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Relationship of Immunoglobulin to Complement Receptors of Human B Cells¹

From the Division of Allergy and Immunology, Department of Medicine, School of Medicine, University of Pennsylvania and Veterans Administration Hospital, Philadelphia, Pennsylvania 19174

Abstract

By using the disappearance of the surface Ig from human peripheral lymphocytes as a parameter of modulation, at 37°C it was shown that anti-Fab antibody is a more effective and faster modulator of the surface Ig than anti-Fc, anti-IgM, or anti-IgG antibodies. The C-binding site was demonstrated to be fully independent and distinct from the surface Ig and a stable marker of Ig-bearing cells. The C receptor can be blocked by the addition of fresh C5-sufficient, C5-deficient mouse serum, or fresh autologous human serum, at 37°C before binding to EAC by a mechanism still to be defined. Both IgM and IgG cells possess the C receptor. The relationship of Ig to C receptors and their role in cell activation by the specific antigen is discussed.

Footnotes

¹ This investigation was supported by Veterans Administration Grant 642-0030 and by United States Public Health Service Grant AI 00319 and AM 13-515.

² Dr. Nilsson is a recipient of a Research Career Development Award of United States Public Health Service Grant AI-50198-02.