ISSN:
1432-1076
Keywords:
Protein phosphorylation
;
Neutrophil
;
Chronic granulomatous disease
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Abstract The phosphorylation and dephosphorylation of proteins in neutrophils from normal children and patients with chronic granulomatous disease (CGD) were studied with two-dimensional gel electrophoresis and autoradiography, followed by densitometric scanning. In normal neutrophils the radio-activities of 11 spots among approximately 50 radioactive spots were changed by stimulation with phorbol 12-myristate 13-acetate (PMA) and 6 of the 11 spots were also changed by stimulation with N-formyl-methionyl-leucyl-phenylalanine (FMLP) and NaF. The phosphorylation of only two spots (Mr=48000 and 62000) was inhibited by 2-deoxyglucose and N-(6-aminohexyl)-5-chloro-1-naphthalene sulphonamide (W-7), which inhibits superoxide production, while it was not affected by dibutyryl cAMP, KCN and ethyleneglycol-bis-(β-aminoethylether)-N,N′-tetraacetic acid (EGTA), which do not affect superoxide production. The observation indicates that the Mr=48000 and 62000 proteins may be involved in the activation process of superoxide production. When the neutrophils of four male and two female CGD patients were examined, the changes in 11 spots on stimulation were similar to those of normal children, indicating that the (de)phosphorylation of the proteins which seems to be involved in the activation process is not affected in CGD neutrophils.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00441847
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