“Amyloid” — Historical Aspects

Tanskanen, Maarit

doi:10.5772/53423

Cited by 18 publications

(16 citation statements)

References 85 publications

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“…More specialized stains and labels have emerged which have begun to probe the structure and composition of pathological protein deposits. The stains Congo red and thioflavin S (ThS) were discovered later and remain in use (reviewed by Westermark ( Sipe and Westermark, 2005 ) and Tanskanen ( Tanskanen, 2013 )), specifically identifying deposits containing a particular structural motif: amyloid β-pleated sheets. Beyond mere detection lies comprehensive identification of the protein components of these deposits; biochemical analyses of the deposits have produced transformative results in the field of neurodegeneration research.…”

Section: Introductionmentioning

confidence: 99%

Determining composition of micron-scale protein deposits in neurodegenerative disease by spatially targeted optical microproteomics

Hadley

Rakhit

Guo

et al. 2015

eLife

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Spatially targeted optical microproteomics (STOMP) is a novel proteomics technique for interrogating micron-scale regions of interest (ROIs) in mammalian tissue, with no requirement for genetic manipulation. Methanol or formalin-fixed specimens are stained with fluorescent dyes or antibodies to visualize ROIs, then soaked in solutions containing the photo-tag: 4-benzoylbenzyl-glycyl-hexahistidine. Confocal imaging along with two photon excitation are used to covalently couple photo-tags to all proteins within each ROI, to a resolution of 0.67 µm in the xy-plane and 1.48 µm axially. After tissue solubilization, photo-tagged proteins are isolated and identified by mass spectrometry. As a test case, we examined amyloid plaques in an Alzheimer's disease (AD) mouse model and a post-mortem AD case, confirming known plaque constituents and discovering new ones. STOMP can be applied to various biological samples including cell lines, primary cell cultures, ex vivo specimens, biopsy samples, and fixed post-mortem tissue.DOI: http://dx.doi.org/10.7554/eLife.09579.001

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Section: Introductionmentioning

confidence: 99%

Determining composition of micron-scale protein deposits in neurodegenerative disease by spatially targeted optical microproteomics

Hadley

Rakhit

Guo

et al. 2015

eLife

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“…The scientific term “amyloid” was coined in 1838 by Matthias Schleiden, a German botanist, who used it to describe a normal, starch-like constituent of plants [ 39 ]. Rudolf Virchow first introduced the term “amyloid” into medical literature in 1854.…”

Section: Amyloid-βmentioning

confidence: 99%

“…He used it to describe deposits in the central nervous system that exhibited the same staining characteristics as starch following reaction with iodine and sulfuric acid [ 40 ]. Virchow concluded that those cerebral structures were made of starch and referred to them as “corpora amylacea” (derived from the Latin and Greek words for starch: “amylum” and “αμυλον”, respectively) [ 39 , 41 ]. The concept of amyloid has transformed several times over the course of the following centuries.…”

Section: Amyloid-βmentioning

confidence: 99%

“…Alzheimer noted the presence of two distinctive pathologies: “miliary bodies” (plaques) and “dense bundles of fibrils” (tangles) which we know today, represent the pathological hallmarks of AD [ 42 ]. The first descriptions of AD pathology, including those of Alois Alzheimer, were based on Nissl’s silver staining method without any idea about its biochemical composition or a relationship to amyloid of such structures [ 39 ]. Indeed, the amyloid nature of senile plaques in AD was described only two decades later [ 39 , 43 ], shortly after the discovery of the Congo red staining for amyloid [ 44 ], and the establishment of Congo red reactivity as research criterion for amyloid [ 45 ].…”

Section: Amyloid-βmentioning

confidence: 99%

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Cerebrospinal Fluid Biomarkers in Alzheimer’s Disease—From Brain Starch to Bench and Bedside

2017

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Alzheimer’s disease is the most common cause of dementia. Over the last three decades, research has advanced dramatically and provided a detailed understanding of the molecular events underlying the pathogenesis of Alzheimer’s disease. In parallel, assays for the detection of biomarkers that reflect the typical Alzheimer’s disease-associated pathology have been developed and validated in myriads of clinical studies. Such biomarkers complement clinical diagnosis and improve diagnostic accuracy. The use of biomarkers will become even more important with the advent of disease-modifying therapies. Such therapies will likely be most beneficial when administered early in the disease course. Here, we summarise the development of the core Alzheimer’s disease cerebrospinal fluid biomarkers: amyloid-β and tau. We provide an overview of their role in cellular physiology and Alzheimer’s disease pathology, and embed their development as cerebrospinal fluid biomarkers into the historical context of Alzheimer’s disease research. Finally, we summarise recommendations for their use in clinical practice, and outline perspectives for novel cerebrospinal fluid candidate biomarkers.

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“…But, already in 1859 Freidrich and Kekule showed that amyloids did not con tain a substance chemically similar to starch or cellulose but were enriched with nitrogen and were protein like [1,38]. However, until the end of his life, Virchow consid ered amyloids to be polysaccharides [41]. Now it is known that amyloid inclusions isolated from mammalian tissues, in addition to the major fibrillar protein compo nent, also contain proteoglycans [42] and glycosamino glycans [43,44], which is an explanation of their stain ability with iodine.…”

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confidence: 99%

Amyloids: from pathogenesis to function

Nizhnikov

Antonets

Inge-Vechtomov

2015

Biochemistry Moscow

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The term "amyloids" refers to fibrillar protein aggregates with cross-β structure. They have been a subject of intense scrutiny since the middle of the previous century. First, this interest is due to association of amyloids with dozens of incurable human diseases called amyloidoses, which affect hundreds of millions of people. However, during the last decade the paradigm of amyloids as pathogens has changed due to an increase in understanding of their role as a specific variant of quaternary protein structure essential for the living cell. Thus, functional amyloids are found in all domains of the living world, and they fulfill a variety of roles ranging from biofilm formation in bacteria to long-term memory regulation in higher eukaryotes. Prions, which are proteins capable of existing under the same conditions in two or more conformations at least one of which having infective properties, also typically have amyloid features. There are weighty reasons to believe that the currently known amyloids are only a minority of their real number. This review provides a retrospective analysis of stages in the development of amyloid biology that during the last decade resulted, on one hand, in reinterpretation of the biological role of amyloids, and on the other hand, in the development of systems biology of amyloids, or amyloidomics.

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“Amyloid” — Historical Aspects

Cited by 18 publications

References 85 publications

Determining composition of micron-scale protein deposits in neurodegenerative disease by spatially targeted optical microproteomics

Determining composition of micron-scale protein deposits in neurodegenerative disease by spatially targeted optical microproteomics

Cerebrospinal Fluid Biomarkers in Alzheimer’s Disease—From Brain Starch to Bench and Bedside

Amyloids: from pathogenesis to function

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