Journal
BIOCHEMISTRY AND CELL BIOLOGY
Volume 99, Issue 5, Pages 645-654Publisher
CANADIAN SCIENCE PUBLISHING
DOI: 10.1139/bcb-2021-0004
Keywords
osteoarthritis; chondrocytes; S-allylcysteine; colchicine; toll-like receptor-4; redox signaling; inflammation; nuclear factor erythroid 2-related factor 2; oxidative stress
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Funding
- Scientific and Technological Research Council of Turkey (TUBITAK-SBAG) [315S012]
- EU-COST Action [CA16112]
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The study found that S-allylcysteine (SAC) and colchicine can modulate the function of human osteoarthritis chondrocytes (OAC) by inhibiting redox-sensitive inflammatory signaling pathways.
The discovery of new pharmacological agents is needed to control the progression of osteoarthritis (OA), characterized by joint cartilage damage. Human OA chondrocyte (OAC) cultures were either applied to S-allylcysteine (SAC), a sulfur-containing amino acid derivative, or colchicine, an ancient anti-inflammatory therapeutic, for 24 h. SAC or colchicine did not change viability at 1 nM-10 mu M but inhibited p-JNK/pan-JNK. While SAC seems to be more effective, both agents inhibited reactive oxygen species (ROS), 3-nitrotyrosine (3-NT), lipid hydroperoxides (LPO), advanced lipoxidation end-products (ALEs as 4-hydroxy-2-nonenal, HNE), advanced glycation end-products (AGEs), and increased glutathione peroxidase (GPx) and type-II-collagen (COL2). IL-1 beta, IL-6, and osteopontin (OPN) were more strongly inhibited by SAC than by colchicine. In contrast, TNF-alpha was inhibited only by SAC, and COX2 was only inhibited by colchicine. Casp-1/ICE, GM-CSF, receptor for advanced glycation end-products (RAGE), and toll-like receptors (TLR4) were inhibited by both agents, but bone morphogenetic protein 7 (BMP7) was partially inhibited by SAC and induced by colchicine. Nuclear factor erythroid 2-related factor 2 (Nrf2) was induced by SAC; in contrast, it was inhibited by colchicine. Although they exert opposite effects on TNF-alpha, COX2, BMP7, andNrf2, SAC and colchicine exhibit anti-osteoarthritic properties in OAC by modulating redox-sensitive inflammatory signaling.
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