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

Aquaporin 9

AQP9, AQP7, aquaporin 9, SSCI, aquaporin 7
The aquaporins are a family of water-selective membrane channels. The protein encoded by this gene allows passage of a wide variety of noncharged solutes. It stimulates urea transport and osmotic water permeability; there are contradicting reports about its role in providing glycerol permeability. The encoded protein may also play a role in specialized leukocyte functions such as immunological response and bactericidal activity. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Aquaporin 1, AQP4, AQP8, CAN, AQP5
Papers on AQP9
A systematic review of biomarkers in the diagnosis of infective endocarditis.
Review
New
Honoré et al., Århus, Denmark. In Int J Cardiol, Feb 2016
Based on current research, N-terminal-pro-B-type natriuretic peptide (NT-proBNP) alone or in combination with Cystatin C (Cys C), lipopolysaccharide-binding protein (LBP), troponins, aquaporin-9 (AQP9), S100 calcium binding protein A11 (S100A11), E-selectin (CD62E) and VCAM-1 (CD54) and interleukin-6 (IL-6) are potential biomarkers for future studies.
Placental programmed cell death: insights into the role of aquaporins.
New
Damiano et al., Buenos Aires, Argentina. In Mol Hum Reprod, Jan 2016
However, TEA and phloretin treatments, to block AQP1/4 or AQP9, respectively, failed in abrogate apoptosis.
The relationship between aquaglyceroporin expression and development of fatty liver in diet-induced obesity and ob/ob mice.
New
Shioda et al., Saitama, Japan. In Obes Res Clin Pract, Jan 2016
We examined the effect of AQP7, AQP9, and lipid metabolism-related gene expression in obese mice.
Hyperosmotic stress induces cisplatin sensitivity in ovarian cancer cells by stimulating aquaporin-5 expression.
New
Zheng et al., Hangzhou, China. In Exp Ther Med, Dec 2015
3AO cell proliferation was inhibited by hyperosmotic stress, while the expression of AQP5, but not that of AQP1, AQP3 or AQP9, was increased in a dose- and time-dependent manner in hypertonic sorbitol-containing medium.
Stress alters the expression of aquaporins in cultured rat intestinal epithelial cells.
New
Huang et al., Taipei, Taiwan. In Exp Ther Med, Nov 2015
AQP9 and glycosylated AQP11 proteins were also markedly upregulated.
Bariatric surgery acutely changes the expression of inflammatory and lipogenic genes in obese adipose tissue.
New
Fernández-Real et al., Girona, Spain. In Surg Obes Relat Dis, Sep 2015
and aquaporin 9 (P<.0001) in SAT; and PPARγ (P = .018)
IL-7-Induced Glycerol Transport and TAG Synthesis Promotes Memory CD8+ T Cell Longevity.
New
Impact
Kaech et al., New Haven, United States. In Cell, Jun 2015
We discover that IL-7 induces expression of the glycerol channel aquaporin 9 (AQP9) in virus-specific memory CD8+ T cells, but not naive cells, and that AQP9 is vitally required for their long-term survival.
Aquaglyceroporins: implications in adipose biology and obesity.
Review
New
Soveral et al., Lisbon, Portugal. In Cell Mol Life Sci, Feb 2015
For a long time, AQP7 has been the only aquaglyceroporin associated with the adipose tissue, which is the major source of circulating glycerol in response to the energy demand.
Sexual Dimorphism of Adipose and Hepatic Aquaglyceroporins in Health and Metabolic Disorders.
Review
Calamita et al., Pamplona, Spain. In Front Endocrinol (lausanne), 2014
Plasma glycerol concentrations are increased in women compared to men probably due to the higher lipolytic rate and larger AQP7 amounts in visceral fat as well as the well-known sexual dimorphism in fat mass with women showing higher adiposity.
Aquaporin7 plays a crucial role in tolerance to hyperosmotic stress and in the survival of oocytes during cryopreservation.
Huang et al., Shanghai, China. In Sci Rep, 2014
Here, we demonstrated that hyperosmosis produced by high concentrations of cryoprotectants, including DMSO, ethylene glycol and sucrose, significantly upregulated the protein levels of aquaporin (AQP) 7, but not AQP3 and AQP9, in mouse oocytes.
Role of aquaglyceroporins and caveolins in energy and metabolic homeostasis.
Review
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.
Novel molecular aspects of ghrelin and leptin in the control of adipobiology and the cardiovascular system.
Review
Rodríguez, Pamplona, Spain. In Obes Facts, 2013
In this sense, leptin modulates via PI3K/Akt/mTOR the expression of aquaglyceroporins such as AQP3 and AQP7 that facilitate glycerol efflux from adipocytes in response to the lipolytic stimuli via its translocation from the cytosolic fraction (AQP3) or lipid droplets (AQP7) to the plasma membrane.
AQP9: a novel target for bone loss induced by microgravity.
GeneRIF
Hou et al., Beijing, China. In Biochem Biophys Res Commun, 2012
AQP9 plays an important role in the development of microgravity-induced bone loss, and may be a potential target for the prevention or management of microgravity-induced bone loss.
Estrogen prevents increased hepatic aquaporin-9 expression and glycerol uptake during starvation.
GeneRIF
Praetorius et al., Århus, Denmark. In Am J Physiol Gastrointest Liver Physiol, 2012
The sexual dimorphism in hepatic AQP9 regulation may be ascribed to estradiol-17 beta suppressing the expression of hepatic AQP9.
Aqp 9 and brain tumour stem cells.
GeneRIF
Murrell et al., Oslo, Norway. In Scientificworldjournal, 2011
Aquaporin 9 is linked to the tumorigenesis of glioblastoma.
The gene expression analysis of blood reveals S100A11 and AQP9 as potential biomarkers of infective endocarditis.
GeneRIF
Mege et al., Marseille, France. In Plos One, 2011
Using transcriptional signatures of blood samples,identified S100A11 as a potential diagnostic marker of infective endocarditis, and AQP9 as a potential prognostic factor.
A new role for aquaporin 7 in insulin secretion.
GeneRIF
Sener et al., Brussels, Belgium. In Cell Physiol Biochem, 2011
AQP7 may, directly or indirectly, play a role at a distal site in the exocytotic pathway.
Aquaporins in the kidney: from molecules to medicine.
Review
Impact
Knepper et al., Århus, Denmark. In Physiol Rev, 2002
AQP7 is abundant in the brush border of proximal tubule cells and is likely to be involved in proximal tubule water reabsorption.
Structural basis of water-specific transport through the AQP1 water channel.
Impact
Jap et al., Berkeley, United States. In Nature, 2002
In mammals, there are currently 10 families of water channels, referred to as aquaporins (AQP): AQP0-AQP9.
Cellular and molecular biology of the aquaporin water channels.
Review
Impact
Agre et al., Baltimore, United States. In Annu Rev Biochem, 1998
Multifunctional aquaglyceroporins AQP3, AQP7, and AQP9 are permeated by water, glycerol, and some other solutes.
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