Next Article in Journal / Special Issue
Structure-Dependent Interfacial Properties of Chaplin F from Streptomyces coelicolor
Previous Article in Journal
The TORC2‐Dependent Signaling Network in the Yeast Saccharomyces cerevisiae
Previous Article in Special Issue
The Role of Functional Amyloids in Multicellular Growth and Development of Gram-Positive Bacteria
Article Menu

Export Article

Open AccessArticle
Biomolecules 2017, 7(3), 67; doi:10.3390/biom7030067

Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils

1
CSL Limited, 45 Poplar Road, Parkville, VIC 3052, Australia
2
School of Biological Sciences and the Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong NSW 2522, Australia
3
Research School of Chemistry, The Australian National University, Acton ACT 2601, Australia
4
School of Biological Science and School of Chemical Science, University of Auckland, Auckland 1010, New Zealand
*
Author to whom correspondence should be addressed.
Academic Editors: Sarah Perrett, Margaret Sunde and Matthew Chapman
Received: 13 July 2017 / Revised: 21 August 2017 / Accepted: 7 September 2017 / Published: 12 September 2017
(This article belongs to the Special Issue Functional Amyloids)
View Full-Text   |   Download PDF [2818 KB, uploaded 18 September 2017]   |  

Abstract

Amyloid fibril formation occurs from a wide range of peptides and proteins and is typically associated with a loss of protein function and/or a gain of toxic function, as the native structure of the protein undergoes major alteration to form a cross β-sheet array. It is now well recognised that some amyloid fibrils have a biological function, which has led to increased interest in the potential that these so-called functional amyloids may either retain the function of the native protein, or gain function upon adopting a fibrillar structure. Herein, we investigate the molecular chaperone ability of α-crystallin, the predominant eye lens protein which is composed of two related subunits αA- and αB-crystallin, and its capacity to retain and even enhance its chaperone activity after forming aggregate structures under conditions of thermal and chemical stress. We demonstrate that both eye lens α-crystallin and αB-crystallin (which is also found extensively outside the lens) retain, to a significant degree, their molecular chaperone activity under conditions of structural change, including after formation into amyloid fibrils and amorphous aggregates. The results can be related directly to the effects of aging on the structure and chaperone function of α-crystallin in the eye lens, particularly its ability to prevent crystallin protein aggregation and hence lens opacification associated with cataract formation. View Full-Text
Keywords: amyloid fibril; small heat-shock protein; molecular chaperone; protein unfolding; protein aggregation amyloid fibril; small heat-shock protein; molecular chaperone; protein unfolding; protein aggregation
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Garvey, M.; Ecroyd, H.; Ray, N.J.; Gerrard, J.A.; Carver, J.A. Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils. Biomolecules 2017, 7, 67.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top