Neutrophil respiratory burst following liver transplantation: in vitro effects of granulocyte colony-stimulating factor

1999 ◽  
Vol 1 (3) ◽  
pp. 153-156 ◽  
Author(s):  
K. Jaeger ◽  
H. Ruschulte ◽  
J. Heine ◽  
D. Scheinichen ◽  
M. Leuwer ◽  
...  
Blood ◽  
2002 ◽  
Vol 99 (1) ◽  
pp. 384-386 ◽  
Author(s):  
Maria Luisa Sulis ◽  
Carmella Van de Ven ◽  
Theresa Henderson ◽  
Lauren Anderson ◽  
Mitchell S. Cairo

Concomitant use of allogeneic donor granulocyte transfusions and amphotericin B in febrile neutropenic recipients may be limited by the increased incidence of respiratory distress. In vitro effects of amphotericin B and AmBisome were compared on polymorphonuclear leukocyte (PMN) aggregation from PMNs isolated from granulocyte–colony-stimulating factor (G-CSF)/dexamethasone–mobilized allogeneic donors. Six allogeneic donors were mobilized with G-CSF (600 μg subcutaneously) and dexamethasone (8 mg orally) 12 hours before leukopheresis. AmBisome was associated with significantly less PMN aggregation (100 μM [μg/mL]) (0.33% ± 0.33% vs 54.33% ± 5.82%; P < .001) than amphotericin B. Furthermore, with the addition of the PMN agonist, FMLP, AmBisome was also associated with significantly less aggregation (100 μM [μg/mL]) (18.67% ± 1.45% vs 54.67% ± 2.4%;P < .001). In summary, these studies demonstrate that liposomal amphotericin is associated with significantly less in vitro PMN aggregation than amphotericin B and could possibly be administered concomitantly with mobilized allogeneic PMN infusions.


Blood ◽  
2011 ◽  
Vol 118 (4) ◽  
pp. 1077-1086 ◽  
Author(s):  
Muneyoshi Futami ◽  
Quan-sheng Zhu ◽  
Zakary L. Whichard ◽  
Ling Xia ◽  
Yuehai Ke ◽  
...  

Abstract Src activation involves the coordinated regulation of positive and negative tyrosine phosphorylation sites. The mechanism whereby receptor tyrosine kinases, cytokine receptors, and integrins activate Src is not known. Here, we demonstrate that granulocyte colony-stimulating factor (G-CSF) activates Lyn, the predominant Src kinase in myeloid cells, through Gab2-mediated recruitment of Shp2. After G-CSF stimulation, Lyn dynamically associates with Gab2 in a spatiotemporal manner. The dephosphorylation of phospho-Lyn Tyr507 was abrogated in Shp2-deficient cells transfected with the G-CSF receptor but intact in cells expressing phosphatase-defective Shp2. Auto-phosphorylation of Lyn Tyr396 was impaired in cells treated with Gab2 siRNA. The constitutively activated Shp2E76A directed the dephosphorylation of phospho-Lyn Tyr507 in vitro. Tyr507 did not undergo dephosphorylation in G-CSF–stimulated cells expressing a mutant Gab2 unable to bind Shp2. We propose that Gab2 forms a complex with Lyn and after G-CSF stimulation, Gab2 recruits Shp2, which dephosphorylates phospho-Lyn Tyr507, leading to Lyn activation.


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