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B-cell activation stimulated by monoclonal anti-Lyb2.1 antibody is mediated through a receptor distinct from the
The experiments in this paper demonstrate that monoclonal anti-Lyb2.1 antibody enhances the proliferative response of anti-immunoglobulin (anti-Ig)-stimulated but not of dextran sulfate-stimulated B cells. The magnitude of this enhanced B-cell proliferation is comparable to that induced by BSF-1 on anti-Ig-stimulated cells. The ability of this antibody to enhance B-cell proliferation does not result from its ability to neutralize the suppressive effects on B-cell activation that is mediated by the Fc fragment of anti-Ig antibody as it is equally as effective in enhancing B-cell proliferative responses stimulated by F(ab')2 fragments of anti-Ig. BSF-1 and Anti-Lyb2.1 appear to stimulate nonoverlapping pathways leading to B-cell activation since the enhanced responses induced by the combination of BSF-1 and anti-Lyb2.1 on anti-Ig-stimulated cells are additive even when maximum quantities of these activators are employed. There is also a marked difference in their activity on T cells; while BSF-1 can enhance T-cell proliferation in synergy with phorbol ester, anti-Lyb2.1 is ineffective in this regard. These data, while consistent with the suggestion that the Lyb2 surface determinant on B cells may be involved in B-cell activation, indicate that it is distinct from the receptors for BSF-1 or BCGF-II.
The experiments in this paper demonstrate that monoclonal anti-Lyb2.1 antibody enhances the proliferative response of anti-immunoglobulin (anti-Ig)-stimulated but not of dextran sulfate-stimulated B cells. The magnitude of this enhanced B-cell proliferation is comparable to that induced by BSF-1 on anti-Ig-stimulated cells. The ability of this antibody to enhance B-cell proliferation does not result from its ability to neutralize the suppressive effects on B-cell activation that is mediated by the Fc fragment of anti-Ig antibody as it is equally as effective in enhancing B-cell proliferative responses stimulated by F(ab')2 fragments of anti-Ig. BSF-1 and Anti-Lyb2.1 appear to stimulate nonoverlapping pathways leading to B-cell activation since the enhanced responses induced by the combination of BSF-1 and anti-Lyb2.1 on anti-Ig-stimulated cells are additive even when maximum quantities of these activators are employed. There is also a marked difference in their activity on T cells; while BSF-1 can enhance T-cell proliferation in synergy with phorbol ester, anti-Lyb2.1 is ineffective in this regard. These data, while consistent with the suggestion that the Lyb2 surface determinant on B cells may be involved in B-cell activation, indicate that it is distinct from the receptors for BSF-1 or BCGF-II.