Literature DB >> 8347681

Amyloid formation by salmon calcitonin.

P J Gilchrist1, J P Bradshaw.   

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 A in diameter and up to 20,000 A 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-beta conformation characteristics of the monomers in the fibre.

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Year:  1993        PMID: 8347681     DOI: 10.1016/0925-4439(93)90160-3

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  8 in total

1.  Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy.

Authors:  M Bouchard; J Zurdo; E J Nettleton; C M Dobson; C V Robinson
Journal:  Protein Sci       Date:  2000-10       Impact factor: 6.725

Review 2.  Factors affecting the physical stability (aggregation) of peptide therapeutics.

Authors:  Karolina L Zapadka; Frederik J Becher; A L Gomes Dos Santos; Sophie E Jackson
Journal:  Interface Focus       Date:  2017-10-20       Impact factor: 3.906

3.  Channel formation by salmon and human calcitonin in black lipid membranes.

Authors:  V Stipani; E Gallucci; S Micelli; V Picciarelli; R Benz
Journal:  Biophys J       Date:  2001-12       Impact factor: 4.033

4.  Prolactin-derived amyloid in the aging pituitary gland.

Authors:  P Westermark; L Eriksson; U Engström; S Eneström; K Sletten
Journal:  Am J Pathol       Date:  1997-01       Impact factor: 4.307

5.  Structural studies of EDTA-induced fibrillation of salmon calcitonin.

Authors:  Stefan Seyferth; Geoffrey Lee
Journal:  Pharm Res       Date:  2003-01       Impact factor: 4.200

6.  Amyloid oligomer neurotoxicity, calcium dysregulation, and lipid rafts.

Authors:  Fiorella Malchiodi-Albedi; Silvia Paradisi; Andrea Matteucci; Claudio Frank; Marco Diociaiuti
Journal:  Int J Alzheimers Dis       Date:  2011-02-08

Review 7.  The slowly aggregating salmon Calcitonin: a useful tool for the study of the amyloid oligomers structure and activity.

Authors:  Marco Diociaiuti; Maria Cristina Gaudiano; Fiorella Malchiodi-Albedi
Journal:  Int J Mol Sci       Date:  2011-12-13       Impact factor: 5.923

8.  Monosialoganglioside-GM1 triggers binding of the amyloid-protein salmon calcitonin to a Langmuir membrane model mimicking the occurrence of lipid-rafts.

Authors:  Marco Diociaiuti; Cristiano Giordani; Gihan S Kamel; Francesco Brasili; Simona Sennato; Cecilia Bombelli; Karen Y Meneses; Marco A Giraldo; Federico Bordi
Journal:  Biochem Biophys Rep       Date:  2016-10-15
  8 in total

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