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식품 및 바이오신소재

The influences of peptide isolated from seahorse, an inhibitor of MMPs, iNOS and COX-2 expression, is mediated by MAPK/NF-κB activation

초록

영어

Currently, there have been considerable efforts to search for naturally occurring bioactive
substances for the amelioration of arthritis. Many substances derived from natural products
have been found to possess substantial bioactive properties. Seahorse, a telelost fish, has been
exhibited positive effects on multiple aspects. However, it’s not clear on arthritis. In the present
work, we have purified and charaterized a bioactive peptide from seahorse hydrolysis using
various enzymes. Among hydrolysates, pronase E derived hydrolysate exhibited the higest
alkaline phosphatase (ALP) activity which phenotype marker of differentiation on osteoblast
and chondrocyte, than those of other enzyme hydrolysates. Pronase E hydrolysate was
separated in diverse purification steps. Finally, the peptide having the ALP activity was isolated and its sequence was identified as LEDPFDKDDWDNWK (1,821 Da). We have shown that isolated peptide exhibits a significant induction of differentiation in osteoblastic MG-63 and chondrocytic SW-1353 cells for ALP activity, minerlaization and collagen synthesis. Our result indicates that peptide affects from early to later stages of differentiation in MG-63, SW-1353 cells. Moreover, we assessed peptide inhibition on 12-O-Tetradecanoylphorbol-13-acetate (TPA) which is a common form of phorbol ester, induced expression of MMPs (1, 3, and 13), iNOS, COX-2 in a concentration-dependent manner and inhibits the NO production on MG-63 and SW-1353 cells. To elucidate the mechanism responsible for the inhibitory effect of peptide, we examined the effect of peptide on TPA-induced MAPKs and NF-κB activation and determined that the isolated peptide treatment significantly reduced p38 kinase/NF-κB in MG-63 cells and MAP kinase/NF-κB in SW-1353 cells.

저자정보

  • Bo Mi RYU Department of Chemistry, Pukyong National University,
  • Zhong-Ji QIAN 1Marine Bioprocess Research Center, Pukyong National University
  • Se-Kwon KIM Department of Chemistry, Pukyong National University

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