Aquaglyceroporin

Aquaglyceroporins are a subfamily of membrane channel proteins within the Membrane Intrinsic Proteins (MIP) superfamily that conduct water, glycerol, and a range of small, uncharged solutes across biological membranes. Unlike "orthodox" aquaporins, which are strictly selective for water, aquaglyceroporins (including human AQP3, AQP7, AQP9, and AQP10) possess wider and more hydrophobic pores allowing facilitated diffusion of glycerol, urea, arsenic compounds, and other small molecules alongside water[2][4][5][8]. These proteins assemble as homotetramers, with each monomer forming its own pore. Aquaglyceroporins are broadly expressed, most notably in adipose tissue, liver, kidney, testis, and in some pathogens. They are essential for glycerol metabolism, energy homeostasis, and have pathophysiological roles in metabolic diseases (such as obesity and diabetes), cancer, and arsenic toxicity. They are regarded as potential drug targets for the modulation of metabolic processes and as uptake routes for therapeutic agents in infectious organisms. No approved drugs directly target aquaglyceroporins in humans, but pharmacological modulators are under investigation[2][5][8].

Other names

Aquaglyceroporin channelAquaglyceroporin familyGlycerol facilitator (GlpF in bacteria)AQP3AQP7AQP9AQP10 (human paralogs)

Channel inhibition (block of glycerol or water permeability); Substrate analog competition; Exploitation as uptake route for cytotoxic agents or antimicrobials (in some pathogens)