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Adaptive Selection in the Evolution of Aquaglyceroporins in Mammals
Journal of Molecular Evolution, 2023Aquaporins (AQPs) are integral membrane proteins responsible for water transport across cellular membranes in both prokaryotes and eukaryotes. A subfamily of AQPs, known as aquaglyceroporins (AQGPs), facilitate the transport of small solutes such as glycerol, water, and other solutes across cellular membranes.
Shiveeli Rajput +7 more
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Interaction of Individual Ions, Ion-Water Clusters with Aquaglyceroporin and Aquaporin-1 Channels [PDF]
Journal of Computational and Theoretical Nanoscience, 2015 Aquaglyceroporin and aquaporin-1 channels provide a mechanism for the transport of water and ions through cell membranes. The present paper proposes a precise geometric structure of these channels to explain their mechanism as selective channels.
Ngamta Thamwattana +2 more
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A Current View of the Mammalian Aquaglyceroporins
Annual Review of Physiology, 2008The discovery of aquaporin water channels by Agre and coworkers answered a long-standing biophysical question of how the majority of water crosses biological membranes. The identification and study of aquaporins have provided insight, at the molecular level, into the fundamental physiology of water balance regulation and the pathophysiology of water ...
Aleksandra, Rojek +4 more
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Aquaglyceroporins: implications in adipose biology and obesity
Cellular and Molecular Life Sciences, 2014Aquaporins (AQPs) are membrane water/glycerol channels that are involved in many physiological processes. Their primary function is to facilitate the bidirectional transfer of water and small solutes across biological membranes in response to osmotic gradients.
Ana, Madeira +2 more
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Aquaglyceroporin 9 in brain pathologies
Neuroscience, 2010Aquaglyceroporins belong to the aquaporin family and are permeable to water and also to small solutes such as glycerol and urea. In this review, we will compare the expression of aquaporin 9 (AQP9), an aquaglyceroporin, with that of AQP4, a pure water channel, in pathological conditions.
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Flow cytometry-assisted rapid isolation of recombinant Plasmodium berghei parasites exemplified by functional analysis of aquaglyceroporin [PDF]
International Journal for Parasitology, 2012 The most critical bottleneck in the generation of recombinant Plasmodium berghei parasites is the mandatory in vivo cloning step following successful genetic manipulation. This study describes a new technique for rapid selection of recombinant P. berghei
Kai Matuschewski +2 more
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Role of aquaglyceroporins and caveolins in energy and metabolic homeostasis
Molecular and Cellular Endocrinology, 2014Aquaglyceroporins and caveolins are submicroscopic integral membrane proteins that are particularly abundant in many mammalian cells. 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.
Leire, Méndez-Giménez +3 more
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Identification of residues controlling transport through the yeast aquaglyceroporin Fps1 using a genetic screen [PDF]
FEBS Journal, 2004 Aquaporins and aquaglyceroporins mediate the transport of water and solutes across biological membranes. Saccharomyces cerevisiae Fps1 is an aquaglyceroporin that mediates controlled glycerol export during osmoregulation.
Markus Tamás +2 more
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Pancreatic beta-cells: Role of glycerol and aquaglyceroporin 7 [PDF]
International Journal of Biochemistry and Cell Biology, 2011 Pancreatic β-cells originate from gut endoderm during development. Pancreatic endocrine cells represent about 10% of the mature pancreatic cells, and β-cells represent the majority of endocrine cells. β-cells secrete insulin in response to elevation of nutrient concentrations.
Jason Perret, Christine Delporte
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Arsenic trioxide uptake by human and rat aquaglyceroporins
Biochemical and Biophysical Research Communications, 2004Aquaglyceroporins are channels that allow downhill movement of uncharged solutes such as glycerol and urea. Arsenic trioxide has recently been shown to be translocated by mouse mAQP7 and rat rAQP9. In this study we examined the ability of the four known human members of the aquaglyceroporin family, hAQP3, hAQP7, hAQP9, and hAQP10, to facilitate As(OH ...
Zijuan, Liu +3 more
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