Analysis of big endothelin-1 digestion by cathepsin D

Tatsuya Sawamura, Osamu Shinmi, Naoya Kishi, Yoshiki Sugita, Masashi Yanagisawa, Katsutoshi Goto, Tomoh Masaki, Sadao Kimura

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


Digestion of big endothelin(ET)-1 by cathepsin D, which is the only substantially identified protease showing ET converting enzyme activity, was characterized. Increased doses of cathepsin D showed decrease of immunoreactive (ir-) ET produced from big ET-1. Time course of big ET-1 conversion showed marked increase of ir-ET in a relatively short period, but further incubation resulted in the decrease of ir-ET. Incubation at various pHs with different doses of cathepsin D revealed that low doses of cathepsin D yielded the maximum production of ir-ET at pH 3.5 - 4.0, but higher doses of cathepsin D showed a bimodal curve of ir-ET production, which may be due to degradation of ir-ET. HPLC analysis revealed that cathepsin D cleaves Asn18-Ile19 bond in addition to Trp21-Val22 bond of big ET-1. These data suggests cathepsin D is not a physiological endothelin converting enzyme.

Original languageEnglish (US)
Pages (from-to)883-889
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Oct 30 1990

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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