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Enhanced in vitro p...
Enhanced in vitro production of amyloid-like fibrils from mutant (S20G) islet amyloid polypeptide
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- Ma, Zhi (författare)
- Linköpings universitet,Molekylär och immunologisk patologi,Hälsouniversitetet
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- Westermark, Gunilla, 1958- (författare)
- Linköpings universitet,Cellbiologi,Hälsouniversitetet
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- Sakagashira, S. (författare)
- First Department of Medicine, Wakayama University of Medical Science, Kagawa Medical University, Japan
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- Sanke, T. (författare)
- First Department of Medicine, Wakayama University of Medical Science, Kagawa Medical University, Japan
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- Gustavsson, Å (författare)
- Linköpings universitet,Molekylär och immunologisk patologi,Hälsouniversitetet
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- Sakamoto, H. (författare)
- Department of Pathology, Kagawa Medical University, Japan
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- Engström, Ulla (författare)
- Ludwig Institute of Cancer Research, Uppsala Branch, Uppsala University, Uppsala, Sweden,Ludwiginstitutet för Cancerforskning
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- Nanjo, K. (författare)
- First Department of Medicine, Wakayama University of Medical Science, Kagawa Medical University, Japan
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- Westermark, P (författare)
- Uppsala universitet,Institutionen för genetik och patologi,Amyloid,Department of Genetics and Pathology, Uppsala University, Uppsala, Sweden
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(creator_code:org_t)
- 2009-08-04
- 2001
- Engelska.
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Ingår i: Amyloid. - : Informa UK Limited. - 1350-6129 .- 1744-2818. ; 8, s. 242-
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.3...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- 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.
Nyckelord
- Islet amyloid polypeptide
- fibrillogenesis
- mutation
- dye fluorescence
- type 2 diabetes
- MEDICINE
- MEDICIN
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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Amyloid
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