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Interleukin 1 receptors and biological responses
C A Dinarello1, B D Clark, T Ikejima
1Department of Medicine, Tufts University School of Medicine, Boston, Massachusetts.
The Yale Journal of Biology and Medicine
|March 1, 1990
Summary
Interleukin 1 (IL-1) receptors are crucial for its diverse actions. This review examines the physical nature of IL-1 receptors, including the dominant 80 kDa form and other binding proteins, to understand IL-1 signaling pathways.
Area of Science:
- Immunology
- Neuroscience
- Cell Biology
Background:
- Interleukin 1 (IL-1) exhibits diverse biological functions, including pyrogenesis and immune cell activation.
- IL-1 influences neural pathways, affecting the hypothalamus to induce fever and sleep.
- Understanding IL-1 receptors (IL-1R) is key to elucidating its complex signaling.
Purpose of the Study:
- To review the physical characteristics of the dominant 80 kDa IL-1R found on murine T cells.
- To discuss newly identified IL-1 binding proteins (68-75 kDa on B cells, 26-30 kDa on T cells and mesangial cells).
- To explore the relationship between IL-1R properties and biological responses.
Main Methods:
- Review of existing literature on IL-1 receptor characterization.
- Analysis of data concerning the physical properties of various IL-1 binding proteins.
- Discussion of the discrepancies between receptor binding and biological effects.
Main Results:
- The dominant high-affinity IL-1R on murine T cells is an 80 kDa protein.
- Additional IL-1 binding proteins of 68-75 kDa and 26-30 kDa exist on different cell types.
- Significant discrepancies exist between the number/affinity of 80 kDa IL-1R and observed biological responses.
Conclusions:
- Multiple IL-1 binding proteins may function as IL-1 receptors, potentially forming complexes for signal transduction.
- The roles of the 68-75 kDa and 26-30 kDa IL-1 binding proteins in biological responses require further investigation.
- Hydrolysis of non-phosphatidyl inositol phospholipids is implicated in IL-1 signaling.