Role of membrane proteins in monosodium urate crystal-membrane interactions. II. Effect of pretreatments of erythrocyte membranes with membrane permeable and impermeable protein crosslinking agents.

Intact, human erythrocytes were pretreated with membrane permeable, dimethyl adipimidate (DMA) and dimethyl suberimidate (DMS) and membrane impermeable 3,3' dithiobis (sulfosuccinimidylpropionate) (DTSSP) protein crosslinking agents and incubated with monosodium urate monohydrate (MSUM) crystals. The percent inhibition of lysis values for pretreated cells relative to untreated cells were determined. All 3 agents caused a concentration dependent inhibition of MSUM induced hemolysis that was not due to a decrease in MSUM binding to the pretreated membranes. It was proposed that the inhibition of lysis was due to crosslinking of integral and cytoskeletal membrane proteins, resulting in a reduced mobility of the proteins, inhibition of lateralization of integral proteins into aggregates and decreased "pore" formation in the membrane.