Amyloid formation by salmon calcitonin

P. J. Gilchrist; J. P. Bradshaw

doi:10.1016/0925-4439(93)90160-3

Amyloid formation by salmon calcitonin

P. J. Gilchrist, J. P. Bradshaw

Vice Chancellor's Office

Research output: Contribution to journal › Article › peer-review

Abstract

It is demonstrated using three independent methods that salmon calcitonin can form amyloid fibrils in vitro. Large aggregates are shown to exhibit a blue-green birefringence in cross polarised light after staining with congo red. Individual fibrils were observed using electron microscopy. These fibrils are approx. 50-60 Å in diameter and up to 20 000 Å in length and are similar in appearance to those observed in Alzheimer's disease. Finally, X-ray diffraction studies of the large aggregates reveal the cross-β conformation characteristic of the monomers in the fibre.

Original language	English
Pages (from-to)	111-114
Number of pages	4
Journal	BBA - Molecular Basis of Disease
Volume	1182
Issue number	1
DOIs	https://doi.org/10.1016/0925-4439(93)90160-3
Publication status	Published - 4 Aug 1993

Keywords

Alzheimer's disease
Amyloid formation
Amyloid plaque
Calcitonin

ASJC Scopus subject areas

Molecular Medicine
Molecular Biology

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10.1016/0925-4439(93)90160-3

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abstract = "It is demonstrated using three independent methods that salmon calcitonin can form amyloid fibrils in vitro. Large aggregates are shown to exhibit a blue-green birefringence in cross polarised light after staining with congo red. Individual fibrils were observed using electron microscopy. These fibrils are approx. 50-60 {\AA} in diameter and up to 20 000 {\AA} in length and are similar in appearance to those observed in Alzheimer's disease. Finally, X-ray diffraction studies of the large aggregates reveal the cross-β conformation characteristic of the monomers in the fibre.",

keywords = "Alzheimer's disease, Amyloid formation, Amyloid plaque, Calcitonin",

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AB - It is demonstrated using three independent methods that salmon calcitonin can form amyloid fibrils in vitro. Large aggregates are shown to exhibit a blue-green birefringence in cross polarised light after staining with congo red. Individual fibrils were observed using electron microscopy. These fibrils are approx. 50-60 Å in diameter and up to 20 000 Å in length and are similar in appearance to those observed in Alzheimer's disease. Finally, X-ray diffraction studies of the large aggregates reveal the cross-β conformation characteristic of the monomers in the fibre.

KW - Alzheimer's disease

KW - Amyloid formation

KW - Amyloid plaque

KW - Calcitonin

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Amyloid formation by salmon calcitonin

Abstract

Keywords

ASJC Scopus subject areas

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