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ADP-ribosylation: role in LPS-induced phosphorylation of two cytosolic proteins (p36/38) in monocytes.

Authors
  • Hauschildt, S1
  • Ulmer, A J
  • Flad, H D
  • Heyden, T
  • Heine, H
  • 1 Department of Immunobiology, University of Leipzig, Germany. , (Germany)
Type
Published Article
Journal
Progress in clinical and biological research
Publication Date
Jan 01, 1998
Volume
397
Pages
147–155
Identifiers
PMID: 9575555
Source
Medline
Language
English
License
Unknown

Abstract

Human monocytes respond to LPS by releasing proinflammatory cytokines such as TNF-alpha, IL-1 and IL-6. Here we show that inhibitors of ADP-ribosylation namely nicotinamide and meta-iodobenzylguanidine prevent production of TNF-alpha and IL-6 at the protein and mRNA level. The inhibitors also influence the LPS-induced phosphorylation pattern of cytosolic proteins. They consistently lead to changes of the phosphorylation state of two proteins with an apparent molecular mass of 36 kDa and 38 kDa. The changes are both time and dose dependent. The data suggest that the conditions leading to altered phosphorylation of p36/38 may correlate with conditions initiating and regulating TNF-alpha and IL-6 production.

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