Signal Transduction from the Haematopoietic Growth Factor Receptors
Haematopoietic growth factors (HGFs) act on the haematopoietic cells via binding to specific cell surface receptors. Many HGF receptors (HGF-R) have certain common structural features and have therefore been grouped in the superfamily of haematopoietin or cytokine receptors also referred to as the class I receptor super-family [1,2]. Activation of these receptors by their respective HGFs is mediated through the formation of dimeric or oligomeric complexes of receptor structures. Some haematopoietin receptors are composed of heteromeric complexes, comprising two or three different receptor chains. For instance this is the case for receptors of interleukin IL-2, IL-3, IL-5, and granulocytemacrophage colony stimulating factor (GM-CSF) . Other receptor structures, e.g., those of granulocyte-CSF (G-CSF) and erythropoietin (EPO), form homodimeric complexes upon growth factor binding [2,4]. This concise overview will start with an introduction to the basic principles of HGF-R signaling. Subsequently, a selection of the recent results obtained in this dynamic area of research, and their implications for our insights in the regulation of normal haematopoietic cell development as well as for understanding disease mechanisms will be briefly discussed.
KeywordsTyrosine Leukemia Serine Interferon Resi
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