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  • Ma, ZhiLinköpings universitet,Molekylär och immunologisk patologi,Hälsouniversitetet (author)

Enhanced in vitro production of amyloid-like fibrils from mutant (S20G) islet amyloid polypeptide

  • Article/chapterEnglish2001

Publisher, publication year, extent ...

  • 2009-08-04
  • Informa UK Limited,2001
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:liu-25451
  • https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-25451URI
  • https://doi.org/10.3109/13506120108993820DOI
  • https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-63251URI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

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

Notes

  • On the day of the defence day the status of this article was submitted
  • Islet amyloid polypeptide (IAPP, “amylin”) is the amyloid-fibril-forming polypeptide in the islets of Langerhans associated with type 2 diabetes mellitus. A missense mutation in the IAPP gene associated with early-onset type 2 diabetes has been identified in the Japanese population. This mutation results in a glycine for serine substitution at position 20 of the mature IAPP molecule. Whether or not formation of islet amyloid with resulting destruction of islet tissue is the cause of this diabetes is yet not known. The present in vitro study was performed in order to investigate any influence of the amino acid substitution on the fibril formation capacity. Synthetic full-length wild type (lAPPwt) and mutant (IAPPS20G) as well as corresponding truncated peptides (position 18-29) were dissolved in dimethylsulfoxide (DMSO) or in 10% acetic acid at a concentration of 10 mg/mL and their fibril forming capacity was checked by Congo red staining, electron microscopy, a Congo red affinity assay and Thioflavine T fluorometric assay. It was found that full-length and truncated IAPPS20G both formed more amyloid-like fibrils and did this faster compared to IAPPwt. The fibril morphology differed slightly between the preparations. Conclusion: The amino acid substitution (S20G) is situated close to the region of the IAPP molecule implicated in the IAPP fibrillogenesis. The significantly increased formation of amyloid-like fibrils by IAPPS20G is highly interesting and may be associated with an increased islet amyloid formation in vivo and of fundamental importance in the pathogenesis of this specific form of diabetes.

Subject headings and genre

  • Islet amyloid polypeptide
  • fibrillogenesis
  • mutation
  • dye fluorescence
  • type 2 diabetes
  • MEDICINE
  • MEDICIN

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

  • Westermark, Gunilla,1958-Linköpings universitet,Cellbiologi,Hälsouniversitetet(Swepub:liu)gunwe13 (author)
  • Sakagashira, S.First Department of Medicine, Wakayama University of Medical Science, Kagawa Medical University, Japan (author)
  • Sanke, T.First Department of Medicine, Wakayama University of Medical Science, Kagawa Medical University, Japan (author)
  • Gustavsson, ÅLinköpings universitet,Molekylär och immunologisk patologi,Hälsouniversitetet (author)
  • Sakamoto, H.Department of Pathology, Kagawa Medical University, Japan (author)
  • Engström, UllaLudwig Institute of Cancer Research, Uppsala Branch, Uppsala University, Uppsala, Sweden,Ludwiginstitutet för Cancerforskning(Swepub:uu)ullaengs (author)
  • Nanjo, K.First Department of Medicine, Wakayama University of Medical Science, Kagawa Medical University, Japan (author)
  • Westermark, PUppsala universitet,Institutionen för genetik och patologi,Amyloid,Department of Genetics and Pathology, Uppsala University, Uppsala, Sweden(Swepub:uu)perweste (author)
  • Linköpings universitetMolekylär och immunologisk patologi (creator_code:org_t)

Related titles

  • In:Amyloid: Informa UK Limited8, s. 242-1350-61291744-2818
  • In:Amyloid: Informa UK Limited8, s. 242-

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