The murine G-CSF cDNA encodes a 208 amino acid (aa) residue precursor protein containing a 30 aa residue signal peptide that is proteolytically cleaved to generate the 178 aa residue mature protein. Human G-CSF is 73% identical at the amino acid level to murine G-CSF and the two proteins show species cross-reactivity.
In vitro, G-CSF stimulates growth, differentiation and functions of cells from the neutrophil lineage. It also has blast cell growth factor activity and can synergize with IL-3 to shorten the Go period of early hematopoietic progenitors. Consistent with its in vitro functions, G-CSF has been found to play important roles 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.