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Immunolocalization of the oligosaccharide trimming enzyme glucosidase II
We used immunoelectron microscopy to localize glucosidase II in pig hepatocytes. The enzyme trims the two inner alpha 1,3-linked glucoses from N-linked oligosaccharide precursor chains of glycoproteins. Immunoreactive enzyme was concentrated in rough (RER) and smooth (SER) endoplasmic reticulum but...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1986
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114248/ https://www.ncbi.nlm.nih.gov/pubmed/3519622 |
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collection | PubMed |
description | We used immunoelectron microscopy to localize glucosidase II in pig hepatocytes. The enzyme trims the two inner alpha 1,3-linked glucoses from N-linked oligosaccharide precursor chains of glycoproteins. Immunoreactive enzyme was concentrated in rough (RER) and smooth (SER) endoplasmic reticulum but not detectable in Golgi apparatus cisternae. Transitional elements of RER and smooth membraned structures close to Golgi apparatus cisternae contained labeling for glucosidase II. Specific labeling was also found in autophagosomes. These results indicate strongly that glucosidase II acts on glycoproteins before their transport to, and processing in Golgi apparatus cisternae, and suggest that an important transitional region for glucosidase II exists between RER and Golgi apparatus cisternae. Degradation in autophagolysosomes could form a normal catabolic pathway for glucosidase II. |
format | Text |
id | pubmed-2114248 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1986 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21142482008-05-01 Immunolocalization of the oligosaccharide trimming enzyme glucosidase II J Cell Biol Articles We used immunoelectron microscopy to localize glucosidase II in pig hepatocytes. The enzyme trims the two inner alpha 1,3-linked glucoses from N-linked oligosaccharide precursor chains of glycoproteins. Immunoreactive enzyme was concentrated in rough (RER) and smooth (SER) endoplasmic reticulum but not detectable in Golgi apparatus cisternae. Transitional elements of RER and smooth membraned structures close to Golgi apparatus cisternae contained labeling for glucosidase II. Specific labeling was also found in autophagosomes. These results indicate strongly that glucosidase II acts on glycoproteins before their transport to, and processing in Golgi apparatus cisternae, and suggest that an important transitional region for glucosidase II exists between RER and Golgi apparatus cisternae. Degradation in autophagolysosomes could form a normal catabolic pathway for glucosidase II. The Rockefeller University Press 1986-06-01 /pmc/articles/PMC2114248/ /pubmed/3519622 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Immunolocalization of the oligosaccharide trimming enzyme glucosidase II |
title | Immunolocalization of the oligosaccharide trimming enzyme glucosidase II |
title_full | Immunolocalization of the oligosaccharide trimming enzyme glucosidase II |
title_fullStr | Immunolocalization of the oligosaccharide trimming enzyme glucosidase II |
title_full_unstemmed | Immunolocalization of the oligosaccharide trimming enzyme glucosidase II |
title_short | Immunolocalization of the oligosaccharide trimming enzyme glucosidase II |
title_sort | immunolocalization of the oligosaccharide trimming enzyme glucosidase ii |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114248/ https://www.ncbi.nlm.nih.gov/pubmed/3519622 |