A comparison of the effects of heat-aggregated and chemically cross-linked IgG on monocyte C2 production

Whaley, K., Lappin, D., McPhaden, A.R., Riches, D.W. and Sandilands, G.P. (1983) A comparison of the effects of heat-aggregated and chemically cross-linked IgG on monocyte C2 production. Immunology, 49(3), pp. 457-461.

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Abstract

Heat or alkali-aggregated IgG was found to inhibit C2 production by monocytes, whereas chemically cross-linked IgG and antigen-antibody complexes stimulated C2 synthesis. Chemically cross-linked IgG was shown to inhibit monocyte EA-rosette formation presumably because it blocked monocyte Fc receptors. Furthermore stimulation of C2 synthesis was limited to polymers of the IgG1 and IgG3 subclasses. In contrast, heat-aggregated IgG failed to inhibit monocyte EA-rosette formation significantly, and all the heat-aggregated IgG subclasses inhibited C2 production. It therefore appears that physically aggregated IgG does not bind effectively to Fc receptors. As the effects of physically aggregated IgG C2 production are similar to those of the hydrophobic proteins casein and alkali-denatured human serum albumin (HSA), it is suggested that hydrophobic residues in the aggregates bind preferentially to the lipid component of the cell membrane.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Lappin, Dr David and Sandilands, Dr Gavin
Authors: Whaley, K., Lappin, D., McPhaden, A.R., Riches, D.W., and Sandilands, G.P.
Subjects:Q Science > QR Microbiology > QR180 Immunology
College/School:College of Medical Veterinary and Life Sciences > School of Medicine, Dentistry & Nursing > Dental School
College of Medical Veterinary and Life Sciences > School of Medicine, Dentistry & Nursing
Journal Name:Immunology
ISSN:0019-2805
ISSN (Online):1365-2567
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