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Am J Physiol Cell Physiol 279: C2011-C2018, 2000;
0363-6143/00 $5.00
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Vol. 279, Issue 6, C2011-C2018, December 2000

Serine phosphorylation of p60 tumor necrosis factor receptor by PKC-delta in TNF-alpha -activated neutrophils

Laurie E. Kilpatrick, Young-Han Song, Michael W. Rossi, and Helen M. Korchak

Departments of Pediatrics and Biochemistry/Biophysics, University of Pennsylvania School of Medicine, and the Joseph Stokes Jr. Research Institute of the Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104

Tumor necrosis factor-alpha (TNF-alpha ) triggers degranulation and oxygen radical release in adherent neutrophils. The p60TNF receptor (p60TNFR) is responsible for proinflammatory signaling, and protein kinase C (PKC) is a candidate for the regulation of p60TNFR. Both TNF-alpha and the PKC-activator phorbol 12-myristate 13-acetate triggered phosphorylation of p60TNFR. Receptor phosphorylation was on both serine and threonine but not on tyrosine residues. The PKC-delta isotype is a candidate enzyme for serine phosphorylation of p60TNFR. Staurosporine and the PKC-delta inhibitor rottlerin inhibited TNF-alpha -triggered serine but not threonine phosphorylation. Serine phosphorylation was associated with receptor desensitization, as inhibition of PKC resulted in enhanced degranulation (elastase release). After neutrophil activation, PKC-delta was the only PKC isotype that associated with p60TNFR within the correct time frame for receptor phosphorylation. In vitro, only PKC-delta , but not the alpha -, beta I-, beta II-, or zeta -isotypes, was competent to phosphorylate the receptor, indicating that p60TNFR is a direct substrate for PKC-delta . These findings suggest a selective role for PKC-delta in negative regulation of the p60TNFR and of TNF-alpha -induced signaling.

cytokines; serine/threonine kinases; signal transduction; inflammation


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