Skip to main content

Main menu

  • Home
  • About the Journal
    • General Information
    • Scope
    • Editorial Board
    • Impact & Metrics
    • Benefits of Publishing
    • Advertising/Sponsorship
    • About the Biochemical Society
  • Current Issue
  • For Authors
    • Submit Your Paper
    • Submission Guidelines
    • Editorial Policy
    • Open Access Policy
    • Rights and Permissions
    • Biochemical Society Member Benefits
  • For Librarians
    • Subscriptions and Pricing
    • Check Your Usage
    • Terms and Conditions
      • Biochemical Journal- Terms and Conditions of Usage
    • Open Access Policy
    • FAQs for Librarians
    • Register for Free Trial
  • For Readers
    • Subscribe
    • Rights and Permissions
    • Biochemical Society Member Benefits
    • Journal Access for Biochemical Society Members
    • Request a Free Trial
  • Collections
    • Article Collections
    • Classic Articles
  • Help
    • Technical Support
    • Contact Us
  • Other Publications
    • NEW: Emerging Topics in Life Sciences
    • NEW: Neuronal Signaling
    • Clinical Science
    • Biochemical Journal
    • Biochemical Society Transactions
    • Bioscience Reports
    • Essays in Biochemistry
    • Biochemical Society Symposia
    • Cell Signalling Biology
    • Glossary of Biochemistry and Molecular Biology
    • The Biochemist
    • Biochemical Society

User menu

  • Log-in
  • Subscribe
  • Contact Us

Search

  • Advanced search
  • Other Publications
    • NEW: Emerging Topics in Life Sciences
    • NEW: Neuronal Signaling
    • Clinical Science
    • Biochemical Journal
    • Biochemical Society Transactions
    • Bioscience Reports
    • Essays in Biochemistry
    • Biochemical Society Symposia
    • Cell Signalling Biology
    • Glossary of Biochemistry and Molecular Biology
    • The Biochemist
    • Biochemical Society

Log-in

Sign-up for alerts  
  • My Cart
Biochemical Journal
Browse Archive
Advanced Search
  • Home
  • About the Journal
    • General Information
    • Scope
    • Editorial Board
    • Impact & Metrics
    • Benefits of Publishing
    • Advertising/Sponsorship
    • About the Biochemical Society
  • Current Issue
  • For Authors
    • Submit Your Paper
    • Submission Guidelines
    • Editorial Policy
    • Open Access Policy
    • Rights and Permissions
    • Biochemical Society Member Benefits
  • For Librarians
    • Subscriptions and Pricing
    • Check Your Usage
    • Terms and Conditions
    • Open Access Policy
    • FAQs for Librarians
    • Register for Free Trial
  • For Readers
    • Subscribe
    • Rights and Permissions
    • Biochemical Society Member Benefits
    • Journal Access for Biochemical Society Members
    • Request a Free Trial
  • Collections
    • Article Collections
    • Classic Articles
  • Help
    • Technical Support
    • Contact Us

Research article

Glucose persistence on high-mannose oligosaccharides selectively inhibits the macroautophagic sequestration of N-linked glycoproteins

Eric OGIER-DENIS, Chantal BAUVY, Françoise CLUZEAUD, Alain VANDEWALLE, Patrice CODOGNO
Biochemical Journal Feb 01, 2000, 345 (3) 459-466; DOI: 10.1042/bj3450459
Eric OGIER-DENIS
Institut National de la Santé et de la Recherche Médicale (INSERM) U504 Glycobiologie et Signalisation Cellulaire, 16 Avenue Paul-Vaillant-Couturier, 94807 Villejuif Cedex, France
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • View author's works on this site
Chantal BAUVY
Institut National de la Santé et de la Recherche Médicale (INSERM) U504 Glycobiologie et Signalisation Cellulaire, 16 Avenue Paul-Vaillant-Couturier, 94807 Villejuif Cedex, France
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • View author's works on this site
Françoise CLUZEAUD
INSERM U478 Hormones Corticostéroïdes et Protéines de Transport Ionique dans les Cellules Epithéliales, Faculté de Médecine Xavier Bichat, BP416, 75870 Paris Cedex 18, France
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • View author's works on this site
Alain VANDEWALLE
INSERM U478 Hormones Corticostéroïdes et Protéines de Transport Ionique dans les Cellules Epithéliales, Faculté de Médecine Xavier Bichat, BP416, 75870 Paris Cedex 18, France
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • View author's works on this site
Patrice CODOGNO
Institut National de la Santé et de la Recherche Médicale (INSERM) U504 Glycobiologie et Signalisation Cellulaire, 16 Avenue Paul-Vaillant-Couturier, 94807 Villejuif Cedex, France
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • View author's works on this site
  • Article
  • Info & Metrics
  • PDF
Loading

Abstract

The macroautophagic-lysosomal pathway is a bulk degradative process for cytosolic proteins and organelles including the endoplasmic reticulum (ER). We have previously shown that the human colonic carcinoma HT-29 cell population is characterized by a high rate of autophagic degradation of N-linked glycoproteins substituted with ER-type glycans. In the present work we demonstrate that glucosidase inhibitors [castanospermine (CST) and deoxynojirimycin] have a stabilizing effect on newly synthesized glucosylated N-linked glycoproteins and impaired their lysosomal delivery as shown by subcellular fractionation on Percoll gradients. The inhibition of macroautophagy was restricted to N-linked glycoproteins because macroautophagic parameters such as the rate of sequestration of cytosolic markers and the fractional volume occupied by autophagic vacuoles were not affected in CST-treated cells. The protection of glucosylated glycoproteins from autophagic sequestration was also observed in inhibitor-treated Chinese hamster ovary (CHO) cells and in Lec23 cells (a CHO mutant deficient in glucosidase I activity). The interaction of glucosylated glycoproteins with the ER chaperone binding protein (BiP) was prolonged in inhibitor-treated cells in comparison with untreated CHO cells. These results show that the removal of glucose from N-glycans of glycoproteins is a key event for their delivery to the autophagic pathway and that interaction with BiP could prevent or delay newly synthesized glucosylated N-linked glycoproteins from being sequestered by the autophagic pathway.

  • autophagy
  • castanospermine
  • endoplasmic reticulum
  • lysosome
  • HT-29 cells
  • The Biochemical Society, London © 2000
Previous ArticleNext Article
Back to top

 

 

February 2000

Volume: 345 Issue: 3

Biochemical Journal: 345 (3)
  • Table of Contents
  • Table of Contents (PDF)
  • Index by author
  • Front Matter (PDF)

Actions

Email

Thank you for your interest in spreading the word about Biochemical Journal.

NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address.

Enter multiple addresses on separate lines or separate them with commas.
Glucose persistence on high-mannose oligosaccharides selectively inhibits the macroautophagic sequestration of N-linked glycoproteins
(Your Name) has forwarded a page to you from Biochemical Journal
(Your Name) thought you would like to see this page from the Biochemical Journal web site.
Share
Glucose persistence on high-mannose oligosaccharides selectively inhibits the macroautophagic sequestration of N-linked glycoproteins
Eric OGIER-DENIS, Chantal BAUVY, Françoise CLUZEAUD, Alain VANDEWALLE, Patrice CODOGNO
Biochemical Journal Feb 2000, 345 (3) 459-466; DOI: 10.1042/bj3450459
del.icio.us logo Digg logo Reddit logo Technorati logo Twitter logo CiteULike logo Facebook logo Mendeley logo
Citation Tools
Glucose persistence on high-mannose oligosaccharides selectively inhibits the macroautophagic sequestration of N-linked glycoproteins
Eric OGIER-DENIS, Chantal BAUVY, Françoise CLUZEAUD, Alain VANDEWALLE, Patrice CODOGNO
Biochemical Journal Feb 2000, 345 (3) 459-466; DOI: 10.1042/bj3450459

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
Alerts

Please log in to add an alert for this article.

Request Permissions
Save to my folders

View Full PDF

 Open in Utopia Docs
  • Tweet Widget
  • Facebook Like

Jump To

  • Article
  • Info & Metrics
  • PDF

Keywords

autophagy
castanospermine
endoplasmic reticulum
lysosome
HT-29 cells

Related Articles

Cited By...

  • Portland Press Homepage
  • Publish With Us
  • Advertising
  • Technical Support
  • Biochemical Journal
  • Clinical Science
  • Essays in Biochemistry
  • Emerging Topics in Life Sciences
  • Biochemical Society Transactions
  • Neuronal Signaling
  • Bioscience Reports
  • Cell Signalling Biology
  • Biochemical Society Symposia

Portland Press Limited
Charles Darwin House
12 Roger Street
London WC1N 2JU
Tel: +44(0) 20 7685 2410
Fax: +44(0) 20 7685 2469
Email: editorial@portlandpress.com

The Biochemical Society