Protein kinases in neutrophils: a review.
In chemotactic factor-stimulated neutrophils, rapid increases of intracellular levels of cyclic AMP, calcium, and diacylglycerol have been observed and may be linked to protein kinase activation. The study of the physiological role and regulation of protein kinases in the neutrophil and the identification of their substrates has provided valuable information on the molecular mechanism of neutrophil activation. The focus of this review is on those aspects of protein kinases that are relevant to neutrophil activation and on the substrate proteins for these protein kinases. The possible role of protein phosphorylation in neutrophil function is also discussed.
Huang
C K
CK
Department of Pathology, University of Connecticut Health Center, Farmington 06032.
D000818:Animals; D002118:Calcium / Q000502:physiology; D002147:Calmodulin / Q000502:physiology; D006801:Humans; D009504:Neutrophils / Q000201:enzymology*; D010766:Phosphorylation; D006656:Protamine Kinase / Q000502:physiology; D011493:Protein Kinase C / Q000037:antagonists & inhibitors / Q000502:physiology; D011494:Protein Kinases / Q000097:blood / Q000502:physiology*; D011505:Protein-Tyrosine Kinases / Q000502:physiology
D002147:Calmodulin; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases; D006656:Protamine Kinase; D011493:Protein Kinase C; D002118:Calcium