Occurrence of a cytosolic neutral chitobiase activity involved in oligomannoside degradation: a study with Madin-Darby bovine kidney (MDBK) cells.
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.
Cacan
R
R
Laboratoire de Chimie Biologique, UMR 111 du C.N.R.S., Université des Sciences et Technologies de Lille, Villenuve d'Ascq, France.
Dengremont
C
C
Labiau
O
O
Kmiécik
D
D
Mir
A M
AM
Verbert
A
A
D000118:Acetylglucosaminidase / Q000378:metabolism*; D000818:Animals; D016466:CHO Cells; D002417:Cattle; D002460:Cell Line; D006224:Cricetinae; D003600:Cytosol / Q000201:enzymology*; D006031:Glycosylation; D006868:Hydrolysis; D007668:Kidney / Q000166:cytology / Q000201:enzymology* / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism*; D013379:Substrate Specificity
D009844:Oligosaccharides; C028569:oligomannoside; D000118:Acetylglucosaminidase