C-reactive protein decreases protein phosphorylation in stimulated human neutrophils.
Treatment of human neutrophils with C-reactive protein (CRP) causes a concentration-dependent in the extent of activation of superoxide production and of granule secretion, induced by phorbol-12-myristate-13-acetate (PMA) or N-formyl-L-methionyl-L-leucyl-L-phenylalanine (fMLF). The same treatment also causes a significant reduction in the degree of PMA- and fMLF-stimulated phosphorylation of several cell proteins. These include the proteins of 43-47 kDa, whose extent of phosphorylation correlates with the activation of superoxide production and of secretion. Contrary to the effects exerted on protein phosphorylation, CRP does not affect the fMLF-elicited increase in neutrophil cytosolic Ca2+.
Buchta
R
R
Dipartimento di Biochimica, Biofisica e Chimica delle Macromolecole, Università di Trieste, Italy.
Gennaro
R
R
Pontet
M
M
Fridkin
M
M
Romeo
D
D
D001798:Blood Proteins / Q000378:metabolism*; D002097:C-Reactive Protein / Q000502:physiology*; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D009504:Neutrophils / Q000502:physiology*; D010710:Phosphates / Q000097:blood; D010750:Phosphoproteins / Q000097:blood / Q000302:isolation & purification; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D013481:Superoxides / Q000097:blood
D001798:Blood Proteins; D010710:Phosphates; D010750:Phosphoproteins; D010761:Phosphorus Radioisotopes; D013481:Superoxides; D002097:C-Reactive Protein