Catabolic effects of muramyl dipeptide on rabbit chondrocytes

Tetsuro Ikebe, Hideaki Iribe, Masato Hirata, Fumi Yanaga, Toshitaka Koga

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

Muramyl dipeptide, an essential structure for the diverse biologic activities of bacterial cell wall peptidoglycan, inhibited the synthesis of glycosaminoglycan/proteoglycan in cultured rabbit costal chondrocytes in a dose‐dependent manner. Muramyl dipeptide, as well as lipopolysaccharide and interleukin‐1α, also enhanced the release of 35S‐sulfate—prelabeled glycosaminoglycan/proteoglycan from the cell layer, which seems to reflect, at least partially, the increasing degradation of glycosaminoglycan/proteoglycan. Five synthetic analogs of muramyl dipeptide known to be adjuvant active or adjuvant inactive were tested for their potential to inhibit synthesis of glycosaminoglycan/proteoglycan and to enhance the release of glycosaminoglycan/proteoglycan in chondrocytes. The structural dependence of these synthetic analogs on chondrocytes was found to parallel that of immunoadjuvant activity. These results suggest that muramyl dipeptide is a potent mediator of catabolism in chondrocytes.

Original languageEnglish
Pages (from-to)1801-1806
Number of pages6
JournalArthritis and Rheumatism
Volume33
Issue number12
DOIs
Publication statusPublished - 1990

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Rheumatology
  • Immunology
  • Pharmacology (medical)

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