Glucosidase II, an asparagine-linked oligosaccharide processing enzyme, is a resident glycoprotein of the endoplasmic reticulum. In kidney tubular cells, in contrast to previous findings on hepatocytes, we found by light and electron microscopy immunoreactivity for glucosidase II predominantly in post-Golgi apparatus structures. The majority of immunolabel was in endocytotic structures beneath the plasma membrane. Immunoprecipitation confirmed presence of the glucosidase II subunit in purified brush border preparations. Kidney glucosidase II contained species carrying endo H-sensitive, high mannose as well as endo H-resistant oligosaccharide chains. Some species of glucosidase II contained sialic acid. The sialylated species were enzymatically active. This study demonstrates than an enzyme presumed to be a resident of the endoplasmic reticulum may show alternative localizations in some cell types.
Article|
February 01 1990
Cell type-specific post-Golgi apparatus localization of a "resident" endoplasmic reticulum glycoprotein, glucosidase II.
D Brada,
D Brada
Interdepartmental Electron Microscopy, University of Basel, Switzerland.
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D Kerjaschki,
D Kerjaschki
Interdepartmental Electron Microscopy, University of Basel, Switzerland.
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J Roth
J Roth
Interdepartmental Electron Microscopy, University of Basel, Switzerland.
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D Brada
Interdepartmental Electron Microscopy, University of Basel, Switzerland.
D Kerjaschki
Interdepartmental Electron Microscopy, University of Basel, Switzerland.
J Roth
Interdepartmental Electron Microscopy, University of Basel, Switzerland.
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1990) 110 (2): 309–318.
Citation
D Brada, D Kerjaschki, J Roth; Cell type-specific post-Golgi apparatus localization of a "resident" endoplasmic reticulum glycoprotein, glucosidase II.. J Cell Biol 1 February 1990; 110 (2): 309–318. doi: https://doi.org/10.1083/jcb.110.2.309
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