Possible mechanism of uptake for several compounds in ionized form through human erythrocyte membrane.
The mechanism underlying uptake of certain compounds in ionized form across human red blood cell membrane was examined. The ionized forms of salicylate, 5-methoxy-salicylate and phenylalanylphenylalanine were significantly taken up into the interior space of human red blood cells instead of remaining in the membrane. Inhibition of the uptake of these compounds by 4,4'-diisothiocyano-2,2'-disulfonate stilbene and phlorizin indicates that their permeation of the erythrocyte membrane may involve the membrane protein fraction. Chelation at the protein site does not appear to occur. Instead, an amino group in the protein structure may mediate the transport of these ionized compounds.
D000042:Absorption; D001692:Biological Transport / Q000187:drug effects; D004151:Dipeptides / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism*; D006461:Hemolysis; D006801:Humans; D062425:Hydroxybenzoate Ethers; D062385:Hydroxybenzoates / Q000378:metabolism; D066298:In Vitro Techniques; D007477:Ions / Q000378:metabolism*; D009994:Osmolar Concentration; D012459:Salicylates / Q000378:metabolism; D020156:Salicylic Acid
D004151:Dipeptides; D062425:Hydroxybenzoate Ethers; D062385:Hydroxybenzoates; D007477:Ions; D012459:Salicylates; C026650:phenylalanylphenylalanine; C033304:5-methoxysalicylic acid; D020156:Salicylic Acid