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Aquaporin 10

AQP10, aquaporin 10
This gene encodes a member of the aquaglyceroporin family of integral membrane proteins. Members of this family function as water-permeable channels in the epithelia of organs that absorb and excrete water. This protein was shown to function as a water-selective channel, and could also permeate neutral solutes such as glycerol and urea. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Aquaporin 1, AQP9, AQP5, CD36, AQP8
Papers on AQP10
Effects of estrogen deprivation on expression of aquaporins in rat vagina.
Lin et al., China. 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.
The key role of aquaporin 3 and aquaporin 10 in the pathogenesis of pompholyx.
McCormick et al., United States. In Med Hypotheses, May 2015
The mechanistic explanation for the epidermal fissuring might lie in the over-expression across the mid and upper epidermis, including the stratum corneum, of two water/glycerol channel proteins aquaporin 3 and aquaporin 10, expressed in the keratinocytes of afflicted pompholyx patients.
Aquaglyceroporins: implications in adipose biology and obesity.
Soveral et al., Lisbon, Portugal. In Cell Mol Life Sci, Feb 2015
Recently, AQP3, AQP9, AQP10 and AQP11 were additionally identified in human adipocytes and proposed as additional glycerol pathways in these cells.
Aquaporins Mediate Silicon Transport in Humans.
Isenring et al., Québec, Canada. In Plos One, 2014
Here, we show for the first time that the human aquaglyceroporins, i.e., AQP3, AQP7, AQP9 and AQP10 can act as silicon transporters in both Xenopus laevis oocytes and HEK-293 cells.
Role of aquaglyceroporins and caveolins in energy and metabolic homeostasis.
Frühbeck et al., Pamplona, Spain. In Mol Cell Endocrinol, 2014
Aquaglyceroporins (AQP3, AQP7, AQP9 and AQP10) encompass a subfamily of aquaporins that allow the movement of water, but also of small solutes, such as glycerol, across cell membranes.
Functional characteristics of aquaporin 7 as a facilitative glycerol carrier.
Yuasa et al., Nagoya, Japan. In Drug Metab Pharmacokinet, 2013
However, our recent studies have indicated that AQP9 and AQP10 operate in a carrier mode, which is of saturable nature, for glycerol transport.
In vivo studies of aquaporins 3 and 10 in human stratum corneum.
Hélix-Nielsen et al., Copenhagen, Denmark. In Arch Dermatol Res, 2013
AQP3 and AQP10 are aqua-glyceroporins, known to transport glycerol as well as water.
Aquaporins 6-12 in the human eye.
Heegaard et al., Copenhagen, Denmark. In Acta Ophthalmol, 2013
No mRNA of AQP6, AQP8, AQP10 or AQP12 was detected.
Expression of aquaporin water channels in equine endometrium is differentially regulated during the oestrous cycle and early pregnancy.
Rutllant et al., Lexington, United States. In Reprod Domest Anim, 2013
Quantitative PCR revealed a time-dependent pattern for all aquaporin subtypes examined except for AQP10 and 12. AQP3, 5 and 7 showed highest mRNA abundance 8 days after ovulation, while AQP0 and 2 were most abundant at Day 14 of the cycle in non-pregnant mares.
Aquaporin expression and function in human pluripotent stem cell-derived retinal pigmented epithelial cells.
Skottman et al., Tampere, Finland. In Invest Ophthalmol Vis Sci, 2013
RESULTS: AQP1, AQP3, AQP4, AQP5, AQP6, AQP7, AQP10, AQP11, and AQP12 were expressed in hESC- and hiPSC-derived RPE cells.
In vitro study of transporters involved in intestinal absorption of inorganic arsenic.
Devesa et al., Paterna, Spain. In Chem Res Toxicol, 2012
RT-qPCR indicates up-regulation of GLUT2, GLUT5, OATPB, AQP3, and AQP10 after exposure to As(III), while exposure to As(V) increases the expression of sodium-dependent phosphate transporters, especially NaPiIIb.
Glycosylation increases the thermostability of human aquaporin 10 protein.
Hedfalk et al., Göteborg, Sweden. In J Biol Chem, 2011
the presence of at least one glycosylated protein within each tetramer is sufficient to convey an enhanced structural stability to the remaining hAQP10 protomers of the tetramer.
Dual functional characteristic of human aquaporin 10 for solute transport.
Yuasa et al., Nagoya, Japan. In Cell Physiol Biochem, 2010
study unveiled the uniquely dual functional characteristic of hAQP10 as a carrier/channel for solute transport, providing a novel insight into its operation mechanism, which would help further elucidate its physiological role
Molecular diversity of vasotocin-dependent aquaporins closely associated with water adaptation strategy in anuran amphibians.
Tanaka et al., Shizuoka, Japan. In J Neuroendocrinol, 2010
The anuran AQP family consists of at least AQP0-AQP5, AQP7-AQP10 and two anuran-specific types, designated as AQPa1 and AQPa2.
Molecular and cellular regulation of water homeostasis in anuran amphibians by aquaporins.
Tanaka et al., Shizuoka, Japan. In Comp Biochem Physiol A Mol Integr Physiol, 2009
Anuran AQP family consists of at least AQP0-AQP5, AQP7-AQP10, and two anuran-specific types, designated as AQPa1 and AQPa2.
Ammonia and urea permeability of mammalian aquaporins.
Zeuthen et al., Denmark. In Handb Exp Pharmacol, 2008
The human aquaporins,AQP3,AQP7, AQP8,AQP9, and possibly AQP10, are permeable to ammonia, and AQP7, AQP9, and possibly AQP3, are permeable to urea.
Compartmentalization of aquaporins in the human intestine.
Rajnarayanan et al., Jackson, United States. In Int J Environ Res Public Health, 2008
differential polarity and selective targeting of AQP3 and AQP10 in the intestinal epithelial cells is influenced by amino acid signal motifs.
Expression and localization of two isoforms of AQP10 in human small intestine.
Yamamoto et al., Niigata, Japan. In Biol Cell, 2005
AQP10 with an insertion of 475 nt was localized in the capillary endothelium in villi of the small intestine and the isoform without the insertion localized in the gastro-entero-pancrestic endocrine cells.
Cloning and identification of a new member of water channel (AQP10) as an aquaglyceroporin.
Imai et al., Tochigi, Japan. In Biochim Biophys Acta, 2002
Results suggest that AQP10 represents a new member of aquaglyceroporins functionally as well as structurally.
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