Abstract

Fibroblast cells (BHK-21, Swiss 3T3, SV403T3, L929) will form rosettes by binding to erythrocytes of specific types. The specificity of binding varies with the cell line. Monolayer cultures of spread baby hamster kidney (BHK) cells also bind erythrocytes with the same specificity exhibited by suspended cells. Our studies have concentrated on rosette formation between trypsinzed-ox (TOx) erythrocytes and BHK cells. Extensive protease treatment of the BHK cells reduces their ability to bind TOx erythrocytes in a dose- and time-dependent manner, suggesting the involvement of protein in the binding site. Simple saccharides, and glycopeptide isolated from ox erythrocyte ghosts, do not inhibit rosetting. However, neutral glycosphinogolipids from ox erythrocyte ghosts inhibit BHK-TOx rosetting, whereas neutral glycosphingolipids from non-rosetting rabbit erythrocytes have no effect on rosetting. Furthermore, incorporation of ox glycolipids into guinea-pig erythrocytes causes these non-rosetting erythrocytes to adhere to BHK cells. These experiments suggest that specific glycolipids of the ox erythrocyte act as receptors for binding sites on the cell surface of BHK cells. These cell-specific binding sites may play a role in cell-surface events involving carbohydrate recognition.

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