PMID: 2116001Aug 1, 1990Paper

Tumor necrosis factor alpha modifies agonist-dependent responses in human neutrophils by inducing the synthesis and myristoylation of a specific protein kinase C substrate

Proceedings of the National Academy of Sciences of the United States of America
M ThelenA Aderem

Abstract

Tumor necrosis factor alpha (TNF-alpha) and bacterial lipopolysaccharide (LPS) induce the synthesis and cotranslational myristoylation of an 82-kDa specific protein kinase C substrate in human neutrophils. The myristic acid is covalently bound via a hydroxylamine-resistant amide linkage to the N-terminal glycine of the protein. The isoelectric point of the protein is at pH 4.6. The protein is rapidly phosphorylated when neutrophils are stimulated with chemotactic agonists or with phorbol 12-myristate 13-acetate, an activator of protein kinase C, and displays two characteristic phosphopeptides in one- and two-dimensional separation systems. Identical phosphopeptides were detected when the 82-kDa protein was phosphorylated in vitro with purified kinase C. The 82-kDa protein was immunoprecipitated by a polyclonal antiserum raised against the 87-kDa specific protein kinase C substrate from bovine brain. From these biochemical and immunological criteria it is concluded that the 82-kDa protein is the human neutrophil homolog of MARCKS, the myristoylated, alanine-rich C kinase substrate previously described in bovine and rat brain and in murine fibroblasts and macrophages. TNF-alpha and LPS prime human neutrophils for potentiated prot...Continue Reading

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Citations

Jul 12, 2005·Marine Biotechnology·Andrea C Hermann, Carol H Kim
Oct 29, 2003·Journal of Immunological Methods·Taisuke OhiraJohn A Badwey
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