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J. Biol. Chem., Vol. 265, Issue 31, 18780-18785, Nov, 1990
EP Feener, WC Shen and HJ Ryser
Whereas there is biological evidence that the reductive cleavage of
disulfide bonds is critical for the activation of endocytosed
macromolecules such as toxins, immunotoxins, and other drug carriers,
virtually nothing is known about the specifics of this cleavage. To study
this process, a model compound was synthesized in which a radioiodinated
tyramine was linked through a disulfide bond to an undegradable carrier,
poly(D-lysine), known to be efficiently endocytosed. Cultured Chinese
hamster ovary cells were pulse-labeled with this probe, and the disulfide
cleavage was measured as released acid-soluble radioactivity at different
times of chase. Pulse-labeled cells were also subjected to subcellular
fractionation to identify intracellular structures associated with
disulfide cleavage. Cleavage began without lag, amounted to about
approximately 7% of the initial cell-bound radioactivity in the first hour
and continued for more than 6 h. It was abolished in the presence of
N-ethylmaleimide. When sulfhydryl groups present at the cell surface were
blocked with cell- impermeant sulfhydryl reagent, the initial phase of
disulfide cleavage was inhibited, indicating that cleavage began at the
cell surface. A long-lasting intracellular phase of disulfide cleavage
began after about approximately 30 min of chase. Subcellular fractionation
and kinetic analysis indicated that neither lysosomes nor endosomes were
participating in that phase, leaving the Golgi apparatus as the most
probable site of endocytic disulfide cleavage.
Cleavage of disulfide bonds in endocytosed macromolecules. A processing not associated with lysosomes or endosomes
Department of Pathology, Boston University School of Medicine, Massachusetts 02118.
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