Disease relevance of ECs4852

• Aquaglyceroporin GlpF selectively conducts water and linear polyalcohols, such as glycerol, across the inner membrane of Escherichia coli [1].
• We then used this system to analyse the effects of mutations in the pore constriction of Gla(Llac), the aquaglyceroporin from Lactococcus lactis [2].

High impact information on ECs4852

• Energetics of glycerol conduction through aquaglyceroporin GlpF [1].
• Freeze-fracture studies on oocyte plasma membranes gave a size of AQP3 particles in favor of a dimeric or trimeric structure [3].
• At first, based on transcript detection by reverse transcription-PCR from human erythroid tissues and membrane expression detected by flow cytometry analysis, we demonstrated that AQP3 is expressed on human and rat but not on mouse red blood cells [3].
• Here, we analyzed the oligomerization of the AQP3 aquaglyceroporin, which presents a mixed selectivity for water, glycerol, and urea [3].
• Finally, by cross-linking experiments with red blood cell membranes, AQP3 is visible as different oligomeric structures, including a tetrameric one [3].

Biological context of ECs4852

• The presence of AqpS in an arsenic resistance operon is interesting, since aquaglyceroporin channels have previously been shown to adventitiously facilitate uptake of arsenite into cells, rendering them sensitive to arsenite [4].

Anatomical context of ECs4852

• Functional characterization of the Escherichia coli glycerol facilitator, GlpF, in Xenopus oocytes [5].
• We conclude that there is an interaction between the glycerol facilitator protein and glycerol kinase that stimulates kinase activity, analogous to the hexokinase- and glycerol kinase-porin interactions in mitochondria [6].

Analytical, diagnostic and therapeutic context of ECs4852

• This anomaly was not due to refractive index differences or to the presence of residual levels of the glycerol facilitator protein in non-induced cells [7].

References