Anticoagulant and anti-inflammatory effects of a degraded sulfate glycosaminoglycan from swimming bladder.

Low molecular weight sulfate glycosaminoglycan has attracted more attention recently for its great bioactivity. In the present study, a degraded sulfate glycosaminoglycan (named D-SBSG) was prepared from swimming bladder by enzymatic depolymerization, the structure characteristics of D-SBSG and its effects on blood coagulation and inflammation in vitro was investigated. HPGPC analysis showed that the molecular weight (Mw) of SBSG was 115.84 kDa, while the Mw of D-SBSG was 4.96 kDa. The bioactivities had arose dramatic differences, though its main molecule structure had little change after enzymatic degradation. Compared with heparin sodium, relatively milder anticoagulant activity in vitro, which were positively associated with molecular weight, were found in SBSG and D-SBSG. In contrast, the results of anti-inflammatory assays indicated that D-SBSG with the lower molecular weight possessed higher bioactivity than SBSG. Additionally, the D-SBSG inhibited the LPS-induced inflammatory in RAW264.7 macrophages by down-regulation of inflammatory mediators, both of NF-κB (including p65) and MAPK (including p38) signaling pathways to exert its anti-inflammatory function. These results indicated that enzymolysis is a viable strategy for degradation of sulfate glycosaminoglycan, and D-SBSG could be a promising ingredient for inflammation management.