Neutral oligomannosides possessing one GlcNAc (OS-Gn1) and two GlcNAc (Os-Gn2) at the reducing end have been reported to be released during the N-glycosylation process in various biological models. To investigate which enzyme is responsible for OS-Gn1 formation, we used the Madin-Darby bovine kidney (MDBK) cell line which exhibits neither lysosomal chitobiase nor endoglucosaminidase activities. However, these cells produced OS-Gn1 and we showed that a neutral chitobiase is responsible for the transformation of OS-Gn2 into OS-Gn1. Using streptolysin O-permeabilized MDBK cells, we demonstrated that this neutral chitobiase activity is located in the cytosolic compartment and is active on oligomannoside species released during the N-glycosylation process.
Occurrence of a cytosolic neutral chitobiase activity involved in oligomannoside degradation: a study with Madin-Darby bovine kidney (MDBK) cells
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René CACAN, Catherine DENGREMONT, Odette LABIAU, Daniel KMIÉCIK, Anne-Marie MIR, André VERBERT; Occurrence of a cytosolic neutral chitobiase activity involved in oligomannoside degradation: a study with Madin-Darby bovine kidney (MDBK) cells. Biochem J 15 January 1996; 313 (2): 597–602. doi: https://doi.org/10.1042/bj3130597
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