liu.seSearch for publications in DiVA
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture
Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Biochemistry.
Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
Norwegian University of Science & Technology.
Linköping University, Department of Clinical and Experimental Medicine, Experimental Pathology . Linköping University, Faculty of Health Sciences.
Show others and affiliations
2008 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, Vol. 377, no 4, 1072-1078 p.Article in journal (Refereed) Published
Abstract [en]

Recent studies Suggest that Soluble, oligomeric species, which are intermediates in the fibril formation process in amyloid disease, might be the key species in amyloid pathogenesis. Soluble oligomers of human wild type transthyretin (TTR) were produced to elucidate oligomer properties. Employing ThT fluorescence, time-resolved fluorescence anisotropy of pyrene-labeled TTR, chemical cross-linking, and electron microscopy we demonstrated that early formed soluble oligomers (within minutes) from A-state TTR comprised on the average 20-30 TTR monomers. When administered to neuroblastoma cells these early oligomers proved highly cytotoxic and induced apoptosis after 48 h of incubation. More Mature fibrils (> 24 h of fibrillation) were non-toxic. Surprisingly, we also found that native tetrameric TTR, when purified and stored under cold conditions (4 degrees C) was highly cytotoxic. The effect Could be partially restored by increasing the temperature of the protein. The cytotoxic effects of native tetrameric TTR likely stems from a hitherto unexplored low temperature induced rearrangement of the tetramer conformation that possibly is related to the conformation of misfolded TTR in amyloigogenic oligomers.

Place, publisher, year, edition, pages
2008. Vol. 377, no 4, 1072-1078 p.
Keyword [en]
Amyloid, Apoptosis, Transthyretin, Misfolding, Oligomer
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-16229DOI: 10.1016/j.bbrc.2008.10.121OAI: oai:DiVA.org:liu-16229DiVA: diva2:133478
Available from: 2009-01-12 Created: 2009-01-09 Last updated: 2009-05-15

Open Access in DiVA

No full text

Other links

Publisher's full text

Authority records BETA

Sörgjerd, KarinKlingstedt, TheréseKågedal, KatarinaHammarström , Per

Search in DiVA

By author/editor
Sörgjerd, KarinKlingstedt, TheréseKågedal, KatarinaHammarström , Per
By organisation
The Institute of TechnologyBiochemistryDepartment of Physics, Chemistry and BiologyExperimental Pathology Faculty of Health Sciences
In the same journal
Biochemical and Biophysical Research Communications - BBRC
Medical and Health Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 97 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf