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The University of Texas Medical Branch, Division of Allergy and Immunology, Department of Internal Medicine, Galveston, Texas 77555-0762
Cytokines are important regulators of
hematopoiesis. They exert their actions by binding to specific
receptors on the cell surface. Interleukin-5 (IL-5) is a critical
cytokine that regulates the growth, activation, and survival of
eosinophils. Because eosinophils play a seminal role in the
pathogenesis of asthma and allergic diseases, an understanding of the
signal transduction mechanism of IL-5 is of paramount importance. The
IL-5 receptor is a heterodimer of 
- and 
-subunits. The
-subunit is specific, whereas the -subunit is common to IL-3,
IL-5, and granulocyte/macrophage colony-stimulating factor (GM-CSF)
receptors and is crucial for signal transduction. It has been shown
that there are two major signaling pathways of IL-5 in eosinophils.
IL-5 activates Lyn, Syk, and JAK2 and propagates signals through the
Ras-MAPK and JAK-STAT pathways. Studies suggest that Lyn, Syk, and JAK2
tyrosine kinases and SHP-2 tyrosine phosphatase are important for
eosinophil survival. In contrast to their survival-promoting activity,
Lyn and JAK2 appear to have no role in eosinophil degranulation or
expression of surface adhesion molecules. Raf-1 kinase, on the other
hand, is critical for eosinophil degranulation and adhesion molecule
expression. Btk is involved in IL-5 stimulation of B cell function.
However, it does not appear to be important for eosinophil function.
Thus a clear segregation of signaling molecules based on their
functional importance is emerging. This review describes the signal
transduction mechanism of the IL-3/GM-CSF/IL-5 receptor system and
compares and contrasts IL-5 signaling between eosinophils and B cells.
interleukin-5; eosinophil; kinase; granulocyte-macrophage colony-stimulating factor
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