The protective effect of sinapic acid in osteoarthritis: In vitro and in vivo studies

• Published in: Journal of cellular and molecular medicine Vol. 23; no. 3; pp. 1940 - 1950
• Main Authors: Li, Xiaobin, Lin, Jian, Ding, Xiaoxia, Xuan, Jiangwei, Hu, Zhichao, Wu, Dengying, Zhu, Xingyu, Feng, Zhenhua, Ni, Wenfei, Wu, Aimin
• Format: Journal Article
• Language: English
• Published: England John Wiley & Sons, Inc 01.03.2019; John Wiley and Sons Inc
• Subjects: ADAM protein; Aggrecan; Animal models; Animals; Arthritis; Cells, Cultured; Chondrocytes; Chondrocytes - drug effects; Chondrocytes - metabolism; Coumaric Acids - pharmacology; Cyclooxygenase 2 - metabolism; Dinoprostone - metabolism; Female; Heme; Heme Oxygenase-1 - metabolism; Humans; IL‐1β; Inflammation; Interleukin-1beta - metabolism; Interleukin-6 - metabolism; Male; Matrix metalloproteinase; Matrix Metalloproteinase 13 - metabolism; Mice; Mice, Inbred C57BL; Middle Aged; NF-kappa B - metabolism; NF‐κB; Nitric oxide; Nitric Oxide - metabolism; Nitric Oxide Synthase Type II - metabolism; Nitric-oxide synthase; Nrf2; Original; Osteoarthritis; Osteoarthritis - drug therapy; Osteoarthritis - metabolism; Oxygenase; Prostaglandin E2; Prostaglandin endoperoxide synthase; Protective Agents - pharmacology; Sinapic acid; Thrombospondin; Tumor necrosis factor; Tumor Necrosis Factor-alpha - metabolism; Tumor necrosis factor-TNF; Tumors; NF-κB; chondrocytes; IL-1β; Nrf2; inflammation; sinapic acid
• ISSN: 1582-1838; 1582-4934; 1582-4934
• DOI: 10.1111/jcmm.14096

The anti‐inflammatory effect of sinapic acid (SA) has been reported in several studies. However, whether SA has the same effect on osteoarthritis (OA) has yet to be clearly elucidated. We designed a series of in vitro and in vivo procedures to verify the above conjecture. Compared with controls, SA‐pretreated human chondrocytes showed lower levels of interleukin (IL)‐1β‐induced IL‐6, prostaglandin E2 (PGE2), nitric oxide (NO) and tumour necrosis factor‐α (TNF‐α) in vitro. Meanwhile, SA could also reverse the degradation of type II collage and aggrecan, as well as the overproduction of matrix metalloproteinase‐9 (MMP‐9) and matrix metalloproteinase‐13 (MMP‐13), inducible nitric oxide synthase (iNOS), cyclooxygenase (COX)‐2 and a disintegrin and metalloproteinase thrombospondin motifs (ADAMTS)‐5. Furthermore, activation of nuclear factor κB (NF‐κB), which was induced by IL‐1β, was also inhibited by SA through the pathway of nuclear factor‐erythroid 2‐related factor‐2 (Nrf2)/heme oxygenase 1. In vivo, SA could delay the progress of mice OA models. We propose that SA may be applied as a potential therapeutic drug in OA treatment.