Amyloid formation by salmon calcitonin

P. J. Gilchrist, J. P. Bradshaw

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)111-114
Number of pages4
JournalBBA - Molecular Basis of Disease
Volume1182
Issue number1
DOIs
Publication statusPublished - 4 Aug 1993

Keywords

  • Alzheimer's disease
  • Amyloid formation
  • Amyloid plaque
  • Calcitonin

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology

Cite this

Amyloid formation by salmon calcitonin. / Gilchrist, P. J.; Bradshaw, J. P.

In: BBA - Molecular Basis of Disease, Vol. 1182, No. 1, 04.08.1993, p. 111-114.

Research output: Contribution to journalArticle

Gilchrist, P. J. ; Bradshaw, J. P. / Amyloid formation by salmon calcitonin. In: BBA - Molecular Basis of Disease. 1993 ; Vol. 1182, No. 1. pp. 111-114.
@article{fdb65dcf1d3f4e3ebd5adda1c7a7a5d6,
title = "Amyloid formation by salmon calcitonin",
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",
author = "Gilchrist, {P. J.} and Bradshaw, {J. P.}",
year = "1993",
month = "8",
day = "4",
doi = "10.1016/0925-4439(93)90160-3",
language = "English",
volume = "1182",
pages = "111--114",
journal = "BBA - Molecular Basis of Disease",
issn = "0925-4439",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Amyloid formation by salmon calcitonin

AU - Gilchrist, P. J.

AU - Bradshaw, J. P.

PY - 1993/8/4

Y1 - 1993/8/4

N2 - 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.

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

UR - http://www.scopus.com/inward/record.url?scp=0027178622&partnerID=8YFLogxK

U2 - 10.1016/0925-4439(93)90160-3

DO - 10.1016/0925-4439(93)90160-3

M3 - Article

VL - 1182

SP - 111

EP - 114

JO - BBA - Molecular Basis of Disease

JF - BBA - Molecular Basis of Disease

SN - 0925-4439

IS - 1

ER -