Catabolic effects of muramyl dipeptide on rabbit chondrocytes
- Kyushu Univ., Fukuoka (Japan)
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-1 alpha, 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.
- OSTI ID:
- 5988041
- Journal Information:
- Arthritis and Rheumatism; (USA), Vol. 33:12; ISSN 0004-3591
- Country of Publication:
- United States
- Language:
- English
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CARTILAGE
CATABOLISM
GLYCOPROTEINS
BIOSYNTHESIS
PEPTIDES
BIOCHEMICAL REACTION KINETICS
CELL WALL
DOSE-RESPONSE RELATIONSHIPS
INHIBITION
LIPOPOLYSACCHARIDES
LYMPHOKINES
RABBITS
SECRETION
SULFUR 35
TRACER TECHNIQUES
ANIMAL TISSUES
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BODY
CARBOHYDRATES
CELL CONSTITUENTS
CONNECTIVE TISSUE
DAYS LIVING RADIOISOTOPES
EVEN-ODD NUCLEI
GROWTH FACTORS
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
LIGHT NUCLEI
LIPIDS
MAMMALS
METABOLISM
MITOGENS
NUCLEI
ORGANIC COMPOUNDS
POLYSACCHARIDES
PROTEINS
RADIOISOTOPES
REACTION KINETICS
SACCHARIDES
SULFUR ISOTOPES
SYNTHESIS
TISSUES
VERTEBRATES
550501* - Metabolism- Tracer Techniques