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Aquaporin 6, kidney specific

Aquaporin 6, AQP6
The protein encoded by this gene is an aquaporin protein, which functions as a water channel in cells. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). This protein is specific for the kidney. This gene and related family members AQP0, AQP2, and AQP5 reside in a cluster on chromosome 12q13. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Aquaporin 1, AQP4, CD36, AQP9, AQP5
Papers on Aquaporin 6
Expression of AQP6 and AQP8 in epithelial ovarian tumor.
Chen et al., Hangzhou, China. In J Mol Histol, Feb 2016
In this study, we aimed to explore the distribution and expression differences of aquaporin 6 (AQP6) and aquaporin 8 (AQP8) in epithelial ovarian tumors.
Expression of Aquaporin-6 in Rat Retinal Ganglion Cells.
Park et al., Puch'ŏn, South Korea. In Cell Mol Neurobiol, Dec 2015
AQP6, which has low water permeability and transports mainly anions, was recently discovered in the eyes.
Analysis of aquaporin expression in liver with a focus on hepatocytes.
Delporte et al., Brussels, Belgium. In Histochem Cell Biol, Oct 2015
AQP1, AQP3, AQP7, AQP8, and AQP9 mRNA and protein expressions were detected in human liver, while only AQP6 and AQP11 mRNAs were detected.
Modification of aquaporin expression in response to fenretinide-induced transdifferentiation of ARPE-19 cells into neuronal-like cells.
Delporte et al., Brussels, Belgium. In Acta Ophthalmol, Oct 2015
RESULTS: Control ARPE-19 cells expressed AQP1, AQP4, AQP6 and AQP11 at the mRNA level, but only AQP4, AQP6 and AQP11 at the protein level.
Effects of estrogen deprivation on expression of aquaporins in rat vagina.
Lin et al., Taiwan. In Menopause, Aug 2015
OBJECTIVE: This study aims to investigate the expression of aquaporin (AQP) 0, AQP3, AQP5, AQP6, AQP10, AQP11, and AQP12 in the vaginal tissue of ovariectomized rats.
Molecular machinery for vasotocin-dependent transepithelial water movement in amphibians: aquaporins and evolution.
Okada et al., Shizuoka, Japan. In Biol Bull, Aug 2015
Anuran-specific AQPa2 was assigned to AQP6, then was further subdivided into the ventral skin-type (AQP6vs; AQPa2S), whose expression is confined to the ventral skin, and the urinary bladder-type (AQP6ub; AQPa2U), which is basically expressed in the urinary bladder.
Meniere's disease: histopathology, cytochemistry, and imaging.
Ishiyama et al., Los Angeles, United States. In Ann N Y Acad Sci, Apr 2015
Cytochemical alterations are significant for altered AQP4 and AQP6 expression in the supporting cell, and altered cochlin and mitochondrial protein expression.
Evidence of Positive Selection of Aquaporins Genes from Pontoporia blainvillei during the Evolutionary Process of Cetaceans.
Lima et al., Itajaí, Brazil. In Plos One, 2014
Considering that aquaporin genes were potentially subject to strong selective pressure, the aim of this study was to analyze the molecular evolution of seven aquaporin genes (AQP1, AQP2, AQP3, AQP4, AQP6, AQP7, and AQP9) comparing the lineages of cetaceans and terrestrial mammals.
Aquaporin 5 Interacts with Fluoride and Possibly Protects against Caries.
Vieira et al., Pittsburgh, United States. In Plos One, 2014
Aquaporins (AQP) are water channel proteins and the genes coding for AQP2, AQP5, and AQP6 are clustered in 12q13.
Expression of adrenergic and cholinergic receptors in murine renal intercalated cells.
Seki et al., Nishinomiya, Japan. In J Vet Med Sci, 2014
Further, b2 receptor-positive cells in the murine cortical collecting ducts also express AQP6, indicating that these cells are ICCs.
The role of renal water channels in health and disease.
Holmes, Winston-Salem, United States. In Mol Aspects Med, 2012
AQP6 and AQP11 are localized within the cell, with AQP6 involved in anion transport and AQP11 water transport.
Cell culture models and animal models for studying the patho-physiological role of renal aquaporins.
Valenti et al., Bari, Italy. In Cell Mol Life Sci, 2012
To date, eight aquaporins have been characterized and localized along the nephron, namely, AQP1 located in the proximal tubule, thin descending limb of Henle, and vasa recta; AQP2, AQP3 and AQP4 in collecting duct principal cells; AQP5 in intercalated cell type B; AQP6 in intercalated cells type A in the papilla; AQP7, AQP8 and AQP11 in the proximal tubule.
Immunohistochemical localization and mRNA expression of aquaporins in the macula utriculi of patients with Meniere's disease and acoustic neuroma.
Ishiyama et al., Los Angeles, United States. In Cell Tissue Res, 2010
Expression of AQP1, AQP4, or AQP6 mRNA did not differ in vestibular endorgans from patients with Meniere's disease.
Gene expression profiling of chromophobe renal cell carcinomas and renal oncocytomas by Affymetrix GeneChip using pooled and individual tumours.
Kovacs et al., Heidelberg, Germany. In Int J Biol Sci, 2008
Data have identified AQP6 s valuable markers for renal oncocytomas.
pH regulated anion permeability of aquaporin-6.
Yasui, Tokyo, Japan. In Handb Exp Pharmacol, 2008
AQP7, AQP8, and AQP11 are also present in the proximal tubules (Nielsen et al. 1998).A rat cDNA clone encoding AQP6 was isolated by PCR-based homologous cloning from a rat kidney cDNA library (Ma et al. 1993; Yasui et al. 1999).
Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63.
Yasui et al., Baltimore, United States. In J Biol Chem, 2002
the primary role of AQP6 may be in cellular regulation
Aquaporins in the kidney: from molecules to medicine.
Knepper et al., Århus, Denmark. In Physiol Rev, 2002
AQP6 is present in intracellular vesicles in collecting duct intercalated cells, and AQP8 is present intracellularly at low abundance in proximal tubules and collecting duct principal cells, but the physiological function of these two channels remains undefined.
Rapid gating and anion permeability of an intracellular aquaporin.
Agre et al., Baltimore, United States. In Nature, 1999
Although mammalian aquaporins were believed to be located in plasma membranes, rat AQP6 is restricted to intracellular vesicles in renal epithelia.
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