Lysolecithin induced membrane alterations in thymocytes. Effects of lysophosphatides possessing adjuvant and immuno-suppressive activities on cell agglutination by concanavalin A.

The effects of lysolecithin and of 2 synthetic ether-desoxy lysolecithin analogs, containing alkyl residues of 16 or 12 carbon atoms, on the agglutination kinetics of calf and rabbit thymocytes by concanavalin A (Con A) were investigated. Unlike the natural lysolecithin, these synthetic analogs are resistant to metabolism by membrane associated enzymes. It was found that pretreatment of thymocytes with lysolecithin or with the C16-analog leads to slightly increased agglutination rates. The C12-analog, in contrast, significantly inhibits thymocyte agglutination by Con A. Moreover, a comparison of these results with lysophosphatide effects on the agglutinability of erythrocytes of various species revealed that the inhibitory effect of the short-chain phosphatide is rather specific for thymocytes. The finding that long- and short-chain lysophosphatides, which have previously been shown to react as adjuvants or immunosuppressants, respectively, induce adserve alterations in thymocyte membranes indicates that these substances may affect the immune response by changing the membrane properties of immune competent cells. Concerning the nature of these membrane alterations it was shown that lysolecithin did not affect the number of Con A receptors per cell nor the affinity of lectin binding. It is therefore concluded that the lysophosphatide induced alterations of Con A agglutinability can not be caused by an uncovering or covering of lectin-receptors.