The Important Role of Aquaglyceroporin 7 in Health and Disease [PDF]
Aquaporins (AQPs) are highly conserved small transmembrane proteins that facilitate the transport of water and small solutes across cell membranes. Aquaglyceroporin 7 (AQP7), a significant member of the AQP family, is widely distributed throughout the ...
Jing Liu +7 more
doaj +4 more sources
Implications of Aquaglyceroporin 7 in Energy Metabolism [PDF]
The aquaglyceroporin AQP7 is a pore-forming transmembrane protein that facilitates the transport of glycerol across cell membranes. Glycerol is utilized both in carbohydrate and lipid metabolism. It is primarily stored in white adipose tissue as part of the triglyceride molecules.
Lebeck, Janne; id_orcid 0000-0003-1716-0417 +1 more
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The yeast aquaglyceroporin Fps1p is a bidirectional arsenite channel [PDF]
The stress‐activated kinase Hog1p mediates arsenic tolerance by decreasing arsenite influx through the aquaglyceroporin Fps1p in Saccharomyces cerevisiae. Unexpectedly, we found that overexpression of FPS1 increased arsenite tolerance suggesting a physiological role of Fps1p in arsenic detoxification.
Maciaszczyk-Dziubinska, Ewa +4 more
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Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF [PDF]
The structure and composition of a biological membrane can severely influence the activity of membrane-embedded proteins. Here, we show that the E. coli aquaglyceroporin GlpF has only little activity in lipid bilayers formed from native E. coli lipids. Thus, at first glance, GlpF appears to not be optimized for its natural membrane environment. In fact,
Klein, Noreen +2 more
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Targeted deletion of the aquaglyceroporin AQP9 is protective in a mouse model of Parkinson's disease. [PDF]
More than 90% of the cases of Parkinson's disease have unknown etiology. Gradual loss of dopaminergic neurons of substantia nigra is the main cause of morbidity in this disease. External factors such as environmental toxins are believed to play a role in
Katja Stahl +12 more
doaj +4 more sources
Acyrthosiphon pisum AQP2: A multifunctional insect aquaglyceroporin [PDF]
Annotation of the recently sequenced genome of the pea aphid (Acyrthosiphon pisum) identified a gene ApAQP2 (ACYPI009194, Gene ID: 100168499) with homology to the Major Intrinsic Protein/aquaporin superfamily of membrane channel proteins. Phylogenetic analysis suggests that ApAQP2 is a member of an insect-specific clade of this superfamily.
Wallace, Ian S. +6 more
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Regulatory mechanisms of Leishmania Aquaglyceroporin AQP1 [PDF]
Pentavalent antimonials [Sb(V)] are the primary drug of choice against all forms of leishmaniasis. Emergence of antimony unresponsiveness is a major issue. There is a dire need of understanding antimony resistance mechanisms in Leishmania.
Sharma, Mansi
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Functional characterization of a microbial aquaglyceroporin [PDF]
The major intrinsic proteins (MIPs) constitute a widespread membrane channel family essential for osmotic cell equilibrium. The MIPs can be classified into three functional subgroups: aquaporins, glycerol facilitators and aquaglyceroporins. Bacterial MIP genes have been identified in archaea as well as in Gram-positive and Gram-negative eubacteria ...
Alexandrine, Froger +9 more
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Role of Aquaglyceroporin (AQP1) Gene and Drug Uptake in Antimony-resistant Clinical Isolates of Leishmania donovani [PDF]
Antimonial-containing drugs are the first line of treatment against Leishmaniasis. Resistance to antimonials in Leishmania is proposed to be due to reduced uptake of trivalent antimony (SbIII) through the aquaglyceroporin (AQP1).
Singh, Sushma +3 more
core +6 more sources
Aquaglyceroporins: ancient channels for metalloids [PDF]
The identification of aquaglyceroporins as uptake channels for arsenic and antimony shows how these toxic elements can enter the food chain, and suggests that food plants could be genetically modified to exclude arsenic while still accumulating boron and silicon.
Bhattacharjee, Hiranmoy +3 more
openaire +2 more sources

