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Activation of p38 MAP Kinase Is Required for Interleukin-6 Synthesis and NF-k B Transactivation Induced by Lipopolysaccharide (LPS) in Cultured Human Dermal Microvessel Endothelial Cells (HDMEC).

ZHANG FX, FAURE E, ARDITI M; Interscience Conference on Antimicrobial Agents and Chemotherapy.

Abstr Intersci Conf Antimicrob Agents Chemother Intersci Conf Antimicrob Agents Chemother. 1999 Sep 26-29; 39: 382 (abstract no. 1592).

Cedars-Sinai Med. Ctr., Div. of Pediatric Infectious Diseases, UCLA Sch. of Med., Los Angeles, CA.

LPS-mediated immune responses, including activation of monocytes, macrophages, and endothelial cells (EC) play an important role in the pathogenesis of gram-negative sepsis and septic shock. We have previously shown that LPS stimulates phosphorylation and activation of several MAP kinases, including p38 MAPK, and induces NF-k B activation and IL-6 synthesis in EC. Recent studies have identified Toll-like receptors (TLRs) as a potential class of LPS receptors. We have recently shown that LPS shares the IL-1 receptor signaling molecules to activate NF-k B, most likely using TLRs, in endothelial cells and THP-1 cells (Zhang et al., JBC 1999: 274:7611). However, the exact role of p38 MAP kinase in IL-6 synthesis and the connection between p38 MAPK pathway with the NFk B activation remain unclear. In this study, HDMEC were transiently co-transfected (Fugen 6) with a dominant negative construct of p38 MAPK (DN p38; p38 TY * AF), reporter-promoter-luciferase constructs of either human IL-6 or NF-k B, and beta-gal contsruct. Cells were lysed and luciferase and beta-gal activities were measured to normalize for transfection efficiency. In triplicate experiments, overexpression of DNp38 construct inhibited (mean inhibition of 90%) both LPS-induced human IL-6 promoter, and NF-k B- luciferase activities. Treatment of HDMEC with the p38 MAP kinase inhibitor (SB203580) also decreased (mean inhibition of 50%) IL-6 promoter and NF-k B-luciferase activity. Taken together, our data suggest that p38 MAPK is required for LPS-induced IL-6 synthesis in endothelial cells. Furthermore, our findings suggest that the p38 MAPK pathway may be involved in LPS-induced transactivation of NF-k B in EC. Further work dissecting signaling events proximal and distal to p38 MAP kinase is under way in our laboratory.

Publication Types:
  • Meeting Abstracts
Keywords:
  • Animals
  • Endothelial Cells
  • Humans
  • Imidazoles
  • Interleukin-6
  • Lipopolysaccharides
  • Mitogen-Activated Protein Kinase 14
  • Mitogen-Activated Protein Kinases
  • Monocytes
  • Pyridines
  • SB 203580
  • Signal Transduction
  • Trans-Activation (Genetics)
  • genetics
  • immunology
  • p38 Mitogen-Activated Protein Kinases
Other ID:
  • GWAIDS0007940
UI: 102245437

From Meeting Abstracts




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