Cacan R, Dengremont C, Labiau O, Kmiécik D, Mir A M, Verbert A
Laboratoire de Chimie Biologique, UMR 111 du C.N.R.S., Université des Sciences et Technologies de Lille, Villenuve d'Ascq, France.
Biochem J. 1996 Jan 15;313 ( Pt 2)(Pt 2):597-602. doi: 10.1042/bj3130597.
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.
据报道,在各种生物学模型的N-糖基化过程中,还原端带有一个N-乙酰葡糖胺(OS-Gn1)和两个N-乙酰葡糖胺(Os-Gn2)的中性低聚甘露糖会被释放出来。为了研究哪种酶负责OS-Gn1的形成,我们使用了既不具有溶酶体壳二糖酶活性也不具有内切葡糖胺酶活性的马德堡-达比牛肾(MDBK)细胞系。然而,这些细胞产生了OS-Gn1,并且我们表明一种中性壳二糖酶负责将OS-Gn2转化为OS-Gn1。使用经链球菌溶血素O通透处理的MDBK细胞,我们证明这种中性壳二糖酶活性位于胞质区室,并且对N-糖基化过程中释放的低聚甘露糖种类具有活性。