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(Received for publication, April 23, 1996, and in revised form, November 20, 1996)
From the Two populations of rat liver lysosomes can be
distinguished on the basis of their density. A major difference between
these populations is that one contains the heat shock cognate protein of 73 kDa (hsc73) within the lysosomal lumen. The lysosomal fraction containing hsc73 exhibits much higher efficiencies in the in
vitro uptake and degradation of glyceraldehyde-3-phosphate
dehydrogenase and ribonuclease A, two well established substrates of
the selective lysosomal pathway of intracellular protein degradation.
Preloading of the lysosomal population that is devoid of lumenal hsc73
with hsc73 isolated from cytosol activated the selective transport of
substrate proteins into these lysosomes. Furthermore, treatment of
animals with leupeptin, an inhibitor of lysosomal cathepsins, or
88 h of starvation also increased the amount of hsc73 within their
lysosomal lumen, and these in vivo treatments also
activated the selective transport of substrate proteins in
vitro. Thus, the hsc73 located within lysosomes appears to be
required for efficient uptake of cytosolic proteins by these
organelles. The difference in hsc73 content between the lysosomal
populations appears to be due to differences in their ability to take
up hsc73 combined with differences in the intralysosomal degradation
rates of hsc73. The increased stability of hsc73 in one population of lysosomes is primarily a consequence of this lysosomal population's more acidic pH.
Volume 272, Number 9,
Issue of February 28, 1997
pp. 5606-5615
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
Instituto de Investigaciones
Citológicas, 46010 Valencia, Spain and the
§ Department of Physiology, Tufts University School of
Medicine, Boston, Massachusetts 02111
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