The evolution of mouse and human complement C3-binding proteins: divergence of form but conservation of function

Immunol Today. 1992 Jun;13(6):231-6. doi: 10.1016/0167-5699(92)90160-9.

Abstract

Despite the fact that the early components of the mouse and human complement cascades are very similar, there are marked differences between the two species in the structure of C3 receptors and the molecules that control homologous lysis. Here, Michael Holers, Taroh Kinoshita and Hector Molina compare and contrast the mouse and human RCA region products and conclude that the receptor and regulatory roles are conserved despite the structural variation.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Animals
  • Antigens, CD / genetics*
  • Antigens, CD / metabolism
  • Antigens, Differentiation, B-Lymphocyte / genetics
  • Antigens, Differentiation, B-Lymphocyte / metabolism
  • Biological Evolution*
  • CD55 Antigens
  • Complement Activation
  • Complement C3 / metabolism*
  • Consensus Sequence
  • Humans
  • Macrophage-1 Antigen / genetics*
  • Macrophage-1 Antigen / metabolism
  • Membrane Cofactor Protein
  • Membrane Glycoproteins / genetics*
  • Membrane Glycoproteins / metabolism
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism
  • Mice / genetics*
  • Mice / immunology
  • Models, Biological
  • Multigene Family*
  • Protein Conformation
  • Receptors, Complement / genetics*
  • Receptors, Complement / metabolism
  • Receptors, Complement 3b
  • Receptors, Complement 3d
  • Recombinant Fusion Proteins / metabolism
  • Repetitive Sequences, Nucleic Acid
  • Species Specificity

Substances

  • Antigens, CD
  • Antigens, Differentiation, B-Lymphocyte
  • CD46 protein, human
  • CD55 Antigens
  • Complement C3
  • Macrophage-1 Antigen
  • Mcp protein, mouse
  • Membrane Cofactor Protein
  • Membrane Glycoproteins
  • Membrane Proteins
  • Receptors, Complement
  • Receptors, Complement 3b
  • Receptors, Complement 3d
  • Recombinant Fusion Proteins