Abstract
Recycling of a number of glycoproteins along the site of action of mannosidase I (the distal endoplasmic reticulum/cis-Golgi) was followed in several different cell lines. Treatment of cells with 1-deoxymannojirimycin (dMM) produced high mannose oligosaccharides at positions otherwise occupied by complex-type oligosaccharides in these glycoproteins. Conversion of high-mannose-type oligosaccharides to complex oligosaccharides of proteins initially synthesized in the presence of dMM was used as a marker for recycling of glycoproteins along the site of action of dMM. In contrast to findings reported by Snider and Rogers (Snider, M. D., and O. C. Rogers. 1986. J. Cell Biol. 103:265-275), removal of dMM did not result in reconversion of high-mannose oligosaccharides to complex-type sugars, even after prolonged periods of culture. We conclude that surface glycoproteins do not recycle through the cis-medial Golgi elements.
MeSH Terms
1-Deoxynojirimycin
Anti-Bacterial Agents/pharmacology
Carcinoma, Hepatocellular
Cell Line, Transformed
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum/enzymology,metabolism
Glucosamine/analogs & derivatives,pharmacology
Glycoproteins/metabolism
Golgi Apparatus/enzymology,metabolism
HLA Antigens
HLA-D Antigens
Humans
Immunoassay
Isoelectric Focusing
Leukemia, Erythroblastic, Acute
Liver Neoplasms
Mannosidases/antagonists & inhibitors
Neuraminidase/metabolism
Receptors, Transferrin/drug effects,metabolism
Transferrin/metabolism
Tumor Cells, Cultured
Chemicals
Anti-Bacterial Agents
Glycoproteins
HLA Antigens
HLA-D Antigens
Receptors, Transferrin
Transferrin
1-Deoxynojirimycin
Mannosidases
mannosyl-oligosaccharide 1,2-alpha-mannosidase
Neuraminidase
Glucosamine
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Neefjes J J
Netherlands Cancer Institute, Amsterdam.
Verkerk J M
Broxterman H J
van der Marel G A
van Boom J H
Ploegh H L
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