Inhibitory activity of sulphoglycolipid derivatives towards pancreatic trypsin

H. Suzuki, M. Ito, T. Kimura, Y. Iwamori, M. Iwamori

研究成果: ジャーナルへの寄稿学術誌査読

10 被引用数 (Scopus)

抄録

Amphipathic sulpholipids have been shown to inhibit pancreatic serine proteases due to their detergent-like properties. To evaluate the structural requirement for this inhibitory activity, we examined the effects of various derivatives of sulphoglycolipids, some of which were prepared by deacylation with sphingolipid ceramide N-deacylase, followed by acylation with acyl chloride, on the activity of pancreatic trypsin. Both deacylated sulphatides and seminolipids exhibited inhibitory activity towards trypsin without any requirement for solubilisation and preincubation. On the other hand, stronger inhibition was observed for acylated sulphatides than for deacylated ones, but increasing the chain length of the fatty acid moiety resulted in the need for a solubilisation agent and preincubation in order to achieve maximal inhibitory activity. The structural isomers of sulphoglycolipids, such as I 6SO 3-GalCer, and phytosphingosine- and diglyceride-containing sulphoglycolipids, showed similar inhibitory activity, indicating the involvement of sulphate and hydrophobic groups, irrespective of the fine structure, in the inhibition. Among the sulphoglycolipids examined, II 3SO 3-LacCer was found to exhibit the highest inhibitory activity.

本文言語英語
ページ(範囲)787-793
ページ数7
ジャーナルGlycoconjugate Journal
17
11
DOI
出版ステータス出版済み - 2000

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学

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