Glycosylated or non-glycosylated G-CSF differently influence human granulocyte functions through RhoA

Leuk Res. 2005 Nov;29(11):1285-92. doi: 10.1016/j.leukres.2005.04.011.

Abstract

Granulocyte function may be altered after in vivo G-CSF administration and this has been related to both an immaturity of mobilized cells and to a defect in F-actin polymerization. In this paper we show that in resting Filgrastim (non-glycosylated G-CSF)-pulsed cells, F-actin polymerization, membrane-linked RhoA and cell polarization are enhanced compared to those found in resting Lenograstim (glycosylated G-CSF)-cells. The basal hyper-activation of RhoA could be responsible for the morphological and functional modifications of Filgrastim-mobilized cells. Moreover, Filgrastim-mobilized cells, but not Lenograstim-mobilized cells, are unable to correctly respond to LPS stimulation, as demonstrated by minor further RhoA activation and cell elongation.

Publication types

  • Comparative Study

MeSH terms

  • Actins / chemistry
  • Actins / drug effects
  • Actins / physiology
  • Cell Count
  • Cell Polarity / drug effects
  • Cell Polarity / physiology
  • Filgrastim
  • Glycosylation
  • Granulocyte Colony-Stimulating Factor / chemistry
  • Granulocyte Colony-Stimulating Factor / pharmacology*
  • Granulocytes / cytology
  • Granulocytes / drug effects*
  • Granulocytes / physiology*
  • Humans
  • Lenograstim
  • Lymphoma, Non-Hodgkin* / therapy
  • Neutrophils / cytology
  • Neutrophils / drug effects
  • Neutrophils / physiology
  • Peripheral Blood Stem Cell Transplantation
  • Recombinant Proteins / pharmacology
  • Remission Induction
  • rhoA GTP-Binding Protein / metabolism
  • rhoA GTP-Binding Protein / physiology*

Substances

  • Actins
  • Recombinant Proteins
  • RHOA protein, human
  • Granulocyte Colony-Stimulating Factor
  • Lenograstim
  • rhoA GTP-Binding Protein
  • Filgrastim