concanavalin-a and Waldenstrom-Macroglobulinemia

An alkylated monomer of Concanavalin A was prepared photochemically according to the method of Tanaka et al. (1981). Its affinities for methyl-alpha-D-gluco, methyl-alpha-D-manno and p-nitrophenyl-alpha-D-manno pyranoside were calculated. The enthalpies of these binding reactions were measured calorimetrically and the thermodynamic parameters were calculated. The values obtained suggest that the structure of the monomer differs from that of the dimeric and tetrameric molecules. Calorimetric studies also showed that the monomeric derivative reacts with IgM but not IgG. The enthalpy per binding site in the monomer-IgM reaction is equal to that of the monomer-mannose derivative reaction; mannose is the terminal residue of the saccharide chains of the IgM molecule. The stoichiometry of the reaction is ten ConA-m per IgM molecule.

Topics: Amino Acids; Calorimetry; Carbohydrates; Chemical Phenomena; Chemistry; Concanavalin A; gamma-Globulins; Humans; Immunoglobulin G; Immunoglobulin M; Kinetics; Thermodynamics; Waldenstrom Macroglobulinemia

In vitro lymphocyte functions in a patient with Waldenström's macroglobulinemia and his kindred were examined. The percentage and number of total peripheral blood T cells and the absolute number of FC gamma bearing T cells were decreased in the patient and family members compared to controls but the B cells and monocytes were normal. In addition, PHA and PWM stimulated proliferation were decreased. Decreased responsiveness to PWM was abrogated by preculturing PBMC in media alone before PWM stimulation. Decreased responsiveness to PHA was not reversed by a similar period of preculture. To further define the above abnormalities in immunoregulation we examined mononuclear subpopulations. In controls, adding purified T cells or Con A activated lymphocytes to autologous cultures which had been stimulated with PHA and PWM significantly decreased proliferative activity. No such suppressive activity of T cells or Con A activated cells from the patient or family members was noted. These data demonstrate an absent or functionally inactive spontaneous and Con A activated T suppressor cells in the family of a patient with Waldenström's macroglobulinemia.

Topics: Adult; Aged; Concanavalin A; Female; Humans; Lymphocyte Activation; Male; Middle Aged; T-Lymphocytes, Regulatory; Waldenstrom Macroglobulinemia

Normal and leukaemic lymphoid cells, both human and murine, were stained for specific carbohydrates with three fluorescein-labelled lectins: Aprotinin for sialyl (or uronyl) groups: Ricinus agglutinin for galactosyl groups; and Concanavalin A for mannosyl (or glucosyl) groups. The method gives permanent preparations of sections from methanol fixed, paraffin embedded tissues, from blood and bone marrow films or touch preparations of lymph nodes that were methanol fixed. Whereas normal lymphocytes and lymphoblasts reacted strongly for sialyl groups, lymphoblasts of acute lymphoblastic leukaemia and lymphocytes of chronic lymphocytic leukaemia gave a much weaker reaction. The same was the case of the lymphocytes of the Sézary variant and the lymphocytes of macroglobulinaemia. The fine processes of the cells of hairy cell leukaemia stained well for sialyl groups. No obvious differences were detected between normal monocytes and the cells of monocytic leukaemia, nor between normal plasma cells and those of myeloma.

Topics: Animals; Aprotinin; Carbohydrates; Concanavalin A; Fluoresceins; Humans; In Vitro Techniques; Lectins; Leukemia; Leukemia, Hairy Cell; Leukemia, Lymphoid; Leukemia, Monocytic, Acute; Lymphoid Tissue; Mice; Multiple Myeloma; Waldenstrom Macroglobulinemia

Pentameric IgM is precipitable by PHA whereas monomeric IgM is not. During electrophoresis in PHA-containing agar gel pentameric IgM is selected by precipitation from concomitant monomeric IgM which may be visualized separately as a precipitation line with specific antibody. This antibody-like use of the lectin in PHA selection electrophoresis provides a quick and simple method of screening macroglobulinemic sera and other biological fluids for the presence of naturally occurring monomeric IgM subunits.

Topics: Absorption; Animals; Binding Sites; Concanavalin A; Electrophoresis, Agar Gel; Goats; Humans; Immunoelectrophoresis; Immunoglobulin M; Paraproteinemias; Phytohemagglutinins; Polymers; Precipitins; Rabbits; Ricin; Waldenstrom Macroglobulinemia