Actin: A Target of Lipopolysaccharid-Induced Phosphorylation in Human Monocytes

We have previously reported that lipopolysaccharide (LPS) causes altered phosphate labelling of cytosolic proteins of 36 kDa and 38 kDa (p36/38) and that inhibition of phosphorylation is accompanied by a loss of cytokine production. Here we have purified the two phosphorylated proteins via two-dimen...

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Published inBiochemical and biophysical research communications Vol. 241; no. 3; pp. 670 - 674
Main Authors Hauschildt, Sunna, Schwarz, Claus, Heine, Holger, Ulmer, Artur J., Flad, Hans-D., Rietschel, Ernst T., Jensen, Ole N., Mann, Matthias
Format Journal Article
LanguageEnglish
Published Elsevier Inc 29.12.1997
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Summary:We have previously reported that lipopolysaccharide (LPS) causes altered phosphate labelling of cytosolic proteins of 36 kDa and 38 kDa (p36/38) and that inhibition of phosphorylation is accompanied by a loss of cytokine production. Here we have purified the two phosphorylated proteins via two-dimensional polyacrylamide gel electrophoresis. P 36 was found to consist of two proteins p36a and p36b. The proteins were analysed by matrix-assisted laser desorption ionization (MALDI) mass spectrometry and p36b was identified as γ-actin, p36a as β/γ-actin. The ability of LPS to cause altered phosphate labelling of β/γ-actin suggests a participation of the microfilament network in LPS-induced monocyte activation.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.7887