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Characterization of the IgA receptor from human polymorphonuclear leucocytes
M Albrechtsen1, G R Yeaman, M A Kerr
1Department of Pathology, University of Dundee, Ninewells Hospital and Medical School, U.K.
Immunology
|June 1, 1988
Summary
Human polymorphonuclear leucocytes (PMNs) phagocytose IgA-opsonized yeast and bind IgA-coated beads, releasing lysozyme. A 60 kDa glycosylated protein on PMN membranes binds IgA, indicating a novel immune receptor.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Human polymorphonuclear leucocytes (PMNs) are crucial immune cells.
- Immunoglobulin A (IgA) plays a role in mucosal immunity.
- The specific receptors for IgA on PMNs are not fully characterized.
Purpose of the Study:
- To investigate the interaction between human PMNs and IgA.
- To identify potential IgA-binding proteins on the surface of PMNs.
Main Methods:
- Phagocytosis assays using IgA-opsonized yeast.
- Binding assays with IgA- and IgG-coated Sepharose beads.
- Affinity chromatography using IgA-Sepharose to isolate PMN membrane proteins.
- SDS-PAGE analysis to characterize isolated proteins.
Main Results:
- PMNs phagocytose IgA-opsonized yeast and bind to IgA-coated beads.
- Binding to IgA-Sepharose stimulates lysozyme release from PMNs.
- A 60 kDa polypeptide, likely glycosylated, was isolated from PMN membranes using IgA-Sepharose, but not IgG-Sepharose.
Conclusions:
- Human PMNs possess a specific mechanism for interacting with IgA.
- A novel, heavily glycosylated 60 kDa protein on PMN membranes appears to be an IgA receptor.
- This finding suggests a new pathway for IgA-mediated PMN function in immunity.