Nonlysosomal processing of cell-surface heparan sulfate proteoglycans. Studies of I-cells and NH4Cl-treated normal cells.
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DOI: 10.1016/S0021-9258(18)45172-1
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摘要: The metabolism of cell-associated proteoglycans, labeled in the glycosaminoglycan portion with 35SO2-4, was studied normal skin fibroblasts (SL66 cells), NH4Cl-treated SL66 fibroblasts, and I-cells derived from patients mucolipidosis II. Kinetic data label-chase experiments gel filtration analysis molecular weight distribution radiolabeled glycosaminoglycans indicated that (a) internalize cell surface (b) remove chains proteoglycan core proteins, (c) degrade heparan sulfate via an endoglycosidic activity. These processes occur rates comparable to those fibroblasts. are consistent hypothesis cell-surface proteoglycans separated protein cores a nonlysosomal compartment prior transport these lysosomes for degradation. observations also raise possibility this early step separation may serve regulate levels glycosaminoglycan-free observed various cells.
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