The actin cytoskeleton: An essential component for enhanced TNFα production by adherent monocytes

Matthew R. Rosengart, Saman Arbabi, Gregory J. Bauer, Iris Garcia, Sandra Jelacic, Ronald V. Maier

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Monocyte adherence induces the formation of focal adhesions, the interaction sites of intracellular signaling molecules and cytoskeletal proteins such as actin. We previously demonstrated that adherence potentiates human monocyte LPS-induced TNFα production. Hence, we hypothesized that the actin cytoskeleton is integral to adherence-induced priming for enhanced LPS-induced TNFα production. In contrast to nonadherent cells, LPS induced significant transcription of TNFα mRNA and production of TNFα in adherent monocytes. Disrupting the actin cytoskeleton with cytochalasin D (CD) in adherent monocytes inhibited LPS-induced TNFα production by 55%, thereby abrogating adherence-induced priming. Moreover, CD pretreatment abrogated adherence-induced activation of Pyk2, a major focal adhesion kinase, and ERK 1/2, a component of the mitogen-activated protein kinase (MAPK) signaling pathway, and it completely inhibited LPS-induced ERK 1/2 activation. However, CD treatment of nonadherent monocytes failed to inhibit cytokine production. In conclusion, the actin cytoskeleton is integral in the reprogramming of the monocyte for enhanced cytokine production and in maintaining this "primed" state.

Original languageEnglish
Pages (from-to)109-113
Number of pages5
JournalShock
Volume17
Issue number2
DOIs
StatePublished - Feb 2002

Keywords

  • Cytokine
  • Focal adhesions
  • Lipopolysaccharide
  • Microfilaments
  • Mitogen-activated protein kinase
  • Tyrosine kinase

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