Volume 36, Issue 11 pp. 1155-1171
Article
Free Access

Species Dependency of In Vitro Macrophage Activation by Bacterial Peptidoglycans

Shigeki Nagao

Shigeki Nagao

Department of Biochemistry, Shimane Medical University, Izumo, Shimane, 693 Japan

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Kiyoko S. Akagawa

Kiyoko S. Akagawa

Department of Cellular Immunology, National Institute of Health, Shinagawa-ku, Tokyo, 141 Japan

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Fumito Okada

Fumito Okada

Department of Biochemistry, Shimane Medical University, Izumo, Shimane, 693 Japan

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Yuji Harada

Yuji Harada

Department of Biochemistry, Shimane Medical University, Izumo, Shimane, 693 Japan

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Katsuro Yagawa

Katsuro Yagawa

Research Institute for Disease of Chest, Faculty of Medicine, Kyushu University, Fukuoka, Fukuoka, 812 Japan

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Keijiro Kato

Keijiro Kato

Department of Oral Microbiology, Okayama University Dental School, Okayama, Okayama, 700 Japan

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Yoshinori Tanigawa

Yoshinori Tanigawa

Department of Biochemistry, Shimane Medical University, Izumo, Shimane, 693 Japan

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First published: November 1992
Citations: 9

Abstract

The effect of various bacterial cell wall components on in vitro biological function of murine peritoneal exudate macrophages was evaluated. We examined four different parameters of metabolic activity and monokine secretion. Peritoneal exudate macrophages from rats and guinea pigs, all of the strains tested, were stimulated by whole bacterial cell wall preparations, purified bacterial cell wall peptidoglucans, its water-soluble peptidoglycan fragments, muramyl dipeptides and amphipathic substances. Murine peritoneal exudate macrophages were activated by amphipathic substances of gram-positive bacteria. However, macrophages from mice, irrespective of strains, were not stimulated in the in vitro assay systems by purified bacterial cell wall peptidoglycan, water-soluble bacterial peptidoglycan fragments or muramyl dipeptides. These results suggest that macrophage activation by bacterial peptidoglycan in vitro is animal species specific.

Abbreviations

  • MDP
  • muramyl dipeptide, specifically, N-acetylmuramyl-l-alanyl-l-isoglutamine
  • L18-MDP
  • 6-O-stearoyl muramyldipeptide
  • L30-MDP
  • 6-O-trecontanyl muramyldipeptide
  • B30-MDP
  • 6-O-[2-tetradecylhexadecanoyl]-muramyl dipeptide
  • BH48-MDP
  • 6-O-[3-hydroxy-2-dodecylhexacosenoyl]-muramyldipeptide
  • MDP-l-Lys(L18)
  • MurNAc-l-Ala-d-isoGln-l-Lys(L18), Nα(N-acetylmuramyl-l-alanyl-d-isoglutaminyl)--stearoyllysine
  • SEPS-M
  • Staphylococcus epidermidis peptidoglycan subunit-monomer
  • LPCM-A
  • bis-dissacharide-stempeptide dimer from Lactobacillus plantarum
  • GMP4
  • N-acetylglucosaminyl-β- (1-4) N-acetylmuramyl-l-alanyl-d-isoglutaminylmeso-2,6 diaminopimelic acid-d-alanine
  • MP4
  • N-acetylmuramyl-l-alanyl-d-isoglutaminyl-meso-2,6 diaminopimelic acid-d-alanine
  • GMP3
  • N-acetylglucosaminyl-β(1-4) N-acetylmuramyl-l-alanyl-d-isoglutaminyl-meso-2,6 diaminopimelic acid
  • MP3
  • N-acetylmuramyl-l-alanyl-d-isoglutaminylmeso-2,6-diaminopimelic acid
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