Phagocytic peripheral blood monocytes from rabbits and humans express membrane receptors specific for IgM molecules: evidence that incubation with neuraminidase exposes cryptic IgM (Fc) receptors

• Published in: Clinical and experimental immunology Vol. 35; no. 3; pp. 484 - 490
• Main Author: Haegert, D G
• Format: Journal Article
• Language: English
• Published: England 01-03-1979
• Subjects: Animals; Cell Membrane - immunology; Humans; Immunoglobulin Fab Fragments - immunology; Immunoglobulin Fc Fragments - immunology; Immunoglobulin M - immunology; Monocytes - immunology; Neuraminidase; Phagocytosis; Rabbits; Receptors, Antigen, B-Cell - immunology; Rosette Formation
• ISSN: 0009-9104; 1365-2249

Phagocytic human and rabbit peripheral blood monocytes, identified by their ingestion of polystyrene particles, were investigated for the presence of surface membrane receptors for IgM molecules. After incubation of freshly isolated monocytes with IgM anti-sheep erythrocyte (SRBC) preparations, a mean of 0.7% of human monocytes and a mean of 16.2% of rabbit monocytes formed rosettes with SRBC. However, if the monocytes were pre-incubated with vibrio cholerae neuraminidase (VCN), these figures increased to 32.6% and 37.8% respectively. The specificity of rosette formation by VCN-treated monocytes was established in several experiments; SRBC sensitized with a F(ab')2 preparation of an IgG anti-SRBC reagent completely failed to rosette with VCN-treated monocytes, and inclusion of IgM, but not other Ig or non-Ig protein molecules in the test medium, inhibited rosette formation. Further, and most important, rosette formation by human monocytes was inhibited by F(c)5mu but not by Fabmi fragments. These findings indicate that both rabbit and human monocytes express IgM-class specific membrane receptors for IgM molecules, that these receptors may be cryptic or hidden but can be revealed by treatment with VCN and that the human monocyte IgM receptor is F(c) specific. Further, the rabbit monocyte IgM receptor was shown to be trypsin-resistant.