Role of membrane integral proteins in the modulation of red cell shape by albumin, dinitrophenol and the glass effect.
Defatted serum albumin is found to induce a cup shape in erythrocytes. At 40 mg/ml of albumin, approx. 80% of washed erythrocytes possess this morphology, which can be reversed to disc shape by dinitrophenol. Erythrocytes treated with trypsin, papain, pronase or neuraminidase show enhanced susceptibility to cup formation by albumin; however, chymotrypsinized erythrocytes exhibit a normal response. Red cells treated with concanavalin A (but not its succinylated derivative) show resistance to the cupping effect of albumin as well as the crenating effects of dinitrophenol and glass. The resistance develops after about 20 min following the exposure of cells to the lectin, and is rapidly abrogated on removal of the bound lectin by alpha-methylmannoside. Incubation of the concanavalin A-exposed cells at low temperature leads to prolongation of the time required to achieve the resistance. These results indicate an involvement of membrane integral proteins in mediating the shape modulating effects of albumin, dinitrophenol and exposure to glass.
D019297:2,4-Dinitrophenol; D003208:Concanavalin A / Q000494:pharmacology; D004140:Dinitrophenols / Q000494:pharmacology*; D004912:Erythrocytes / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000097:blood*; D009439:Neuraminidase / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000494:pharmacology; D012709:Serum Albumin / Q000494:pharmacology*
D004140:Dinitrophenols; D008565:Membrane Proteins; D012709:Serum Albumin; D003208:Concanavalin A; D009439:Neuraminidase; D010447:Peptide Hydrolases; D019297:2,4-Dinitrophenol