SwePub
Sök i LIBRIS databas

  Extended search

id:"swepub:oai:DiVA.org:umu-4474"
 

Search: id:"swepub:oai:DiVA.org:umu-4474" > Characterisation of...

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist
  • Goldsteins, GundarsUmeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten) (author)

Characterisation of two highly amyloidogenic mutants of transthyretin

  • Article/chapterEnglish1997

Publisher, publication year, extent ...

  • 1997-05-06
  • American Chemical Society (ACS),1997
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:umu-4474
  • https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-4474URI
  • https://doi.org/10.1021/bi961649cDOI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • The plasma protein transthyretin (TTR) has the potential to form amyloid under certain conditions. More than 50 different point mutations have been associated with amyloid formation that occurs only in adults. It is not known what structural changes are introduced into the structure of this otherwise stable molecule that results in its aggregation into insoluble amyloid fibrils. On the basis of calculations of the frequency of known mutations over the polypeptide, we have constructed two mutants in the D-strand of the polypeptide. These molecules, containing either a deletion or a substitution at amino acid positions 53−55, were unstable and spontaneously formed aggregates upon storage in TBS (pH 7.6). The precipitates were shown to be amyloid by staining with thioflavin T and Congo Red. Their ultrastructure was very similar to that of amyloid fibrils deposited in the vitreous body of patients with familial amyloidotic polyneuropathy type 1 with an amino acid replacement in position 30 (TTRmet30). Like amyloid isolated from the vitreous body of the eye, the amyloid precipitates generated from the TTR mutants exposed a trypsin cleavage site between amino acid residues 48 and 49, while plasma TTRmet30 isolated from amyloidosis patients as well as wild-type TTR only showed minor trypsin sensitivity. Our data indicate that the mutants we have constructed are similar to amyloid precursors or may share structural properties with intermediates on a pathway leading to amyloid deposits of plasma TTR.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Andersson, KarinUmeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)kaan0001 (author)
  • Olofsson, Anders,1970-Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)anol0042 (author)
  • Dacklin, IngridUmeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)inda0001 (author)
  • Edvinsson, ÅsaUmeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten) (author)
  • Baranov, Vladimir,1940-Umeå universitet,Institutionen för klinisk mikrobiologi(Swepub:umu)vlba0001 (author)
  • Sandgren, OlaUmeå universitet,Oftalmiatrik(Swepub:umu)olsa0001 (author)
  • Thylén, ChristinaUmeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten) (author)
  • Hammarström, StenUmeå universitet,Institutionen för klinisk mikrobiologi(Swepub:umu)stha0002 (author)
  • Lundgren, ErikUmeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)erlu0003 (author)
  • Umeå universitetInstitutionen för molekylärbiologi (Medicinska fakulteten) (creator_code:org_t)

Related titles

  • In:Biochemistry: American Chemical Society (ACS)36:18, s. 5346-53520006-29601520-4995

Internet link

Find in a library

To the university's database

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view