Mouse immunoglobulin receptors on lymphocytes: identification of IgM and IgD molecules by tryptic cleavage and a postulated role for cell surface IgD.
The two mouse immunoglobulin receptors on lymphocytes (IgM and IgD-like) were individually digested by trypsin. The tryptic susceptibility, and the products released, were similar to those of their human counterparts. Evidence for a structural homology between human IgD and its presumed mouse conterpart has been provided by the ramarkably similar profile of fragments resulting from digestion. More definitive homology awaits sequence determination. The extreme susceptibility of surface IgD to proteolysis contrasted with the resistance of surface IgM. We therefore propose that the major role of IgD is to release a fragment (Fabdelata) following exposure to antigen and then elicit a regulatory anti-idiotype response which acts through recognition of the protease-resistant IgM idiotype remaining on the cell surface.
D000818:Animals; D000918:Antibody Specificity; D007072:Immunoglobulin D; D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007075:Immunoglobulin M; D007138:Immunoglobulin delta-Chains; D008214:Lymphocytes / Q000276:immunology*; D051379:Mice; D011947:Receptors, Antigen, B-Cell; D013601:T-Lymphocytes / Q000276:immunology; D014357:Trypsin / Q000494:pharmacology
D007072:Immunoglobulin D; D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007075:Immunoglobulin M; D007138:Immunoglobulin delta-Chains; D011947:Receptors, Antigen, B-Cell; D014357:Trypsin