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Demonstration and partial characterization of the interferon-gamma receptor on human B lymphocytes
T Nakagawa1, N Nakagawa, G A Delsing
1Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892.
Insights
Normal human B cells and B cell lines express high-affinity interferon-gamma (IFN-gamma) receptors. These receptors, approximately 93 kD, are constitutively present on B lymphocytes and are internalized rapidly.
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Background:
- Interferon-gamma (IFN-gamma) is a crucial cytokine involved in immune regulation.
- Understanding IFN-gamma receptor expression on B cells is vital for comprehending B cell function and immune responses.
Purpose of the Study:
- To investigate the expression and characteristics of IFN-gamma receptors on normal human B cells and B cell lines.
- To determine the molecular weight and binding affinity of the IFN-gamma receptor.
Main Methods:
- Radiolabeling of recombinant human IFN-gamma with [gamma-32P]ATP.
- Binding assays to quantify receptor number and affinity.
- Chemical cross-linking to determine receptor molecular weight.
- In vitro activation of B cells using Staphylococcus aureus Cowan strain I (SAC).
Main Results:
- All tested B cell lines and normal unactivated B lymphocytes express high-affinity IFN-gamma receptors.
- Normal B cells exhibit approximately 1,400 receptors/cell with an affinity of 295 pM.
- Activation with SAC led to a decrease in receptor number and density.
- A 93 kD IFN-gamma receptor was identified, forming a 110 kD complex upon ligand binding.
- Rapid internalization of IFN-gamma was observed in B cell lines and normal B cells.
Conclusions:
- Normal human B lymphocytes constitutively express a ~93 kD IFN-gamma receptor.
- This receptor is similar to that found on Epstein-Barr virus-transformed B cell lines.
- The findings provide insights into IFN-gamma signaling pathways in B cells.
Abstract:
The expression of interferon-gamma (IFN-gamma) receptors on normal human B cells and four B cell lines was studied. Recombinant human IFN-gamma was labeled with [gamma-32P]ATP using the catalytic subunit of a cAMP-dependent protein kinase. All four B cell lines, although differing in their responsiveness to IFN-gamma, were found to express high-affinity receptors (1,000-11,000 receptors/cell). Normal unactivated B lymphocytes were also found to express constitutively high-affinity receptors, approximately 1,400 receptors per cell with an estimated affinity of 295 pM. Activation of the normal B cells in vitro with the polyclonal B cell activator, Staphylococcus aureus Cowan strain I (SAC), resulted in a slight decline in receptor number and a more pronounced fall in receptor density. One of the B cell lines and unactivated normal B cells were shown to internalize labeled IFN-gamma rapidly. Chemical cross-linking of 32P-IFN-gamma to the CB B cell line and to freshly isolated B lymphocytes revealed one major cross-linked receptor-ligand complex which had an estimated molecular weight of approximately 110 kilodaltons. This complex corresponded to a 93 kD receptor cross-linked to recombinant IFN-gamma. Our data indicate that normal B lymphocytes constitutively express an approximately 93 kD IFN-gamma receptor which is similar to the receptor present on Epstein-Barr virus-transformed B cell lines.
