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Interleukin 1 and tumour necrosis factor increase phosphorylation of fibroblast proteins
Author(s) -
Kaur P.,
Saklatvala J.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81019-6
Subject(s) - phosphoserine , phosphorylation , serine , cytosol , tumor necrosis factor alpha , cytokine , microbiology and biotechnology , kinase , threonine , chemistry , biology , necrosis , biochemistry , endocrinology , immunology , enzyme , genetics
Interleukin 1 (IL1) or tumour necrosis factor (TNF) stimulated phosphorylation of a triad of 27 kDa phosphoproteins (p I 6.0, 5.7 and 5.5) in human dermal fibroblasts. The change was dependent on the dose of cytokine in the range 0.1–20 ng, was detectable between 3 and 5 min after stimulation and was maximal by 10 min. The proteins were found in the cytosol after subcellular fractionation. The 32 P was removed from them by alkali, indicating the presence of phosphoserine and/or phosphothreonine. The results suggest that early changes in serine/threonine protein kinase activity may be involved in responses of fibroblasts to IL1 and TNF.