CSIRO Publishing blank image blank image blank image blank imageBooksblank image blank image blank image blank imageJournalsblank image blank image blank image blank imageAbout Usblank image blank image blank image blank imageShopping Cartblank image blank image blank image You are here: Journals > Australian Journal of Chemistry   
Australian Journal of Chemistry
Journal Banner
  An international journal for chemical science
 
blank image Search
 
blank image blank image
blank image
 
  Advanced Search
   

Journal Home
About the Journal
Editorial Board
Contacts
For Advertisers
Content
Online Early
Current Issue
Just Accepted
All Issues
Virtual Issues
Special Issues
Research Fronts
Sample Issue
Covers
For Authors
General Information
Notice to Authors
Submit Article
Open Access
For Referees
Referee Guidelines
Review an Article
For Subscribers
Subscription Prices
Customer Service
Print Publication Dates

blue arrow e-Alerts
blank image
Subscribe to our Email Alert or RSS feeds for the latest journal papers.

red arrow Connect with us
blank image
facebook twitter youtube

Affiliated with RACI

Royal Australian Chemical Institute
Royal Australian
Chemical Institute


 

Article << Previous     |     Next >>   Contents Vol 56(5)

Intracellular Protein Unfolding and Aggregation: The Role of Small Heat-Shock Chaperone Proteins

Teresa M. Treweek, Amie M. Morris and John A. Carver

Australian Journal of Chemistry 56(5) 357 - 367
Published: 20 May 2003

Abstract

Molecular chaperones are a diverse group of proteins that interact with partially folded protein states to stabilize and prevent their mutual (illicit) association. Proteins require involvement with molecular chaperones throughout their lifespan: from their synthesis and folding through intracellular transport, membrane translocation, and to their ultimate degradation. Small heat-shock proteins (sHsps) are a ubiquitous family of molecular chaperones that are found in all organisms. Unlike many of the well-characterized chaperones, for example from the Hsp60 and Hsp70 families, sHsps are not involved in regulating protein folding. Instead, under conditions of cellular stress, such as elevated temperatures, they interact and stabilize partially folded target proteins to prevent their aggregation and precipitation. Because of this ability, their expression is elevated in many protein diseases that are characterized by protein aggregation and precipitation, including Alzheimer's, Creutzfeldt–Jakob, and Parkinson's diseases. The principal lens protein, α-crystallin, is a sHsp. Its chaperone ability is important in preventing lens protein precipitation and hence in maintaining lens transparency. This review summarizes the salient structural features of sHsps that enable them to act as highly efficient chaperones to prevent protein precipitation under stress conditions. The mechanism of chaperone action and the state of the target protein when interacting with sHsps are also discussed. Finally, diseases in which sHsp expression is elevated are discussed including the potential roles of sHsps and their therapeutic uses in the treatment of these diseases.



Full text doi:10.1071/CH03031

© CSIRO 2003

blank image
Subscriber Login
Username:
Password:  

 
PDF (306 KB) $25
 Export Citation
 Print
  


    
Legal & Privacy | Contact Us | Help

CSIRO

© CSIRO 1996-2014