Characterization of amyloid deposits in neurodegenerative diseases

Research output: Chapter in Book/Report/Conference proceedingChapter

10 Citations (Scopus)

Abstract

The extracellular accumulation of insoluble fibrillar peptides in brain parenchyma and vessel walls as amyloid is the hallmark of neurodegenerative diseases, such as Alzheimer's disease and Prion diseases. Regardless their amino acid sequences, all amyloid peptides adopt an insoluble, highly ordered beta sheet structure when aggregated. Amyloid is homogeneous and eosinophilic and, common to most cross-beta-type structures; it is generally identified by apple-green birefringence when stained with Congo red and seen under polarized light. Amyloid can also be identified by an apple green color when stained with thioflavine-S and seen under a fluorescence microscope. By electron microscopy, the typical fibrillar ultrastructure of amyloid deposits is revealed. The biochemical nature of the amyloid subunits present in the deposits can be recognized by immunohistochemistry using specific antibodies or by amino acid sequencing analysis, western blot, and mass spectrometry after isolation of parenchymal or vascular amyloid proteins.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
Pages241-258
Number of pages18
Volume793
DOIs
StatePublished - 2011

Publication series

NameMethods in Molecular Biology
Volume793
ISSN (Print)10643745

Fingerprint

Amyloid Plaques
Amyloid
Neurodegenerative Diseases
Birefringence
Amyloidogenic Proteins
Congo Red
Peptides
Prion Diseases
Protein Sequence Analysis
Malus
Blood Vessels
Amino Acid Sequence
Mass Spectrometry
Electron Microscopy
Alzheimer Disease
Color
Fluorescence
Western Blotting
Immunohistochemistry
Light

Keywords

  • Amyloid
  • Cerebral amyloid angiopathy
  • Dementia
  • Fibrillar
  • Neurodegeneration

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Vidal, R., & Ghetti, B. (2011). Characterization of amyloid deposits in neurodegenerative diseases. In Methods in Molecular Biology (Vol. 793, pp. 241-258). (Methods in Molecular Biology; Vol. 793). https://doi.org/10.1007/978-1-61779-328-8_16

Characterization of amyloid deposits in neurodegenerative diseases. / Vidal, Ruben; Ghetti, Bernardino.

Methods in Molecular Biology. Vol. 793 2011. p. 241-258 (Methods in Molecular Biology; Vol. 793).

Research output: Chapter in Book/Report/Conference proceedingChapter

Vidal, R & Ghetti, B 2011, Characterization of amyloid deposits in neurodegenerative diseases. in Methods in Molecular Biology. vol. 793, Methods in Molecular Biology, vol. 793, pp. 241-258. https://doi.org/10.1007/978-1-61779-328-8_16
Vidal R, Ghetti B. Characterization of amyloid deposits in neurodegenerative diseases. In Methods in Molecular Biology. Vol. 793. 2011. p. 241-258. (Methods in Molecular Biology). https://doi.org/10.1007/978-1-61779-328-8_16
Vidal, Ruben ; Ghetti, Bernardino. / Characterization of amyloid deposits in neurodegenerative diseases. Methods in Molecular Biology. Vol. 793 2011. pp. 241-258 (Methods in Molecular Biology).
@inbook{e6ceaf15fb6b4913920ead41a5aaa68f,
title = "Characterization of amyloid deposits in neurodegenerative diseases",
abstract = "The extracellular accumulation of insoluble fibrillar peptides in brain parenchyma and vessel walls as amyloid is the hallmark of neurodegenerative diseases, such as Alzheimer's disease and Prion diseases. Regardless their amino acid sequences, all amyloid peptides adopt an insoluble, highly ordered beta sheet structure when aggregated. Amyloid is homogeneous and eosinophilic and, common to most cross-beta-type structures; it is generally identified by apple-green birefringence when stained with Congo red and seen under polarized light. Amyloid can also be identified by an apple green color when stained with thioflavine-S and seen under a fluorescence microscope. By electron microscopy, the typical fibrillar ultrastructure of amyloid deposits is revealed. The biochemical nature of the amyloid subunits present in the deposits can be recognized by immunohistochemistry using specific antibodies or by amino acid sequencing analysis, western blot, and mass spectrometry after isolation of parenchymal or vascular amyloid proteins.",
keywords = "Amyloid, Cerebral amyloid angiopathy, Dementia, Fibrillar, Neurodegeneration",
author = "Ruben Vidal and Bernardino Ghetti",
year = "2011",
doi = "10.1007/978-1-61779-328-8_16",
language = "English",
isbn = "9781617793271",
volume = "793",
series = "Methods in Molecular Biology",
pages = "241--258",
booktitle = "Methods in Molecular Biology",

}

TY - CHAP

T1 - Characterization of amyloid deposits in neurodegenerative diseases

AU - Vidal, Ruben

AU - Ghetti, Bernardino

PY - 2011

Y1 - 2011

N2 - The extracellular accumulation of insoluble fibrillar peptides in brain parenchyma and vessel walls as amyloid is the hallmark of neurodegenerative diseases, such as Alzheimer's disease and Prion diseases. Regardless their amino acid sequences, all amyloid peptides adopt an insoluble, highly ordered beta sheet structure when aggregated. Amyloid is homogeneous and eosinophilic and, common to most cross-beta-type structures; it is generally identified by apple-green birefringence when stained with Congo red and seen under polarized light. Amyloid can also be identified by an apple green color when stained with thioflavine-S and seen under a fluorescence microscope. By electron microscopy, the typical fibrillar ultrastructure of amyloid deposits is revealed. The biochemical nature of the amyloid subunits present in the deposits can be recognized by immunohistochemistry using specific antibodies or by amino acid sequencing analysis, western blot, and mass spectrometry after isolation of parenchymal or vascular amyloid proteins.

AB - The extracellular accumulation of insoluble fibrillar peptides in brain parenchyma and vessel walls as amyloid is the hallmark of neurodegenerative diseases, such as Alzheimer's disease and Prion diseases. Regardless their amino acid sequences, all amyloid peptides adopt an insoluble, highly ordered beta sheet structure when aggregated. Amyloid is homogeneous and eosinophilic and, common to most cross-beta-type structures; it is generally identified by apple-green birefringence when stained with Congo red and seen under polarized light. Amyloid can also be identified by an apple green color when stained with thioflavine-S and seen under a fluorescence microscope. By electron microscopy, the typical fibrillar ultrastructure of amyloid deposits is revealed. The biochemical nature of the amyloid subunits present in the deposits can be recognized by immunohistochemistry using specific antibodies or by amino acid sequencing analysis, western blot, and mass spectrometry after isolation of parenchymal or vascular amyloid proteins.

KW - Amyloid

KW - Cerebral amyloid angiopathy

KW - Dementia

KW - Fibrillar

KW - Neurodegeneration

UR - http://www.scopus.com/inward/record.url?scp=80054720192&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=80054720192&partnerID=8YFLogxK

U2 - 10.1007/978-1-61779-328-8_16

DO - 10.1007/978-1-61779-328-8_16

M3 - Chapter

SN - 9781617793271

VL - 793

T3 - Methods in Molecular Biology

SP - 241

EP - 258

BT - Methods in Molecular Biology

ER -