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Increased efficiency of binding of nascent C3b to the erythrocytes of chronic cold agglutinin disease.

Publication ,  Journal Article
Parker, CJ; Soldato, CM; Telen, MJ
Published in: J Clin Invest
September 1984

The pathogenesis of chronic cold agglutinin disease (CCAD) has been enigmatic. To determine if abnormal erythrocyte membrane constituents might provide the stimulus for antibody production, we compared the electrophoretic pattern of radiolabeled membrane glycoproteins of four patients with CCAD to that of normal control erythrocytes. For the CCAD erythrocytes, fluorographs revealed the appearance of an abnormal band whose molecular weight was estimated at 126,000 D. Using two-dimensional gel analysis and immunoblotting techniques, it was determined that the 126,000 D glycoprotein consisted predominately of polymeric glycophorin-alpha. Previous investigations had suggested that abnormalities in glycophorin-alpha influence the functional activity of the complement system. When purified complement (C)3 was activated in the fluid-phase by cobra venom factor complexes, CCAD erythrocytes bound nascent C3b 7-27 times more efficiently than normal erythrocytes. Normal erythrocytes could be induced to manifest the appearance of the 126,000 D band, and the increased efficiency of binding of nascent C3b by incubation with CCAD serum or with the purified cold agglutinin antibody plus autologous serum, but not with the purified antibody alone or the purified antibody plus EDTA-chelated autologous serum. These studies demonstrate that the interactions of IgM cold-reacting antibody and complement with glycophorin induce changes in the biophysical properties of the erythrocyte membrane which modify subsequent interactions with complement.

Duke Scholars

Published In

J Clin Invest

DOI

ISSN

0021-9738

Publication Date

September 1984

Volume

74

Issue

3

Start / End Page

1050 / 1062

Location

United States

Related Subject Headings

  • Sialoglycoproteins
  • Reference Values
  • Receptors, Complement 3b
  • Receptors, Complement
  • Molecular Weight
  • Membrane Proteins
  • Immunology
  • Immunoglobulin M
  • Immunoglobulin G
  • Humans
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Parker, C. J., Soldato, C. M., & Telen, M. J. (1984). Increased efficiency of binding of nascent C3b to the erythrocytes of chronic cold agglutinin disease. J Clin Invest, 74(3), 1050–1062. https://doi.org/10.1172/JCI111472
Parker, C. J., C. M. Soldato, and M. J. Telen. “Increased efficiency of binding of nascent C3b to the erythrocytes of chronic cold agglutinin disease.J Clin Invest 74, no. 3 (September 1984): 1050–62. https://doi.org/10.1172/JCI111472.
Parker CJ, Soldato CM, Telen MJ. Increased efficiency of binding of nascent C3b to the erythrocytes of chronic cold agglutinin disease. J Clin Invest. 1984 Sep;74(3):1050–62.
Parker, C. J., et al. “Increased efficiency of binding of nascent C3b to the erythrocytes of chronic cold agglutinin disease.J Clin Invest, vol. 74, no. 3, Sept. 1984, pp. 1050–62. Pubmed, doi:10.1172/JCI111472.
Parker CJ, Soldato CM, Telen MJ. Increased efficiency of binding of nascent C3b to the erythrocytes of chronic cold agglutinin disease. J Clin Invest. 1984 Sep;74(3):1050–1062.

Published In

J Clin Invest

DOI

ISSN

0021-9738

Publication Date

September 1984

Volume

74

Issue

3

Start / End Page

1050 / 1062

Location

United States

Related Subject Headings

  • Sialoglycoproteins
  • Reference Values
  • Receptors, Complement 3b
  • Receptors, Complement
  • Molecular Weight
  • Membrane Proteins
  • Immunology
  • Immunoglobulin M
  • Immunoglobulin G
  • Humans