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C1q receptor on murine cells
1Basel Institute for Immunology, Switzerland.
Insights
Murine B cells and macrophages bind the C1q subcomponent, with varying capacity across different cell types. These C1q-binding molecules on murine cells are antigenically similar to human C1q receptors.
Area of Science:
- Immunology
- Cell Biology
Background:
- The complement system plays a crucial role in innate and adaptive immunity.
- C1q is the initiating component of the classical complement pathway.
- Understanding C1q-cell interactions is vital for immunomodulation.
Purpose of the Study:
- To investigate the binding capacity of the C1q subcomponent to various murine cells.
- To identify and characterize C1q-binding molecules on murine cells.
- To assess the antigenic relationship between murine and human C1q receptors.
Main Methods:
- Cytofluorometric analysis using biotinylated human C1q and streptavidin-FITC.
- In vitro cell activation assays.
- C1q affinity chromatography followed by SDS-PAGE.
- Immunological cross-reactivity using a polyclonal antibody against human C1q receptor.
Main Results:
- Splenocytes and thymocytes showed the majority of C1q-reactive cells in B cell and macrophage populations.
- Activated B cell blasts demonstrated significant C1q binding, while T cell blasts did not.
- Pre-B lymphomas and myeloid cell lines exhibited strong C1q binding (90-98%).
- SDS-PAGE identified C1q-binding molecules at approximately 80 kDa, with additional bands at 50 and 45 kDa in splenocytes and B cell blasts.
- A polyclonal antibody against human C1q receptor cross-reacted with murine C1q-binding molecules.
Conclusions:
- Murine B cells and macrophages are primary C1q-binding cells.
- C1q-binding capacity varies significantly with cell type and activation status.
- Murine C1q receptors share antigenic similarities with their human counterparts.
Abstract:
Different cells and cell lines of murine origin were tested for their capacity to bind the C subcomponent C1q by using biotinylated human C1q and streptavidin-FITC. Cytofluorometric analysis of splenocytes and thymocytes shows that the majority of C1q-reactive cells reside in the population of B cells and macrophages. There is a significant difference in the C1q-binding capacity of in vitro activated cells; although more than half of the B cell blasts bind the C subcomponent, T cell blasts are virtually negative. It is shown that pre-B lymphomas and cell lines of myeloid origin bind C1q strongly (90 to 98%), whereas in the case of mature B cell lymphomas, plasmocytomas, and the tested T cell lines, the percentage of C1q binding cells varies from 0 to 56. C1q affinity chromatography of the detergent extracts from P388D1 and WEHI-3 cells followed by SDS-PAGE of the eluted proteins under reducing conditions reveals a band at approximately 80 kDa. Analysis of splenocytes shows two additional minor C1q-binding molecules with apparent molecular masses of 50 and 45 kDa, whereas in the case of B cell blasts three bands of similar density are seen at approximately 95, 50 and 45 kDa. C1q-receptors of murine cells are shown to be antigenically related to their human counterpart, because a polyclonal antibody (266A) raised against the human C1q receptor reacts with them.
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