Priming of human neutrophils by tumour necrosis factor-alpha and substance P is associated with tyrosine phosphorylation.
The mechanisms involved in neutrophil 'priming' are unknown. 'Priming' by substance P and tumour necrosis factor-alpha (TNF-alpha) occurred without effecting cytosolic-free Ca2+ signalling and was independent of actin polymerization. We demonstrate here that these two primers, which act on different receptor classes, both cause tyrosine phosphorylation of a number of protein substrates including a prominent 74,000 MW protein. This protein was not recognized by anti-c-raf antibodies. The concentration relationship and time-course of tyrosine phosphorylation were consistent with a role in mediating priming. Pretreatment with genistein both inhibited tyrosine phosphorylation and abolished the priming by either substance P or TNF-alpha.
Lloyds
D
D
University Department of Surgery, University of Wales College of Medicine, Cardiff, UK.
Brindle
N P
NP
Hallett
M B
MB
D019833:Genistein; D006801:Humans; D007150:Immunohistochemistry; D007529:Isoflavones / Q000494:pharmacology; D009504:Neutrophils / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation / Q000187:drug effects; D011505:Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors*; D013373:Substance P / Q000494:pharmacology*; D014409:Tumor Necrosis Factor-alpha / Q000494:pharmacology*; D014443:Tyrosine / Q000378:metabolism*
D007529:Isoflavones; D010750:Phosphoproteins; D014409:Tumor Necrosis Factor-alpha; D013373:Substance P; D014443:Tyrosine; D019833:Genistein; D011505:Protein-Tyrosine Kinases