doi:10.1152/ajprenal.00491.2005. PMID 16825342.
Sasaki S, Fushimi K, Saito H, Saito F, Uchida S, Ishibashi K, Kuwahara M, Ikeuchi T, Inui K, Nakajima K (March 1994). "Cloning, characterization, and chromosomal mapping of human aquaporin of collecting duct". The Journal of Clinical Investigation. 93 (3): 1250–6. doi:10.1172/JCI117079. PMC 294077. PMID 7510718.
Deen PM, Weghuis DO, Sinke RJ, Geurts van Kessel A, Wieringa B, van Os CH (1994). "Assignment of the human gene for the water channel of renal collecting duct Aquaporin 2 (AQP2) to chromosome 12 region q12-->q13". Cytogenetics and Cell Genetics. 66 (4): 260–2. doi:10.1159/000133707. PMID 7512890.
Uchida S, Sasaki S, Fushimi K, Marumo F (September 1994). "Isolation of human aquaporin-CD gene". The Journal of Biological Chemistry. 269 (38): 23451–5. PMID 7522228.
van Lieburg AF, Verdijk MA, Knoers VV, van Essen AJ, Proesmans W, Mallmann R, Monnens LA, van Oost BA, van Os CH, Deen PM (October 1994). "Patients with autosomal nephrogenic diabetes insipidus homozygous for mutations in the aquaporin 2 water-channel gene". American Journal of Human Genetics. 55 (4): 648–52. PMC 1918308. PMID 7524315.
Saito F, Sasaki S, Chepelinsky AB, Fushimi K, Marumo F, Ikeuchi T (1994). "Human AQP2 and MIP genes, two members of the MIP family, map within chromosome band 12q13 on the basis of two-color FISH". Cytogenetics and Cell Genetics. 68 (1–2): 45–8. doi:10.1159/000133885. PMID 7525161.
Nielsen S, Chou CL, Marples D, Christensen EI, Kishore BK, Knepper MA (February 1995). "Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane". Proceedings of the National Academy of Sciences of the United States of America. 92 (4): 1013–7. doi:10.1073/pnas.92.4.1013. PMC 42627. PMID 7532304.
Brown D (May 2003). "The ins and outs of aquaporin-2 trafficking". American Journal of Physiology. Renal Physiology. 284 (5): F893–901. doi:10.1152/ajprenal.00387.2002. PMID 12676734.
Maruyama K, Sugano S (January 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, Wieringa B, Monnens LA, van Os CH, van Oost BA (April 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, Rosendahl W, Rascher W, Bichet DG, Rosenthal W (November 1996). "Two novel mutations in the aquaporin-2 and the vasopressin V2 receptor genes in patients with congenital nephrogenic diabetes insipidus". Human Genetics. 98 (5): 587–9. doi:10.1007/s004390050264. PMID 8882880.
Mulders SM, Knoers NV, Van Lieburg AF, Monnens LA, Leumann E, Wühl E, Schober E, Rijss JP, Van Os CH, Deen PM (February 1997). "New mutations in the AQP2 gene in nephrogenic diabetes insipidus resulting in functional but misrouted water channels". Journal of the American Society of Nephrology. 8 (2): 242–8. PMID 9048343.
Ma T, Yang B, Umenishi F, Verkman AS (August 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, Verkman AS, Holtzman EJ (October 1997). "Identification and characterization of aquaporin-2 water channel mutations causing nephrogenic diabetes insipidus with partial vasopressin response". Human Molecular Genetics. 6 (11): 1865–71. doi:10.1093/hmg/6.11.1865. PMID 9302264.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 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, Niaudet P, Déchaux M, Antignac C (December 1997). "Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12 families with congenital nephrogenic diabetes insipidus". Journal of the American Society of Nephrology. 8 (12): 1855–62. PMID 9402087.
Kuwahara M (February 1998). "Aquaporin-2, a vasopressin-sensitive water channel, and nephrogenic diabetes insipidus". Internal Medicine. 37 (2): 215–7. doi:10.2169/internalmedicine.37.215. PMID 9550615.
Mulders SM, Bichet DG, Rijss JP, Kamsteeg EJ, Arthus MF, Lonergan M, Fujiwara M, Morgan K, Leijendekker R, van der Sluijs P, van Os CH, Deen PM (July 1998). "An aquaporin-2 water channel mutant which causes autosomal dominant nephrogenic diabetes insipidus is retained in the Golgi complex". The Journal of Clinical Investigation. 102 (1): 57–66. doi:10.1172/JCI2605. PMC 509065. PMID 9649557.
Goji K, Kuwahara M, Gu Y, Matsuo M, Marumo F, Sasaki S (September 1998). "Novel mutations in aquaporin-2 gene in female siblings with nephrogenic diabetes insipidus: evidence of disrupted water channel function". The Journal of Clinical Endocrinology and Metabolism. 83 (9): 3205–9. doi:10.1210/jc.83.9.3205. PMID 9745427.
Saito T, Ishikawa S, Ito T, Oda H, Ando F, Higashiyama M, Nagasaka S, Hieda M, Saito T (June 1999). "Urinary excretion of aquaporin-2 water channel differentiates psychogenic polydipsia from central diabetes insipidus". The Journal of Clinical Endocrinology and Metabolism. 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)
Human AQP2 genome location and AQP2 gene details page in the UCSC Genome Browser.
v
t
e
Membrane transport protein: ion channels (TC 1A)
Ca2+: Calcium channel
Ligand-gated
Inositol trisphosphate receptor
1
2
3
Ryanodine receptor
1
2
3
Voltage-gated
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
Na+: Sodium channel
Constitutively active
Epithelial sodium channel
α
β
γ
δ
Proton-gated
Amiloride-sensitive cation channel
1
2
3
4
Voltage-gated
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
K+: Potassium channel
Calcium-activated
BK channel
α1
β1
β2
β3
β4
SK channel
SK1
SK2
SK3
IK channel
IK1
KCa
1.1
2.1
2.2
2.3
3.1
4.1
4.2
5.1
Inward-rectifier
KATP
Kir
1.1
2.1
2.2
2.3
2.4
2.6
GIRK/Kir
3.1
3.2
3.3
3.4
Kir
4.1
4.2
5.1
6.1
6.2
7.1
Tandem pore domain
K2P
1
2
3
4
5
6
7
9
10
12
13
15
16
17
18
Voltage-gated
Kvα1-6
1.1
1.2
1.3
1.4
1.5
1.6
1.7
1.8
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
Miscellaneous
Cl−: Chloride channel
Calcium-activated chloride channels
Anoctamin
ANO1
Bestrophin
1
2
Chloride Channel Accessory
1
2
3
4
CFTR
CLCN
1
2
3
4
5
6
7
KA
KB
CLIC
1
2
3
4
5
6
L1
CLNS
1A
1B
H+: Proton channel
HVCN1
M+: CNG cation channel
α
1
2
3
4
β
1
2
3
HCN
FC
1
2
3
4
M+: TRP cation channel
TRPA (1)
TRPC
1
2
3
4
4AP
5
6
7
TRPM
1
2
3
4
5
6
7
8
TRPML
1
2
3
TRPN
TRPP
1
2
TRPV
1
2
3
4
5
6
H2O (+ solutes): Porin
Aquaporin
0
1
2
3
4
5
6
7
8
9
Voltage-dependent anion channel
1
2
3
General bacterial porin family
Cytoplasm: Gap junction
Connexin
A
GJA1
GJA3
GJA4
GJA5
GJA8
GJA9
GJA10
B
GJB1
GJB2
GJB3
GJB4
GJB5
GJB6
GJB7
C
GJC1
GJC2
GJC3
D
GJD2
GJD3
GJD4
Innexin
By gating mechanism
Ion channel class
Ligand-gated
Light-gated
Voltage-gated
Stretch-activated
see also disorders
UpToDate Contents
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…the aquaporin-2 gene that encodes the ADH-sensitive water channels in the collecting tubule cells. This variant may have autosomal recessive or autosomal dominant modes of inheritance . Aquaporin-2 channels …
…incompletely understood. Two factors that play at least a contributory role are decreased expression of aquaporin-2, the water channel that fuses with the luminal membrane under the influence of antidiuretic hormone…
…appears to be mediated by decreased expression of aquaporin-2, the ADH-sensitive water channel in the collecting tubules . The regulation of aquaporin-2 in this setting appears to be unrelated to plasma …
…permeability of principal cells in the collecting tubule is regulated by antidiuretic hormone (ADH). Aquaporin-2 water channels (AQP2), which normally reside in the endosomes of principal cells, move to and fuse…
…the ADH receptor V2 and autosomal recessive and dominant nephrogenic DI due to mutations in the aquaporin-2 (water channel) gene. Nephrogenic DI presenting in adults is almost always acquired with chronic …
English Journal
Bile acid signaling in renal water regulation.
Li S, Li C, Wang W.
American journal of physiology. Renal physiology. 2019 May;().
Emerging evidence has shown that bile acids play important roles in renal physiology and diseases by activating two major receptors, the nuclear farnesoid X receptor (FXR) and the membrane G protein-coupled bile acid receptor-1 (Gpbar1, also known as TGR5). Both FXR and TGR5 have been identified in
A versatile aquaporin-2 cell system for quantitative temporal expression and live-cell imaging.
Holst MR, Nejsum LN.
American journal of physiology. Renal physiology. 2019 May;().
AQP2 fine-tunes urine concentration in response to the antidiuretic hormone vasopressin. In addition, AQP2 has been suggested to promote cell migration and epithelial morphogenesis. A cell system allowing temporal and quantitative control of expression levels of AQP2 and phospho-mimicking mutants ha
Protective effect of morin on doxorubicin-induced hepatorenal toxicity in rats.
Kuzu M, Yildirim S, Kandemir FM, Küçükler S, Çağlayan C, Türk E, Dörtbudak MB.
Chemico-biological interactions. 2019 May;().
Although Doxorubicin (DOX) is a widespread drug used in the treatment of cancer, its clinical use is restricted due to its common side effects. In addition, administrating DOX with an antioxidant has recently become a new strategy in preventing the side effects of DOX. The protective effects of mori
Increased serum C-reactive protein and decreased urinary aquaporin2 levels are predictive of the efficacy of tolvaptan in patients with liver cirrhosis
… Methods: Fifty-two patients were treated with TVP, with therapeutic effects judged by a decrease in body weight (>= 2 kg) and increase in urinary volume (>= 500 mL) within 7 days. … Blood biochemical tests were carried out at baseline and post-treatment, including serum soluble CD14 (sCD14) and urinary aquaporin2 (AQP2) levels. …
American Journal of Physiology. Renal Physiology 312(6), F1112-F1119, 2017-06
… Determination of urine protein and creatinine (Cr) concentrations and quantitative analyses of Pod-mRNA, nephrin mRNA (Nep-mRNA), synaptopodin mRNA (Syn-mRNA), and aquaporin2 mRNA expression were performed using RT-PCR in pelleted urine samples. …
Journal of Obstetrics and Gynaecology Research 43(5), 873-879, 2017-05
… This study was performed to examine whether podocyturia and urine aquaporin2 mRNA expression are increased in healthy pregnant women (PW) compared to healthy non-pregnant women (NPW). … Methods: Eleven urines obtained from 11 NPW and longitudinal 76 urines from 40 PW with uncomplicated pregnancies (median number [range] of urine samples/person, 2 [1 - 3]) were studied. …
This gene encodes a water channel protein located in the kidney collecting tubule. It belongs to the MIP/aquaporin family, some members of which are clustered together on chromosome 12q13. Mutations in this gene ...