Identification of a precursor form of cathepsin D in microsomal lumen: Characterization of enzymatic activation and proteolytic processing in vitro

Yukio Nishimura, Masahide Higaki, Keitaro Kato

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

A precursor form of cathepsin D with 45 kDa was demonstrated in the rat liver microsomal lumen by immunoblotting analysis. The microsomal fraction containing procathepsin D which passed through a pepstatin-Sepharose resin showed no appreciable activity of cathepsin D. The in vitro incubation of this fraction at pH 3.0 resulted in a gradual increase of proteolytic activity toward hemoglobin as substrate and also, the proteolytic conversion of procathepsin D to the mature form was concomitantly observed. The proteolytic processing step was sensitive to pepstatin. These results suggest that procathepsin D is inactive in the endoplasmic reticulum and may be converted to the active forms by autoproteolytic processing mechanism at acidic pH during biosynthesis.

Original languageEnglish
Pages (from-to)335-343
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume148
Issue number1
DOIs
Publication statusPublished - Oct 14 1987

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Cathepsin D
Chemical activation
Processing
Biosynthesis
Immunoblotting
Endoplasmic Reticulum
Liver
Sepharose
Rats
Hemoglobins
Resins
Substrates
procathepsin D
In Vitro Techniques
pepstatin

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Identification of a precursor form of cathepsin D in microsomal lumen : Characterization of enzymatic activation and proteolytic processing in vitro. / Nishimura, Yukio; Higaki, Masahide; Kato, Keitaro.

In: Biochemical and Biophysical Research Communications, Vol. 148, No. 1, 14.10.1987, p. 335-343.

Research output: Contribution to journalArticle

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