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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Aquaporin 8

AQP8, aquaporin-8
plays a role in water transport across hepatocyte membranes [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: Aquaporin 1, AQP9, AQP4, AQP5, POLYMERASE
Papers on AQP8
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.
Aquaporin - 1 and 8 expression in the gallbladder mucosa might not be associated with the development of gallbladder stones in humans.
Störkel et al., Wuppertal, Germany. In Eur J Clin Invest, Jan 2016
This study investigated the expression of Aquaporin - 1 (AQP1) and Aquaporin - 8 (AQP8) in the human gallbladder mucosa and their possible association with the formation of gallbladder stones.
Aquaporin8 regulates cellular development and reactive oxygen species production, a critical component of virulence in Botrytis cinerea.
Tian et al., Beijing, China. In New Phytol, Dec 2015
The role of AQP8 in reactive oxygen species (ROS) production, distribution and transport were further determined.
Stress alters the expression of aquaporins in cultured rat intestinal epithelial cells.
Huang et al., Taipei, Taiwan. In Exp Ther Med, Nov 2015
The mRNA expression levels of all the tested AQPs were not altered by ischemia alone or by ischemia/reperfusion; however, AQP8 protein was markedly reduced by ischemic injury.
The effects of over expressing aquaporins on the cryopreservation of hepatocytes.
Lee et al., Charlotte, United States. In Cryobiology, Oct 2015
Hepatocytes express aquaporin (AQP) 0, 8, 9, 11, and 12; this study investigates whether increasing the localization of AQP8 on the cellular membrane would improve cell viability by increasing water transport during cryopreservation.
Changes in aquaporin 5 in the non-ciliated cells of mouse oviduct according to sexual maturation and oestrous cycle.
Gye et al., In Reprod Fertil Dev, Sep 2015
In the oviduct of cycling females, aqp1, aqp3, aqp4, aqp5, aqp6, aqp7, aqp8, and aqp11 mRNA were detected.
Acidosis-induced downregulation of hepatocyte mitochondrial aquaporin-8 and ureagenesis from ammonia.
Marinelli et al., Rosario, Argentina. In Biochem Cell Biol, Aug 2015
Since we previously demonstrated that hepatocyte mitochondrial aquaporin-8 channels (mtAQP8) facilitate the uptake of ammonia and its metabolism into urea, we studied whether mtAQP8 is involved in the liver adaptive response to acidosis.
Ethyl pyruvate reduces hepatic mitochondrial swelling and dysfunction in a rat model of sepsis.
Chen et al., Guangzhou, China. In Int J Clin Exp Pathol, 2014
Ethyl pyruvate (EP) is a cytoprotective agent, while aquaporin-8 (AQP8) is a mitochondrial water channel that can induce mitochondrial swelling.
Identification of genes in ulcerative colitis associated colorectal cancer based on centrality analysis of co-expression network.
Ji et al., In Neoplasma, 2014
We found 21 common genes, such as SLC4A4 and AQP8, both existed in CRC and UC top 200 genes.
Are the basal cells of the mammalian epididymis still an enigma?
Arrighi, Milano, Italy. In Reprod Fertil Dev, 2014
Members of the aquaporin (AQP) and/or aquaglyceroporin family (AQP3, AQP7 and AQP8) are also specifically expressed in the rat epididymal basal cells.
Aquaporins in avian kidneys: function and perspectives.
Yang et al., Memphis, United States. In Am J Physiol Regul Integr Comp Physiol, 2013
Also, gene and/or amino acid sequences of AQP5, AQP7, AQP8, AQP9, AQP11, and AQP12 have been reported in birds.
Brain water channel proteins in health and disease.
Huber et al., Cluj-Napoca / Kolozsvár, Romania. In Mol Aspects Med, 2012
Then the localization and functional roles of WCPs found in the brain are described: AQP1, AQP2, AQP3, AQP4, AQP5, AQP7, AQP8, AQP9 and AQP11.
Mitochondrial aquaporin-8 in renal proximal tubule cells: evidence for a role in the response to metabolic acidosis.
Marinelli et al., Rosario, Argentina. In Am J Physiol Renal Physiol, 2012
AQP8 plays an important role in the adaptive response of proximal tubule to acidosis possibly facilitating mitochondrial ammonia 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.
Reconstitution of water channel function and 2D-crystallization of human aquaporin 8.
Kjellbom et al., Lund, Sweden. In Biochim Biophys Acta, 2012
Reconstitution of water channel function and 2D-crystallization of human aquaporin 8.
Early compensatory adaptations in maternal undernourished pregnancies in rats: role of the aquaporins.
Ross et al., Torrance, United States. In J Matern Fetal Neonatal Med, 2011
increased in placental labyrinth zone in maternal undernutrition
Differential proteomic shotgun analysis elucidates involvement of water channel aquaporin 8 in presence of α-amylase in the colon.
Yamamoto et al., Niigata, Japan. In J Proteome Res, 2011
Studies confirmed the involvement of AQP8 in alpha-amylase 2 regulation.
Hepatocyte aquaporins in bile formation and cholestasis.
Marchissio et al., Rosario, Argentina. In Front Biosci, 2010
Aquaporin-8 (AQP8), localized to canalicular membranes, modulates membrane water permeability providing a molecular mechanism for the osmotically-coupled transport of solute and water during bile formation.
Increased female fertility in aquaporin 8-deficient mice.
Ma et al., Changchun, China. In Iubmb Life, 2010
we conclude that AQP8 deficiency increases the number of mature follicles by reducing the apoptosis of granulosa cells, thus increasing the fertility of female mice[aquaporin 8]
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.
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