Two Mechanisms for IgG Uptake in Cultured Human Trophoblast: Evidence for a Novel High Affinity Fc Receptor
Autor: | Joseph Dancis, Michael J. Rindler, Abbie L. Esterman, Jeffrey D. Lee |
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Rok vydání: | 1995 |
Předmět: |
Male
Fc receptor Receptors Fc Immunoglobulin E Mice Species Specificity Pregnancy Cell surface receptor Placenta medicine Animals Humans Cells Cultured reproductive and urinary physiology Fetus biology Trophoblast Biological Transport Immunohistochemistry Molecular biology In vitro Trophoblasts Kinetics medicine.anatomical_structure Immunoglobulin G embryonic structures Pediatrics Perinatology and Child Health biology.protein Female Antibody |
Zdroj: | Pediatric Research. 38:1-6 |
ISSN: | 1530-0447 0031-3998 |
DOI: | 10.1203/00006450-199507000-00001 |
Popis: | The mechanism of IgG transport by the placental trophoblast was examined by studying IgG uptake by purified trophoblast maintained in culture. This model retains the ability to bind and endocytose human IgG from human serum. Comparison of the relative IgG uptake by the trophoblast among the four subclasses of both human and mouse IgG indicates that the trophoblast IgG receptor has different affinities from those described for the three known human Fc gamma receptors, FcR gamma I, FcR gamma II, and FcR gamma III. These results suggest the presence of a novel trophoblast Fc gamma receptor. Although Fc gamma RIII has been reported to be present on trophoblasts, immunocytochemical studies failed to detect binding to the cell surface of antibody-specific for Fc gamma RIII, 3G8 MAb. In addition, blocking studies with MAb 3G8 did not interfere with IgG uptake. Scatchard analysis of human IgG uptake revealed a biphasic curve consistent with two distinct mechanisms for the transport of IgG by the trophoblast. The first is a higher affinity system (Ka = 1.7 x 10(7) M-1, 1.7 x 10(4) binding sites/cell) which exhibits IgG subclass and species specificity, and the second is a low affinity system (Ka = 6.9 x 10(3) M-1, 7.5 x 10(7) binding sites/cell). |
Databáze: | OpenAIRE |
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