Lysosomal cysteine protease, cathepsin H, is targeted to lysosomes by the mannose 6-phosphate-independent system in rat hepatocytes

Yoshitaka Tanaka, Rie Tanaka, Masaru Himeno

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Abstract

The contribution of mannose 6-phosphate (Man 6-P)-dependent and - independent systems to lysosomal targeting of cathepsin H, a lysosomal cysteine protease, was investigated by metabolic labeling with [32P]phosphate and [35S]methionine/cysteine in primary cultures of rat hepatocytes. Metabolic labeling experiments with [32P]phosphate revealed that only the proform of cathepsin H acquired Man 6-P residues on its high mannose type oligosaccharide, and that most of the phosphorylated procathepsin H was secreted into the medium without having undergone significant intracellular dephosphorylation. Thus, acquisition of Man 6-P residues did not correlate with targeting of cathepsin H to lysosomes. Pulse- chase experiments with [35S]methionine/cysteine showed that only about 10% of the newly synthesized cathepsin H was secreted as a proform while the remainder was retained intracellularly in processed mature form. These results indicate that the majority of newly synthesized cathepsin H is targeted to lysosomes by a Man 6-P-independent mechanism, at least in rat hepatocytes.

Original languageEnglish
Pages (from-to)805-809
Number of pages5
JournalBiological and Pharmaceutical Bulletin
Volume23
Issue number7
DOIs
Publication statusPublished - Jul 2000

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All Science Journal Classification (ASJC) codes

  • Pharmacology
  • Pharmaceutical Science

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