EFFICIENT ROUTING OF GLUCOCEREBROSIDASE TO LYSOSOMES REQUIRES COMPLEX OLIGOSACCHARIDE CHAIN FORMATION
EFFICIENT ROUTING OF GLUCOCEREBROSIDASE TO LYSOSOMES REQUIRES COMPLEX OLIGOSACCHARIDE CHAIN FORMATION
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DOI:
10.1016/s0006-291x(86)80194-2
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发表时间:
1986-12-15
影响因子:
3.1
通讯作者:
SCHRAM, AW
中科院分区:
文献类型:
--
作者:
AERTS, JMFG;BRUL, S;SCHRAM, AW
The biosynthesis and intracellular transport of the membrane-associated lysosomal enzyme glucocerebrosidase was studied in the monoblast cell line U937. Addition to the cultures of the oligosaccharide trimming inhibitors swainsonine or deoxymannojirimycin led to an increased intracellular activity of glucocerebrosidase. This was due to prevention of the lysosomal degradation of the enzyme. When homogenates of control cells were fractionated on Percoll gradients glucocerebrosidase, like .beta.-hexosaminidase, was distributed in two peaks, one at low density and one at high density. When homogenates of cells cultured in the presence of oligosaccharide trimming inhibitors were fractionated .beta.-hexosaminidase was still distributed in two peaks but glucocerebrosidase was found mainly in low density fractions also containing galactosyltransferase activity. It is concluded that complex type oligosaccharide chain formation is required for efficient routing of glucocerebrosidase to the lysosomes in U937 cells.