ACTION OF SPHINGOMYELINASE-C AND OTHER LIPID-SPECIFIC AGENTS AS INHIBITORS OF FC BINDING AND LOCOMOTION IN HUMAN LEUKOCYTES

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  • 1 January 1977
    • journal article
    • research article
    • Vol. 33  (3) , 407-412
Abstract
The binding of antibody-coated chicken erythrocytes (EA) to human blood lymphocytes and monocytes is inhibited by pretreatment of the leukocytes with sphingomyelinase C. Inhibition of rosetting of neuraminidase-treated EA with neutrophils is also seen with this enzyme. The cholesterol-binding .theta.-toxin of Clostridium perfringens and pronase also inhibit EA-rosette formation, but less strongly than sphingomyelinase. The lipid-specific agents also inhibit chemotactic migration of leukocytes to casein and denatured HSA [human serum albumin], whereas proteases and glycosidases do not. Membrane lipids are apparently important constituents of the binding sites for Fc fragments and for certain chemotactic factors. Sphingomyelin probably has an important role in this binding.