Retention of membrane proteins by the endoplasmic reticulum

Retention of membrane proteins by the endoplasmic reticulum

We have used a monoclonal antibody specific for a hydrocarbon-induced cytochrome P450 to localize, by electron microscopy, the epitope- specific cytochrome P450. The cytochrome was found in the rough and smooth endoplasmic reticulum (ER) and the nuclear envelope of hepatocytes. Significant quantitie...

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Format: Online
Language:English
Published: The Rockefeller University Press 1985
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113977/
id pubmed-2113977
recordtype oai_dc
spelling pubmed-21139772008-05-01 Retention of membrane proteins by the endoplasmic reticulum Articles We have used a monoclonal antibody specific for a hydrocarbon-induced cytochrome P450 to localize, by electron microscopy, the epitope- specific cytochrome P450. The cytochrome was found in the rough and smooth endoplasmic reticulum (ER) and the nuclear envelope of hepatocytes. Significant quantities of cytochrome P450 were not found in Golgi stacks. We also could not find any evidence of Golgi- associated processing of the Asn-linked oligosaccharide chains of two well-characterized ER membrane glycoprotein enzymes (glucosidase II and hexose-6-phosphate dehydrogenase), or of the oligosaccharides attached to the bulk of the glycoproteins of the ER membrane. We conclude that these ER membrane proteins are efficiently retained during a process of highly selective export from this organelle. The Rockefeller University Press 1985-11-01 /pmc/articles/PMC2113977/ /pubmed/3932365 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/).
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
title Retention of membrane proteins by the endoplasmic reticulum
spellingShingle Retention of membrane proteins by the endoplasmic reticulum
title_short Retention of membrane proteins by the endoplasmic reticulum
title_full Retention of membrane proteins by the endoplasmic reticulum
title_fullStr Retention of membrane proteins by the endoplasmic reticulum
title_full_unstemmed Retention of membrane proteins by the endoplasmic reticulum
title_sort retention of membrane proteins by the endoplasmic reticulum
description We have used a monoclonal antibody specific for a hydrocarbon-induced cytochrome P450 to localize, by electron microscopy, the epitope- specific cytochrome P450. The cytochrome was found in the rough and smooth endoplasmic reticulum (ER) and the nuclear envelope of hepatocytes. Significant quantities of cytochrome P450 were not found in Golgi stacks. We also could not find any evidence of Golgi- associated processing of the Asn-linked oligosaccharide chains of two well-characterized ER membrane glycoprotein enzymes (glucosidase II and hexose-6-phosphate dehydrogenase), or of the oligosaccharides attached to the bulk of the glycoproteins of the ER membrane. We conclude that these ER membrane proteins are efficiently retained during a process of highly selective export from this organelle.
publisher The Rockefeller University Press
publishDate 1985
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113977/
_version_ 1611412953375965184

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