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J. Biol. Chem., Vol. 266, Issue 19, 12131-12134, 07, 1991
KB Clairmont and MP Czech
The presence of a soluble, truncated form of the IGF-II/Man-6-P receptor in
serum has suggested that cleavage from the cell surface may be an initial
step in the degradation of this protein (MacDonald, R. G., Tepper, M. A.,
Clairmont, K. B., Perregaux, S. B., and Czech, M. P. (1989) J. Biol. Chem.
264, 3256-3261). In order to test this hypothesis, we pulse-labeled
cultured BRL-3A rat liver cells with [35S]methionine and [35S]cysteine and
measured the fate of labeled receptor at various times after incubation
with unlabeled amino acids. It was found that the appearance of labeled
IGF-II/Man-6-P receptor in the medium accounts quantitatively for the loss
of labeled receptor from the BRL-3A cells. In similar experiments with
Chinese hamster ovary cells, L6 rat myoblasts, and chick embryo
fibroblasts, labeled receptor from the cell membranes decreases with a time
course corresponding to the appearance of soluble receptor in the medium.
The release of labeled receptor into the medium can be blocked by the
addition of the protease inhibitors aprotinin, chymostatin, or
phenylmethylsulfonyl fluoride, but not antipain, leupeptin, and
benzamidine. The results are consistent with the hypothesis that the
degradation and loss of cellular IGF-II/Man-6-P receptors occurs by a
nonlysosomal mechanism involving their proteolysis and removal into the
extracellular fluid.
Extracellular release as the major degradative pathway of the insulin- like growth factor II/mannose 6-phosphate receptor
Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester 01605.
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