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J. Biol. Chem., Vol. 265, Issue 16, 8999-9005, Jun, 1990
GM Kindberg, O Gudmundsen and T Berg
Vanadate is a phosphate analogue that inhibits enzymes involved in
phosphate release and transfer reactions (Simons, T. J. B. (1979) Nature
281, 337-338). Since such reactions may play important roles in
endocytosis, we studied the effects of vanadate on various steps in
receptor-mediated endocytosis of asialoorosomucoid labeled with 125I-
tyramine-cellobiose (125I-TC-AOM). The labeled degradation products formed
from 125I-TC-AOM are trapped in the lysosomes and may therefore serve as
lysosomal markers in subcellular fractionation studies. Vanadate reduced
the amount of active surface asialoglycoprotein receptors approximately
70%, but had no effect on the rate of internalization and retroendocytosis
of ligand. The amount of surface asialoglycoprotein receptors can be
reduced by lowering the incubation temperature gradually from 37 to 15
degrees C (Weigel, P. H., and Oka, J. A. (1983) J. Biol. Chem. 258,
5089-5094); vanadate affected only the temperature--sensitive receptors.
Vanadate inhibited degradation of 125I-TC-AOM 70-80%. Degradation was much
more sensitive to vanadate than binding; half-maximal effects were seen at
approximately 1 mM vanadate for binding and approximately 0.1 mM vanadate
for degradation. By subcellular fractionation in sucrose and Nycodenz
gradients, it was shown that vanadate completely prevented the transfer of
125I-TC-AOM from endosomes to lysosomes. Therefore, the inhibition of
degradation by vanadate was indirect; in the presence of vanadate, ligand
did not gain access to the lysosomes. The limited degradation in the
presence of vanadate took place in a prelysosomal compartment. Vanadate did
not affect cell viability and ATP content.
The effect of vanadate on receptor-mediated endocytosis of asialoorosomucoid in rat liver parenchymal cells
Institute for Nutrition Research, University of Oslo, Norway.
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