Abstract
In line with the theme of this meeting, this contribution will confine itself to a consideration of how the IgM molecule could alter its conformation on binding to antigens, so as to provide a signal for the binding and subsequent activation of C1, the first component of the classical complement system. A model for the IgM molecule (based on electron microscopy and other evidence) which we have found useful is shown in Figure 1.1. In each of the five subunits a pair of Cµ2 domains is present where a hinge region would be found in the IgG molecule.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
A. Feinstein, Conclusions. An IgM model, in:“Prog.Immunol.(II)” L. Brent and J. Holborrow, eds., North Holland, Amsterdam 115 (1974).
H. Metzger, The effect of antigen on antibodies: Recent studies in:Cont.Topics Molecular Imm. 7. R.A. Reisfeld and F.P. Inman, eds., Plenum Press, New York. 119. (1978).
T. Borsos, and H.J. Rapp, Hemolysin titration based on fixation of the activated first component of complement. Evidence that one molecule of hemolysin suffices to sensitize an erythrocyte. J.Immun. 95:559 (1965).
T. Borsos and H.J. Rapp, Complement fixation on cell surfaces by 19S and 7S antibodies, Science N.Y. 150:505 (1963).
T. Ishizaka, T. Tada, and K. Ishizaka, Fixation of C’ and C’la by rabbit γG and γM antibodies with particulate and soluble antigens, J.Immun. 100:1145 (1968).
A. Feinstein, E.A. Munn, and N.E. Richardson, The three-dimensional conformation of γM and γA globulin molecules, Ann.N.Y. Acad.Sci. 190:104 (1971).
D. Beale and A. Feinstein, Structure and function of the constant regions of immunoglobulins, Q.Rev.Biophys. 9:135 (1976).
A. Feinstein and D. Beale, Models of immunoglobulins and antigenantibody complexes, in:“Immunochemistry ‘An advanced textbook’,” L.E. Glynn and M.W. Steward, eds., Wiley, Chichester. 263 (1977).
E.A. Munn, L. Bachmann, and A. Feinstein, Structure of hydrated immunoglobulins and antigen-antibody complexes. Electron microscopy of spray-freeze-etched specimens, Biochim.Biophys.Acta. 625:1 (1980).
F. Karush, M-M Chua, and J.D. Rodwell, Interaction of a bivalent ligand with IgM anti-lactose antibody, Biochemistry 18:2226 (1979).
J.C. Brown and M.E. Koshland, Activation of antibody Fc function by antigen-induced conformational changes, Proc.Natl.Acad.Sci. U.S.A. 72:511 (1975).
H-C. Chiang and M.E. Koshland, Antigen induced conformational changes in IgM antibody. I. The role of the antigenic determinant, J.Biol.Chem. 254:2736 (1979).
G.M.K. Humphries and H.M. McConnell, Membrane-controlled depletion of complement activity by spin label-specific IgM, Proc.Natl.Acad.Sci.U.S.A. 74:3537 (1977).
T. Borsos, R.M. Chapuis and J.J. Langone, Distinction between fixation of C1 and the activation of complement by natural IgM antihapten antibody: effect of cell surface hapten density, Mol.Immunol. 18:863 (1981).
A. Feinstein and N.E. Richardson, Structure and Activity of IgM, in:“Immunology 1978,” J. Gergely, G.A. Medgyesi, and S.R. Hollan, eds., Akademiai Kiado, Budapest. 257 (1978).
E.J. Folkerd, B. Gardner, and N.C. Hughes-Jones, The relationship between the binding ability and the rate of activation of the complement component C1, Immunology 41:179 (1980).
D. Beale and J.K. Fazakerley, The action of pepsin on porcine immunoglobulin M and its effect on biological activity. Biochem.J. 191:183 (1980).
N.C. Hughes-Jones, Functional affinity constants of the reaction between 125I-labelled C1q and C1q binders and their use in the measurement of plasma C1q concentrations, Immunology 32:191 (1977).
A. Feinstein and N.E. Richardson, Tertiary structure of the constant regions of immunoglobulins in relation to their function, Monogr.Allergy. 17:28 (1981).
R.C. Siegel and R.E. Cathou, Conformation of immunoglobulin M. III. Structural requirements of antigen for complement fixation by equine IgM, J.Immunol. 125:1910 (1980).
N.M. Young, I.B. Jocius, and M.A. Leon, Binding properties of a mouse immunoglobulin M myeloma protein with carbohydrate specificity, Biochemistry 10:3457 (1971).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1983 Plenum Press, New York
About this chapter
Cite this chapter
Feinstein, A., Richardson, N.E., Gorick, B.D., Hughes-Jones, N.C. (1983). Immunoglobulin M Conformational Change is a Signal for Complement Activation. In: Celada, F., Schumaker, V.N., Sercarz, E.E. (eds) Protein Conformation as an Immunological Signal. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3778-2_6
Download citation
DOI: https://doi.org/10.1007/978-1-4613-3778-2_6
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-3780-5
Online ISBN: 978-1-4613-3778-2
eBook Packages: Springer Book Archive