LOGIN TO YOUR ACCOUNT

Username
Password
Remember Me
Or use your Academic/Social account:

CREATE AN ACCOUNT

Or use your Academic/Social account:

Congratulations!

You have just completed your registration at OpenAire.

Before you can login to the site, you will need to activate your account. An e-mail will be sent to you with the proper instructions.

Important!

Please note that this site is currently undergoing Beta testing.
Any new content you create is not guaranteed to be present to the final version of the site upon release.

Thank you for your patience,
OpenAire Dev Team.

Close This Message

CREATE AN ACCOUNT

Name:
Username:
Password:
Verify Password:
E-mail:
Verify E-mail:
*All Fields Are Required.
Please Verify You Are Human:
fbtwitterlinkedinvimeoflicker grey 14rssslideshare1
Goodchild, SC; Sheynis, T; Thompson, R; Tipping, KW; Xue, W-F; Ranson, NA; Hewitt, EW; Radford, SE; Beales, PA (2014)
Publisher: Public Library of Science
Languages: English
Types: Article
Subjects:
Although the molecular mechanisms underlying the pathology of amyloidoses are not well understood, the interaction between amyloid proteins and cell membranes is thought to play a role in several amyloid diseases. Amyloid fibrils of β-microglobulin (βm), associated with dialysis-related amyloidosis (DRA), have been shown to cause disruption of anionic lipid bilayers in vitro. However, the effect of lipid composition and the chemical environment in which βm-lipid interactions occur have not been investigated previously. Here we examine membrane damage resulting from the interaction of βm monomers and fibrils with lipid bilayers. Using dye release, tryptophan fluorescence quenching and fluorescence confocal microscopy assays we investigate the effect of anionic lipid composition and pH on the susceptibility of liposomes to fibrilinduced membrane damage. We show that βm fibril-induced membrane disruption is modulated by anionic lipid composition and is enhanced by acidic pH. Most strikingly, the greatest degree of membrane disruption is observed for liposomes containing bis(monoacylglycero)phosphate (BMP) at acidic pH, conditions likely to reflect those encountered in the endocytic pathway. The results suggest that the interaction between βm fibrils and membranes of endosomal origin may play a role in the molecular mechanism of βm amyloid-associated osteoarticular tissue destruction in DRA.

Share - Bookmark

Funded by projects

  • EC | AMYTOX
  • EC | AMYLOID
  • WT | The molecular basis of biolo...
  • WT | The Structural Basis of Biol...
  • WT | The molecular mechanisms of ...

Cite this article