Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Statistics
  • Help & Advice
University of Warwick

The Library

  • Login

An interaction between ricin and calreticulin that may have implications for toxin trafficking

Tools
- Tools
+ Tools

UNSPECIFIED (2001) An interaction between ricin and calreticulin that may have implications for toxin trafficking. JOURNAL OF BIOLOGICAL CHEMISTRY, 276 (10). pp. 7202-7208. ISSN 0021-9258

Full text not available from this repository.

Abstract

Here we demonstrate that ricin is able to interact with the molecular chaperone calreticulin both in vitro and in vivo. The interaction occurred with ricin holotoxin, but not with free:ricin A chain; and it was prevented in the presence of lactose, suggesting that it was mediated by the lectin activity of the ricin B chain. This lectin is galactose-specific, and metabolic labeling with [H-3]galactose or treating galactose oxidase-modified calreticulin with sodium [H-3]borohydride indicated that Vero cell calreticulin possesses a terminally galactosylated oligosaccharide. Brefeldin A treatment indicated that the intracellular interaction occurred initially in a post-Golgi stack compartment,:possibly the trans-Golgi network, whereas the reductive separation of ricin subunits occurred in an earlier part of the secretory pathway, most probably the endoplasmic reticulum (ER), Intoxicating Vero cells with ricin whose A chain had been modified to include either a tyrosine sulfation site or the sulfation site plus available N-glycosylation sites, in the presence of (Na2OSO4)-S-35, confirmed that calreticulin interacted with endocytosed ricin that had already undergone retrograde transport to both the Golgi and the ER, Although we cannot exclude the possibility that the interaction between ricin and calreticulin is an indirect one, the data presented are consistent with the idea that calreticulin may function as a recycling carrier for retrograde transport of ricin from the Golgi to the ER.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Journal or Publication Title: JOURNAL OF BIOLOGICAL CHEMISTRY
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
ISSN: 0021-9258
Date: 9 March 2001
Volume: 276
Number: 10
Number of Pages: 7
Page Range: pp. 7202-7208
Publication Status: Published
URI: http://wrap.warwick.ac.uk/id/eprint/12364

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item View Item
twitter

Email us: publications@warwick.ac.uk
Contact Details
About Us