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Questions And Answer

• Properties

  Mr. of human G-CSF is 18,671 (calculated polypeptide backbone) and 18–19 kDa on SDS-PAGE (O-glycosylated form secreted from tumor cell lines). The pI varies from 5 to 6 depending on O-glycosylation. The nonglycosylated form produced by E. coli retains biological activity.;

• Synthesis and release

  The expression of the G-CSF gene is regulated by pathogen-mediated transcriptional and posttranscriptional pathways. Inflammatory factors such as bacterial lipopolysaccharide, interleukin-1β, tumor necrosis factor α, IL-1, and IL-17 from Th17 cells induce G-CSF expression via intracellular signaling though NF-κB, C/EBPα, and C/EBPβ. The increase in the number of circulating neutrophils reduces the production of G-CSF in the bone marrow.;

• Agonists and Antagonists

  Filgrastim produced by E. coli attached an additional N-terminal methionine, and lenograstim produced by CHO cells attached a single O-glycan; these were developed as therapeutic biologicals. Other molecules, including pegylated filgrastim, follow as next-generation therapeutic reagents. The fusion proteins of G-CSF with IgG1-Fc and IgG4-Fc are reported. 
  An antagonistic compound specific to G-CSF-G-CSFR signaling has not been reported yet.;

• Biological functions

  G-CSF stimulates the proliferation, differentiation, and survival of neutrophil precursors in the bone marrow to promote their maturation process. G-CSF exerts minimal direct effects on the production of hematopoietic cell types other than the neutrophil lineage, as obtained in white blood cell differentials during clinical trials. The G-CSF-G-CSFR signaling in mature neutrophils activates multiple effector functions in response to bacterial infections, such as superoxide anion generation, the release of arachidonic acid, and the production of leukocyte alkaline phosphatase and myeloperoxidase. Neurons of the CNS express both G-CSF and G-CSF-R, suggesting an autocrine neuroprotection system, as a nonhematopoietic function;

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