Association of the precursor of cathepsin D with coated membranes. Kinetics and carbohydrate processing.
Specific anti-chlathrin antibodies were used to isolate clathrin-coated membranes from homogenates of metabolically labelled fibroblasts. The isolated membranes were extracted with detergents and cathepsin D was isolated from the extracts. The 53-kDa precursor of cathepsin D was transiently associated with the coated membranes with a maximum approximately 60 min after synthesis. At maximum about 4.0% of the precursor was recovered with the coated membranes and the associated precursor contained complex oligosaccharides. The proportion of complex oligosaccharides in the coated membrane-associated precursor did not differ from that in the total precursor. These data support the view that coated membranes are involved in the transport of cathepsin D between trans Golgi and a prelysosomal organelle.
D001692:Biological Transport / Q000187:drug effects; D002402:Cathepsin D / Q000378:metabolism*; D002738:Chloroquine / Q000494:pharmacology; D002966:Clathrin / Q000378:metabolism; D003034:Coated Pits, Cell-Membrane / Q000378:metabolism* / Q000502:physiology; D011992:Endosomes / Q000378:metabolism*; D004792:Enzyme Precursors / Q000378:metabolism*; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008247:Lysosomes / Q000378:metabolism; D009113:Muramidase / Q000378:metabolism; D011319:Primaquine / Q000494:pharmacology; D012867:Skin / Q000378:metabolism
D002966:Clathrin; D004792:Enzyme Precursors; D002738:Chloroquine; D009113:Muramidase; D002402:Cathepsin D; D011319:Primaquine