Peptidoglycan induces transcription and secretion of TNF-α and activation of lyn, extracellular signal-regulated kinase, and rsk signal transduction proteins in mouse macrophages

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Abstract

Insoluble peptidoglycan (PGN) from staphylococcal cell walls as well as soluble PGN (sPGN) secreted by staphylococci in the presence of β-lactam antibiotics induced TNF-α mRNA and secretion of bioactive TNF-α in the murine RAW264.7 macrophage cell line. PGN and sPGN also induced rapid and dose-dependent tyrosine phosphorylation of several cellular proteins, including lyn and mitogen-activated protein kinases (extracellular signal- regulated kinases; but not hck, fgr, or vav) and increased the activities of mitogen-activated protein and rsk kinases. These PGN- and sPGN-induced effects were qualitatively similar to the effects induced by ReLPS, but higher concentrations of PGN and sPGN than ReLPS were required. In contrast to the ReLPS-induced effects, the PGN-and sPGN induced effects were not inhibited by polymyxin B. All PGN-, sPGN, and ReLPS-induced effects were serum independent, since they were observed both in RAW264.7 cells grown and stimulated in the presence of serum and in the cells adapted to growth and stimulated in a serum- and albumin free medium. These results indicate that lyn, extracellular signal-regulated kinase, and rsk signal transduction molecules may be involved in macrophage activation by PGN and further support the idea that PGN and LPS may activate the cells through similar mechanisms.

Original languageEnglish
Pages (from-to)2620-2630
Number of pages11
JournalJournal of Immunology
Volume155
Issue number5
StatePublished - 1995

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Peptidoglycan
Extracellular Signal-Regulated MAP Kinases
Signal Transduction
Macrophages
Proteins
Mitogen-Activated Protein Kinases
Lactams
Polymyxin B
Macrophage Activation
Serum-Free Culture Media
Serum
Staphylococcus
Serum Albumin
Cell Wall
Tyrosine
Phosphorylation
Anti-Bacterial Agents
Cell Line
Messenger RNA

ASJC Scopus subject areas

  • Immunology

Cite this

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title = "Peptidoglycan induces transcription and secretion of TNF-α and activation of lyn, extracellular signal-regulated kinase, and rsk signal transduction proteins in mouse macrophages",
abstract = "Insoluble peptidoglycan (PGN) from staphylococcal cell walls as well as soluble PGN (sPGN) secreted by staphylococci in the presence of β-lactam antibiotics induced TNF-α mRNA and secretion of bioactive TNF-α in the murine RAW264.7 macrophage cell line. PGN and sPGN also induced rapid and dose-dependent tyrosine phosphorylation of several cellular proteins, including lyn and mitogen-activated protein kinases (extracellular signal- regulated kinases; but not hck, fgr, or vav) and increased the activities of mitogen-activated protein and rsk kinases. These PGN- and sPGN-induced effects were qualitatively similar to the effects induced by ReLPS, but higher concentrations of PGN and sPGN than ReLPS were required. In contrast to the ReLPS-induced effects, the PGN-and sPGN induced effects were not inhibited by polymyxin B. All PGN-, sPGN, and ReLPS-induced effects were serum independent, since they were observed both in RAW264.7 cells grown and stimulated in the presence of serum and in the cells adapted to growth and stimulated in a serum- and albumin free medium. These results indicate that lyn, extracellular signal-regulated kinase, and rsk signal transduction molecules may be involved in macrophage activation by PGN and further support the idea that PGN and LPS may activate the cells through similar mechanisms.",
author = "Dipika Gupta and Jin, {Y. P.} and Roman Dziarski",
year = "1995",
language = "English",
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pages = "2620--2630",
journal = "Journal of Immunology",
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T1 - Peptidoglycan induces transcription and secretion of TNF-α and activation of lyn, extracellular signal-regulated kinase, and rsk signal transduction proteins in mouse macrophages

AU - Gupta, Dipika

AU - Jin, Y. P.

AU - Dziarski, Roman

PY - 1995

Y1 - 1995

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AB - Insoluble peptidoglycan (PGN) from staphylococcal cell walls as well as soluble PGN (sPGN) secreted by staphylococci in the presence of β-lactam antibiotics induced TNF-α mRNA and secretion of bioactive TNF-α in the murine RAW264.7 macrophage cell line. PGN and sPGN also induced rapid and dose-dependent tyrosine phosphorylation of several cellular proteins, including lyn and mitogen-activated protein kinases (extracellular signal- regulated kinases; but not hck, fgr, or vav) and increased the activities of mitogen-activated protein and rsk kinases. These PGN- and sPGN-induced effects were qualitatively similar to the effects induced by ReLPS, but higher concentrations of PGN and sPGN than ReLPS were required. In contrast to the ReLPS-induced effects, the PGN-and sPGN induced effects were not inhibited by polymyxin B. All PGN-, sPGN, and ReLPS-induced effects were serum independent, since they were observed both in RAW264.7 cells grown and stimulated in the presence of serum and in the cells adapted to growth and stimulated in a serum- and albumin free medium. These results indicate that lyn, extracellular signal-regulated kinase, and rsk signal transduction molecules may be involved in macrophage activation by PGN and further support the idea that PGN and LPS may activate the cells through similar mechanisms.

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