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J. Biol. Chem., Vol. 269, Issue 5, 3846-3851, Feb, 1994
Y Zhu and GE Conner
To study the mechanism involved in mannose-6-phosphate (Man-6-P)
independent lysosomal proenzyme membrane association, we used a reversible
cross-linker to probe radiolabeled human HepG2 cells permeabilized with
saponin in the presence of Man-6-P. After immunoprecipitation of the
extracted and cross-linked cells with anti- cathepsin D antibody, followed
by complete reduction of the immunoprecipitates and SDS-polyacrylamide gel
electrophoresis analysis, we found that procathepsin D was specifically and
transiently associated, independent of Man-6-P, with two co-synthesized
glycoproteins having molecular masses of 68 and 72 kDa. Pulse-chase and
cell fractionation experiments showed that the Man-6-P independent
association of procathepsin D with the 68-kDa protein started in the rough
endoplasmic reticulum, continued in the Golgi, but had no association with
either membrane. The Man-6-P independent association of procathepsin D with
the 72-kDa protein and the membrane was found in compartments all the way
from the Golgi to the dense lysosome, where processing of procathepsin D is
believed to occur and where procathepsin D dissociated from the 72-kDa
protein and the membrane. Endo H digestion of the 72-kDa protein showed
that this protein was partially resistant to Endo H, suggesting that
membrane association of the procathepsin D-72-kDa protein complex probably
began in a late Golgi compartment. Endo F digestion of the proteins showed
both have the same molecular mass around 58 kDa. Using antiserum against
human saposin C, we identified the two glycoproteins as forms of prosaposin
with different glycosylation. The transient, Man-6-P independent, membrane
association of the procathepsin D-prosaposin complex and the presence of
this complex in heavy lysosomes indicated that the proteins were
transported to the lysosome as a complex. The association of two lysosomal
proteins in the endoplasmic reticulum early after synthesis suggested that
preassembly of some lysosomal components occurs before the earliest
previously identified steps in the sorting pathway.
Intermolecular association of lysosomal protein precursors during biosynthesis
Department of Cell Biology and Anatomy, University of Miami School of Medicine, Florida 33101.
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