Literature DB >> 9434766

Actin: a target of lipopolysaccharide-induced phosphorylation in human monocytes.

S Hauschildt1, C Schwarz, H Heine, A J Ulmer, H D Flad, E T Rietschel, O N Jensen, M Mann.   

Abstract

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 gamma-actin, p36a as beta/gamma-actin. The ability of LPS to cause altered phosphate labelling of beta/gamma-actin suggests a participation of the microfilament network in LPS-induced monocyte activation.

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Year:  1997        PMID: 9434766     DOI: 10.1006/bbrc.1997.7887

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Mono-ADP-ribosyltransferases in human monocytes: regulation by lipopolysaccharide.

Authors:  Andreas Grahnert; Maik Friedrich; Martin Pfister; Friedrich Haag; Friedrich Koch-Nolte; Sunna Hauschildt
Journal:  Biochem J       Date:  2002-03-15       Impact factor: 3.857

2.  Immunomodulating properties of the antibiotic novobiocin in human monocytes.

Authors:  A Lührmann; J Thölke; I Behn; J Schumann; G Tiegs; S Hauschildt
Journal:  Antimicrob Agents Chemother       Date:  1998-08       Impact factor: 5.191

  2 in total

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