Induction of heat-shock protein 70 in neutrophils during exposure to subphysiologic temperatures.
The expression of heat-shock protein (HSP) 70, a marker of cellular stress, was evaluated in neutrophils. In cells isolated by conventional method, expression of both the inducible HSP72 and the constitutive HSP73 forms of HSP70 was found. This was observed when cells were isolated at room temperature or at 4 degrees C. When autologous plasma was used during the isolation procedure and the entire procedure was done at 37 degrees C, there was no expression of HSP72. Omission of plasma from the isolation procedure done at 37 degrees C also resulted in increased expression of HSP72. These studies demonstrate that the expression of HSP70 in neutrophils is induced by isolation at low temperatures and in the absence of plasma. These observations may be important for studies of the regulation of HSP expression and for other studies that relate to neutrophil activation.
Cox
G
G
Department of Medicine, University of Iowa College of Medicine, Iowa City.
Moseley
P
P
Hunninghake
G W
GW
D000328:Adult; D015153:Blotting, Western; D002469:Cell Separation; D002478:Cells, Cultured; D003080:Cold Temperature; D003470:Culture Media; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006801:Humans; D009504:Neutrophils / Q000378:metabolism*
D003470:Culture Media; D006360:Heat-Shock Proteins