• yeast hydrolysate;
  • arthritis;
  • rabbit chondrocyte;
  • type II collagen;
  • interleukin-1β;
  • metalloproteases-13

Type II collagen (COL II) is one of the primary components of hyaline cartilage and plays a key role in maintaining chondrocyte function. COL II is the principal target of destruction, and matrix metalloproteases (MMPs) have a major role in arthritis. In the present study, we investigated the chondroctye protection effects of specific fraction of yeast hydrolysate ((10–30 kDa molecular weight peptides). The mRNA expression of COL II was significantly increased in the YH-treated group compared to the control at concentrations above 50 µg/ml, respectively. The 200 µg/ml YH-treated group (3.43 ± 0.23 µg/ml) showed significantly reduced glycosaminoglycan (GAG) degradation relative to that in the interleukin-1β (IL-1β)-treated control group (4.72 ± 0.05 µg/ml). In the YH-treated group, MMP-13 level was significantly decreased in a dose-dependent manner compared to the IL-1β-treated group without YH treatment. However, MMP-1 and MMP-3 level were not different from that of control. Under the same conditions, we also examined mRNA levels of COL II. The mRNA expression of COL II was significantly higher in the YH-treated group than in the IL-1β-treated control group at concentrations above 100 µg/ml. In conclusion, YH stimulated COL II synthesis and significantly inhibited MMP-13 and GAG degradation caused by IL-1β treatment. Copyright © 2012 John Wiley & Sons, Ltd.