The transformation of human lymphocytes by monkey antisera to human immunoglobulins.

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  • 1 January 1969
    • journal article
    • Vol. 16  (1) , 123-38
Abstract
Cultures of human peripheral leucocytes were stimulated to incorporate tritiated thymidine when incubated with monkey antisera to human immunoglobulins. Twenty-five of forty-four monkey antisera were active and stimulated 90 per cent of leucocyte (WBC) cultures to incorporate a small but significantly greater amount of tritiated thymidine (TdR3H) than that incorporated by controls. This stimulation of TdR3H uptake correlated with an increase from 2 to 8 per cent lymphoblasts in the cultures. Leucocytes washed free of serum immunoglobulins responded to a greater degree to the anti-immunoglobulin sera than when they were cultured in the presence of human serum. Prior absorption of antisera with either whole serum or homologous immunoglobulin blocked antiserum stimulation completely. The anti-IgG and anti-IgM antisera were consistently more effective than anti-IgA, anti-κ and anti-λ chain antisera. Sequential stimulation by antisera against two different immunoglobulins was not significantly different from those stimulated by only one of the two. Lymphocytes from three asymptomatic subjects with low or absent serum IgA levels transformed as well with anti-IgA as did lymphocytes from subjects with normal serum IgA levels. Antisera were cytotoxic to the lymphocytes only in the presence of complement. Presumably the transformation of human lymphocytes was due to a reaction of anti-immunoglobulin antisera with specific immunoglobulin antigenic determinants present on or in the circulating lymphocytes.