Bestatin inhibits covalent coupling of [3H]LTA4 to human leukocyte LTA4 hydrolase

FEBS Lett. 1992 Feb 3;297(1-2):139-42. doi: 10.1016/0014-5793(92)80345-h.

Abstract

The covalent coupling of [3H]LTA4 to human leukocyte LTA4 hydrolase is inhibited in a concentration-dependent fashion by pre-incubation with bestatin. This inhibition correlated with the concentration-dependent inhibition by bestatin of LTB4 and LTB5 synthesis by LTA4 hydrolase. Epibestatin, a diastereomer of bestatin, neither inhibited LTB4 or LTB5 production by LTA4 hydrolase nor prevented the covalent coupling of [3H]LTA4 to the enzyme. In contrast, captopril inhibited both LTB4 synthesis by LTA4 hydrolase and covalent coupling of [3H]LTA4 to the enzyme.

MeSH terms

  • Captopril / pharmacology
  • Chromatography, Gel
  • Epoxide Hydrolases / metabolism*
  • Humans
  • Leucine / analogs & derivatives*
  • Leucine / pharmacology
  • Leukocytes / enzymology*
  • Leukotriene A4
  • Leukotriene Antagonists
  • Leukotriene B4 / antagonists & inhibitors
  • Leukotriene B4 / metabolism
  • Leukotrienes / metabolism*

Substances

  • Leukotriene A4
  • Leukotriene Antagonists
  • Leukotrienes
  • Leukotriene B4
  • Captopril
  • Epoxide Hydrolases
  • Leucine
  • ubenimex
  • leukotriene A4 hydrolase