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

Biochemical and Biophysical Research Communications
S HauschildtM 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.

References

Nov 18, 1976·Nature·K G Sundqvist, A Ehrnst
Jan 1, 1987·Annual Review of Medicine·D C Morrison, J L Ryan
Apr 7, 1993·Molecular and Cellular Biochemistry·C RiscoJ L Carrascosa
Oct 1, 1995·Electrophoresis·S D Patterson, R Aebersold
Mar 1, 1996·Analytical Chemistry·A ShevchenkoM Mann
Dec 10, 1996·Proceedings of the National Academy of Sciences of the United States of America·A ShevchenkoM Mann

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Citations

Mar 7, 2002·The Biochemical Journal·Andreas GrahnertSunna Hauschildt
Feb 26, 2003·Cell Motility and the Cytoskeleton·Luo GuJing Chen
Aug 4, 1998·Antimicrobial Agents and Chemotherapy·A LührmannS Hauschildt
Jan 30, 2007·Environmental Science & Technology·Augustine Arukwe

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