Brefeldin A inhibits the targeting of cathepsin D and cathepsin H to lysosomes in rat hepatocytes

Kimimitsu Oda, Yukio Nishimura

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Effect of brefeldin A on the transport of lysosomal acid hydrolases (cathepsins D and H) was investigated in primary cultured rat hepatocytes. Both cathepsins were synthesized as proenzymes and progressively converted to mature enzymes in the control cells. However, BFA strongly inhibited the appearance of the mature enzymes in the cells in a dose dependent manner, suggesting that transport of newly synthesized lysosomal enzymes from the endoplasmic reticulum to lysosomes is blocked by the drug. The inhibitory effect by brefeldin A was reversible. Upon recovery from brefeldin A-intoxication, procathepsin D was effectively targeted into lysosomes, whereas a substantial amount of procathepsin H was found to be missorted, resulting in its secretion into the culture medium.

Original languageEnglish
Pages (from-to)220-225
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume163
Issue number1
DOIs
Publication statusPublished - Aug 30 1989

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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