アクアポリン5 aquaporin 5
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2017/03/05 10:41:30」(JST)
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AQP5 |
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Available structures |
PDB |
Ortholog search: PDBe RCSB |
List of PDB id codes |
3D9S, 5C5X, 5DYE
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Identifiers |
Aliases |
AQP5, AQP-5, PPKB, aquaporin 5 |
External IDs |
MGI: 106215 HomoloGene: 20398 GeneCards: AQP5 |
Gene ontology |
Molecular function |
• transporter activity
• protein binding
• water channel activity
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Cellular component |
• integral component of membrane
• membrane
• plasma membrane
• integral component of plasma membrane
• microvillus
• basal plasma membrane
• apical plasma membrane
• endoplasmic reticulum
• extracellular exosome
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Biological process |
• excretion
• water transport
• pancreatic juice secretion
• saliva secretion
• odontogenesis
• ion transmembrane transport
• transport
• camera-type eye morphogenesis
• carbon dioxide transport
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Sources:Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) |
Chr 12: 49.96 – 49.97 Mb |
Chr 15: 99.59 – 99.59 Mb |
PubMed search |
[1] |
[2] |
Wikidata |
View/Edit Human |
View/Edit Mouse |
Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene.[3][4]
Aquaporin 5 (AQP5) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. AQP0, AQP2, AQP5, and AQP6 are closely related and all map to 12q13.[4]
Contents
- 1 See also
- 2 References
- 3 Further reading
- 4 External links
See also
References
- ^ "Human PubMed Reference:".
- ^ "Mouse PubMed Reference:".
- ^ Lee MD, Bhakta KY, Raina S, Yonescu R, Griffin CA, Copeland NG, Gilbert DJ, Jenkins NA, Preston GM, Agre P (Jun 1996). "The human Aquaporin-5 gene. Molecular characterization and chromosomal localization". J Biol Chem. 271 (15): 8599–604. doi:10.1074/jbc.271.15.8599. PMID 8621489.
- ^ a b "Entrez Gene: AQP5 aquaporin 5".
Further reading
- Verkman AS (2003). "Role of aquaporin water channels in eye function.". Exp. Eye Res. 76 (2): 137–43. doi:10.1016/S0014-4835(02)00303-2. PMID 12565800.
- 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.
- Smith JK, Siddiqui AA, Modica LA, et al. (1999). "Interferon-alpha upregulates gene expression of aquaporin-5 in human parotid glands.". J. Interferon Cytokine Res. 19 (8): 929–35. doi:10.1089/107999099313479. PMID 10476940.
- Kreda SM, Gynn MC, Fenstermacher DA, et al. (2001). "Expression and localization of epithelial aquaporins in the adult human lung.". Am. J. Respir. Cell Mol. Biol. 24 (3): 224–34. doi:10.1165/ajrcmb.24.3.4367. PMID 11245621.
- Gresz V, Kwon TH, Hurley PT, et al. (2001). "Identification and localization of aquaporin water channels in human salivary glands.". Am. J. Physiol. Gastrointest. Liver Physiol. 281 (1): G247–54. PMID 11408278.
- Nejsum LN, Kwon TH, Jensen UB, et al. (2002). "Functional requirement of aquaporin-5 in plasma membranes of sweat glands.". Proc. Natl. Acad. Sci. U.S.A. 99 (1): 511–6. doi:10.1073/pnas.012588099. PMC 117591. PMID 11773623.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Burghardt B, Elkaer ML, Kwon TH, et al. (2003). "Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas.". Gut. 52 (7): 1008–16. doi:10.1136/gut.52.7.1008. PMC 1773699. PMID 12801959.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Chen Z, Wang X, Gao L, et al. (2006). "Regulation of MUC5AC mucin secretion by depletion of AQP5 in SPC-A1 cells.". Biochem. Biophys. Res. Commun. 342 (3): 775–81. doi:10.1016/j.bbrc.2006.01.103. PMID 16500622.
- Sidhaye VK, Güler AD, Schweitzer KS, et al. (2006). "Transient receptor potential vanilloid 4 regulates aquaporin-5 abundance under hypotonic conditions.". Proc. Natl. Acad. Sci. U.S.A. 103 (12): 4747–52. doi:10.1073/pnas.0511211103. PMC 1450241. PMID 16537379.
- Pedersen PS, Braunstein TH, Jørgensen A, et al. (2007). "Stimulation of aquaporin-5 and transepithelial water permeability in human airway epithelium by hyperosmotic stress.". Pflugers Arch. 453 (6): 777–85. doi:10.1007/s00424-006-0157-3. PMID 17043812.
- Skowron-zwarg M, Boland S, Caruso N, et al. (2007). "Interleukin-13 interferes with CFTR and AQP5 expression and localization during human airway epithelial cell differentiation.". Exp. Cell Res. 313 (12): 2695–702. doi:10.1016/j.yexcr.2007.02.035. PMID 17553491.
External links
- AQP5 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
- Human AQP5 genome location and AQP5 gene details page in the UCSC Genome Browser.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Membrane transport protein: ion channels (TC 1A)
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Ca2+: Calcium channel
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Ligand-gated |
- Inositol trisphosphate receptor
- Ryanodine receptor
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Voltage-gated |
- L-type/Cavα
- N-type/Cavα2.2
- P-type/Cavα
- Q-type/Cavα2.1
- R-type/Cavα2.3
- T-type/Cavα
- α2δ-subunits
- β-subunits
- γ-subunits
- Cation channels of sperm
- Two-pore channel
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Na+: Sodium channel
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Constitutively active |
- Epithelial sodium channel
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Proton-gated |
- Amiloride-sensitive cation channel
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Voltage-gated |
- Navα
- 1.1
- 1.2
- 1.3
- 1.4
- 1.5
- 1.6
- 1.7
- 1.8
- 1.9
- 7A
- Navβ
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K+: Potassium channel
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Calcium-activated |
- BK channel
- SK channel
- IK channel
- KCa
- 1.1
- 2.1
- 2.2
- 2.3
- 3.1
- 4.1
- 4.2
- 5.1
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Inward-rectifier |
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Tandem pore domain |
- K2P
- 1
- 2
- 3
- 4
- 5
- 6
- 7
- 9
- 10
- 12
- 13
- 15
- 16
- 17
- 18
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Voltage-gated |
- Kvα1-6
- 1.1
- 1.2
- 1.3
- 1.4
- 1.5
- 1.6
- 1.7
- 1.8
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- Kvβ
- KCNIP
- minK/ISK
- minK/ISK-like
- MiRP
- Shaker gene
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Miscellaneous
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Cl−: Chloride channel |
- Calcium-activated chloride channels
- Anoctamin
- Bestrophin
- Chloride Channel Accessory
- CFTR
- CLCN
- CLIC
- CLNS
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H+: Proton channel |
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M+: CNG cation channel |
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M+: TRP cation channel |
- TRPA (1)
- TRPC
- TRPM
- TRPML
- TRPN
- TRPP
- TRPV
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H2O (+ solutes): Porin |
- Aquaporin
- Voltage-dependent anion channel
- General bacterial porin family
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Cytoplasm: Gap junction |
- Connexin: A
- GJA1
- GJA3
- GJA4
- GJA5
- GJA8
- GJA9
- GJA10
- B
- GJB1
- GJB2
- GJB3
- GJB4
- GJB5
- GJB6
- GJB7
- C
- D
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By gating mechanism
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Ion channel class |
- Ligand-gated
- Light-gated
- Voltage-gated
- Stretch-activated
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see also disorders
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UpToDate Contents
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English Journal
- Cellular overexpression of Aquaporins slows down the natural HIF-2α degradation during prolonged hypoxia.
- Galán-Cobo A, Sánchez-Silva R, Serna A, Abreu-Rodríguez I, Muñoz-Cabello AM, Echevarría M.SourceInstituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocío/CSIC/Universidad de Sevilla, Departamento de Fisiología Médica y Biofísica, Seville, Spain.
- Gene.Gene.2013 Jun 10;522(1):18-26. doi: 10.1016/j.gene.2013.03.075. Epub 2013 Mar 29.
- Overexpression of cell membrane aquaporins (AQPs) has recently been associated with tumor formation, particularly with angiogenesis, cell migration and proliferation. Additionally, the hypoxia inducible factor (HIF) family has been extensively implicated in tumor growth and recent studies evidence i
- PMID 23545307
- Regulated traffic of anion transporters in mammalian Brunner's glands: a role for water and fluid transport.
- Collaco AM, Jakab RL, Hoekstra N, Mitchell K, Brooks A, Ameen NA.Source1Yale University School of Medicine.
- American journal of physiology. Gastrointestinal and liver physiology.Am J Physiol Gastrointest Liver Physiol.2013 Jun 6. [Epub ahead of print]
- The Brunner's glands of the proximal duodenum exert barrier functions through secretion of glycoproteins and antimicrobial peptides. However, ion transporter localization, function, and regulation in the glands are less clear. Mapping the subcellular distribution of transporters is an important step
- PMID 23744739
- Mesenchymal stem cells protect against neonatal rat hyperoxic lung injury.
- Zhang H, Fang J, Wu Y, Mai Y, Lai W, Su H.SourceSun Yat-Sen Memorial Hospital of Sun Yat-Sen University, Department of Pediatric , Yanjiang Road 107, Guangzhou, Guangdong 510120 , China +86 20 13642640725 ; zhhosh@126.com.
- Expert opinion on biological therapy.Expert Opin Biol Ther.2013 Jun;13(6):817-29. doi: 10.1517/14712598.2013.778969. Epub 2013 Mar 27.
- Objectives: Bronchopulmonary dysplasia (BPD) is a significant global health problem and currently lacks effective therapy. We established a neonatal rat model of BPD to investigate therapeutic potential of bone marrow-derived mesenchymal stem cells (BMSCs) in neonatal hyperoxic lung injury. Methods:
- PMID 23534609
Japanese Journal
- 町田 雄一郎,上田 善道,上野 正克,田中 良,相川 広一,薄田 勝男,佐川 元保,佐久間 勉
- 肺癌 52(1), 17-22, 2012
- … 現と進展への関与に関する知見を紹介する.結果.肺癌ではAQP1,3,4,5が腺癌細胞に発現する.その発現は,1)細胞分化に相当する極性を有するAQP1,3の発現,2)極性は保たれるが正常肺では認められないAQP5の異所性発現,3)極性を喪失したAQP1,5の過剰発現に区分される.1)は細気管支肺胞上皮癌に高頻度で,進展に伴い減少する.2)は肺胞上皮癌のみならず異型腺腫様過形成でも見られ,腫瘍発生に関係して …
- NAID 130002060207
- Function of the Membrane Water Channel Aquaporin-5 in the Salivary Gland
- Matsuzaki Toshiyuki,Susa Taketo,Shimizu Kinue,Sawai Nobuhiko,Suzuki Takeshi,Aoki Takeo,Yokoo Satoshi,Takata Kuniaki
- ACTA HISTOCHEMICA ET CYTOCHEMICA 45(5), 251-259, 2012
- … It is well known that aquaporin-5 (AQP5) is expressed in the salivary glands, in which it is mainly localized at the apical membrane of the acinar cells. … This suggests the physiological importance of AQP5 in transcellular water transfer. … Reduced saliva secretion under pilocarpine stimulation in AQP5-null mice compared with normal mice further indicates the importance of AQP5 in this process, at least in stimulated saliva secretion. …
- NAID 130001854258
- Autonomic Nerve-Regulated AQP5 Distribution in Salivary Glands and AQP5 Release into Saliva
- WANG Di,ISHIKAWA Yasuko
- Journal of oral biosciences 53(1), 38-47, 2011-02-20
- NAID 10027793648
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アクアポリン aquaporin