Role of lysosomes in protein turnover: catch-up proteolysis after release from NH4Cl inhibition

Journal of Cellular Physiology
J S Amenta, S C Brocher

Abstract

Cultured rat embryo fibroblasts, when placed in media with 10% serum containing 20 mM NH4Cl, show an inhibition of protein degradation and, concurrently, an accumulation of numerous, large vacuoles, partially filled with cellular debris. Cells placed in a serum-free media exhibit an enhanced degradation of cell protein, which is also inhibited by NH4Cl. When these cells are removed from media containing NH4Cl and placed in fresh media, the material accumulated in these vacuoles is rapidly and quantitatively released to the media in both an acid-soluble and acid-insoluble from. NH4Cl inhibits rapidly and specifically the lysosomal proteolytic mechanism, and is without effect on the basal turnover mechanism. The lysosomal proteolytic mechanism accounts for approximately 25% of protein turnover, and, at least in low density cultures, can be stimulated to levels which account for more than half of the protein turnover in the cell. The major pathway for the degradation of fast turnover proteins appears to be separate from lysosomal mechanism.

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Citations

Oct 19, 2006·The Journal of Biological Chemistry·Weijie LiJohn T Seykora
Jan 1, 1989·Progress in Histochemistry and Cytochemistry·G Rappay
Dec 3, 2008·The European Journal of Neuroscience·Shengchun LiuWeihong Song
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Mar 31, 1986·FEBS Letters·R J Mayer, F Doherty
Mar 16, 1981·Life Sciences·J S Amenta, S C Brocher
Jul 30, 1984·Biochimica Et Biophysica Acta·B Grinde
Mar 11, 1988·Biochimica Et Biophysica Acta·D A Leonard, H W Chen
Nov 24, 1982·Biochimica Et Biophysica Acta·P J BatesD R Van der Westhuyzen
Sep 1, 1984·Archives of Biochemistry and Biophysics·J F Hare, M Huston

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