Measured by its ability to inhibit the G-CSF-induced proliferation of NFS‑60 mouse myelogenous leukemia lymphoblast cells. The ED50 for this effect is 1-4 µg/mL in the presence of 0.125 ng/mL of recombinant human G-CSF.
Mouse myeloma cell line, NS0-derived human G-CSF R/CD114 protein Glu25-Pro621
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
<0.01 EU per 1 μg of the protein by the LAL method.
66.5 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Granulocyte Colony Stimulating Factor (G-CSF) is a pleiotropic cytokine best known for its specific effects on the proliferation, differentiation, and activation of hematopoietic cells of the neutrophilic granulocyte lineage (1). G-CSF plays an important role in defense against infection, in inflammation and repair, and in the maintenance of steady state hematopoiesis. Recombinant human G-CSF has been approved for the amelioration of chemotherapy induced neutropenia as well as for severe chronic neutropenia following marrow transplant.
Cell activation by G-CSF is mediated by a type I membrane protein belonging to the cytokine receptor superfamily. Human G-CSF R is 836 amino acids (aa) in length, with 24 amino acid signal sequence, a 603 aa extracellular domain, a 23 aa transmembrane domain, and a 186 aa cytoplasmic domain. As a result of alternative splicing, at least four isoforms of G-CSF R that differ in their C-terminal region exist. Isoform 2 lacks the transmembrane region and may represent a soluble form of the receptor. The existence of 80 & 85 kDa forms of soluble G-CSF R in human serum has been reported (2). Mutations have been found in the gene encoding G-CSF R in some patients with severe congenital neutropenia. These mutations typically led to a truncation in the cytoplasmic domain of the G-CSF R leading to maturation arrest of neutrophil precursors in the bone marrow and neutropenia in peripheral blood (3). Human and mouse G-CSF R have a homology of 62.5%.
G-CSF R is expressed in mature neutrophils, neutrophilic precursors, myeloid leukemia cells, and placenta. Binding of G-CSF to its receptor induces dimerization or oligomerization of the receptor activating cytoplasmic tyrosine kinases. Signal transduction from pathways that involve Janus tyrosine kinases/signal transducer and activator of transcription proteins (Jak1, Jak2, and Tyk2/STAT3, STAT3, and STATG), src-related protein tyrosine kinases (Lyn and Syk), Ras/MAP kinase, and phosphatidylinositol have been reported to be activated upon G-CSF stimulation (1).
Nicola, N.A., in Cytokine Reference, (2001) Oppenhiem, J.J. and M. Feldmann, eds. Academic Press p. 193
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