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Inhibition of acyl transferase ec in lymphocytes by concanavalin a

, : Inhibition of acyl transferase ec in lymphocytes by concanavalin a. Biochimica et Biophysica Acta 629(2): 305-316

The effects of concanavalin [Con] A and succinylated Con A on the transformation of mouse splenic lymphocytes and on early biochemical events in the transformation were compared. Lymphocyte transformation was biphasic with respect to Con A concentration, with optimal activation at .apprx. 1 .mu.g/ml. Activation by succinyl Con A was not biphasic over a range of lectin concentration of 1-16 .mu.g/ml. In intact lymphocytes cultured for 4 h, the enzyme Acyl-CoA:1-acylglycero-3-phosphocholine O-acyltransferase (EC was not activated by Con A but was inhibited at all concentrations tested and was .apprx. 60% inhibited at 16 .mu.g Con A/ml. Succinyl Con A gave little or no inhibition at similar concentrations. Lymphocytes became committed to divide while their acyltransferase activities were markedly inhibited by Con A. The inhibition of acyltransferase by Con A was lifted by displacing the lectin from the cells by .alpha.-methylmannoside. Lowered enzyme activity was not caused by cell agglutination or by direct cross-linking of lectin receptors. Inhibition of acyltransferase was probably not due to indirect cross-linking via the cytoskeleton since colchicine did not reverse the inhibition. The inhibition of acyltransferase and the reduced stimulation of transformation by higher levels of Con A may be due to hydrophobic interaction of the lectin with the plasma membrane as shown by liposome aggregation studies.


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