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Intracellular degradation of 125I-labelled asialo-glycoproteins in rat hepatocytes: effect of leupeptin on subcellular distribution of asialo-fetuin
Authors:T Berg  T Ose  L Ose  H Tolleshaug
Affiliation:1. Department of Economics, University of Ottawa, Canada;2. Graduate School of Public and International Affairs and Institute of the Environment, University of Ottawa, Canada;1. Department of Mechanical Engineering, Malnad College of Engineering, Hassan, Visvesvaraya Technological University,Belagavi, India;2. Department of Mechanical Engineering, Ramaiah Institute of Technology, Bengaluru, Visvesvaraya Technological University, Belagavi, India;3. Department of Mechanical and Process Engineering, The Sirindhorn International ThaiGerman Graduate School of Engineering (TGGS), King Mongkut''s University of Technology North Bangkok, Bangkok, Thailand;4. Department of Chemistry, Manipal Institute of Technology, Manipal Academy of Higher Education, Manipal, Karnataka, India;1. Department of Mechanics, Tianjin University, Tianjin 300354, China;2. Tianjin Key Laboratory of Nonlinear Dynamics and Control, Tianjin 300354, China;3. National Demonstration Center for Experimental Mechanics Education (Tianjin University), Tianjin 300354, China;4. School of Mechanical Engineering, Tianjin University, Tianjin 300072, China
Abstract:
  • 1.1. Isolated rat hepatocytes endocytose and degrade asialo-glycoproteins effectively.
  • 2.2. The degradation of asialo-glycoproteins takes place in the lysosomes and is effectively inhibited by the bacterial tripeptide leupeptin.
  • 3.3. Subcellular fractionation studies showed that leupeptin led to an accumulation of undegraded asialo-fetuin both in lysosomes and in a more buoyant particle (possibly an endosome).
  • 4.4. This observation suggests that the protease inhibitor leupeptin inhibits degradation of endocytosed asialo-fetuin both by inhibiting lysosomal proteases and by retarding fusion between endosomes and lysosomes.
Keywords:
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