Perturbation of neuronal cobalamin transport by lysosomal enzyme inhibition
                    
                        
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                    چکیده
منابع مشابه
Perturbation of neuronal cobalamin transport by lysosomal enzyme inhibition
Cbl (cobalamin) utilization as an enzyme cofactor is dependent on its efficient transit through lysosomes to the cytosol and mitochondria. We have previously proposed that pathophysiological perturbations in lysosomal function may inhibit intracellular Cbl transport with consequences for down-stream metabolic pathways. In the current study, we used both HT1080 fibroblasts and SH-SY5Y neurons to...
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The major excreted protein (MEP) of transformed mouse fibroblasts is the lysosomal protease, cathepsin L. MEP is also secreted by untransformed mouse cells in response to growth factors and tumor promoters, and is thought to play a role in cell growth and transformation. To determine the relationship between MEP synthesis and MEP secretion, we have examined these events in PDGF-treated NIH 3T3 ...
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This work was presented in part at the meeting ofthe American Society of Human Genetics, San Diego, Calif., October 1977. Dr. Mellman and Dr. Willard are recipients of traineeships from the National Institutes of Health (T01-GM 02299). Dr. Mellman's present address is Laboratory of Cellular Physiology and Immunology, The Rockefeller University, New York 10021. Received for publication 18 May 19...
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Adsorptive pinocytosis of acid hydrolases by fibroblasts depends on phosphomannosyl recognition markers on the enzymes and high-affinity pinocytosis receptors on the cell surface. In this study, beta-glucuronidase binding to the cell surface of attached fibroblasts was found to be saturable and inhibitable by mannose-6-phosphate (Man-6-P). Dissociation of cell-bound beta-glucuronidase occurred ...
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ژورنال
عنوان ژورنال: Bioscience Reports
سال: 2014
ISSN: 0144-8463,1573-4935
DOI: 10.1042/bsr20130130