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

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27 Scopus citations

Abstract

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
Volume172
Issue number2
DOIs
StatePublished - Oct 30 1990

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ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Sawamura, T., Shinmi, O., Kishi, N., Sugita, Y., Yanagisawa, M., Goto, K., Masaki, T., & Kimura, S. (1990). Analysis of big endothelin-1 digestion by cathepsin D. Biochemical and Biophysical Research Communications, 172(2), 883-889. https://doi.org/10.1016/0006-291X(90)90758-F