Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee

Benson, Merrill D.; Buxbaum, Joel N.; Eisenberg, David; Merlini, Giampaolo; Saraiva, Maria João; Sekijima, Yoshiki; Sipe, Jean D.; Westermark, Per

doi:10.1080/13506129.2020.1835263

Cited by 286 publications

(316 citation statements)

References 15 publications

(15 reference statements)

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“…Alzheimer's Disease) and other major pathologies (e.g. type II diabetes) or systemic forms such as light-chain amyloidosis 1 .…”

Section: Introductionmentioning

confidence: 99%

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A structural analysis of amyloid polymorphism in disease: clues for selective vulnerability?

Kant

Louros

Schymkowitz

et al. 2021

Preprint

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The increasing amount of amyloid structures offers an opportunity to investigate the general principles determining amyloid stability and polymorphism in disease. We find that amyloid stability is dominated by about 30% of residues localized in few segments interspersed with regions that are often structurally frustrated in the cross-β conformation. These stable segments correspond to known aggregation-nucleating regions and constitute a cross-β structural framework that is shared among polymorphs. Alternative tertiary packing of these segments within the protofibril results in conformationally different but energetically similar polymorphs. This combination of a conserved structural framework along the axis and energetic ambiguity across the axis results in polymorphic plasticity that explains a number of fundamental amyloid properties, including fibril defects and brittleness but also the polymorphic instability of amyloids in simple aqueous buffers. Together these findings suggest a structural model for in vivo polymorphic bias and selective cellular vulnerability whereby (1) polymorphic bias is induced by particular templating interactions in susceptible cells, (2) once formed specific polymorphs are entropically primed to selectively bind similar targets in neighbouring cells, (3) conservation of polymorphic bias during pathological spreading implies the continued presence of similar templating interactions in successive susceptible cells and (4) absence of templating interactions relaxes polymorphic bias possibly allowing for the modification of cellular susceptibilities during disease progression by novel templating interactions.

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“…Alzheimer's Disease) and other major pathologies (e.g. type II diabetes) or systemic forms such as light-chain amyloidosis 1 .…”

Section: Introductionmentioning

confidence: 99%

“…Alzheimer’s Disease) and other major pathologies (e.g. type II diabetes) or systemic forms such as light-chain amyloidosis 1 . These proteins are completely dissimilar in terms of sequence, native structure, and function.…”

Section: Introductionmentioning

confidence: 99%

A structural analysis of amyloid polymorphism in disease: clues for selective vulnerability?

Kant

Louros

Schymkowitz

et al. 2021

Preprint

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“…A broad range of human diseases arise from protein aggregation and subsequent amyloid deposition in different organs [1]. One such condition is transthyretin amyloidosis (ATTR), a systemic amyloid disease associated with deposition of transthyretin (TTR).…”

Section: Introductionmentioning

confidence: 99%

Enhanced detection of ATTR amyloid using a nanofibril-based assay

Rahman

Schmuck

Hansson

et al. 2021

Amyloid

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More than 30 proteins and peptides have been found to form amyloid fibrils in human diseases. Fibrils formed by transthyretin (TTR) are associated with ATTR amyloidosis, affecting many vital organs, including the heart and peripheral nervous system. Congo red staining is the gold standard method for detection of amyloid deposits in tissue. However, Congo red staining and amyloid typing methods such as immunofluorescence labelling are limited to relatively large deposits. Detection of small ATTR deposits present at an early stage of the disease could enable timely treatment and prevent severe tissue damage. In this study, we developed an enhanced ATTR amyloid detection method that uses functionalised protein nanofibrils. Using this method, we achieved sensitive detection of monomeric TTR in a microplate immunoassay and immunofluorescence labelling of ex vivo tissue from two patients containing ATTR aggregates. The system's utility was confirmed on sections from a patient with AA amyloidosis and liver sections from inflamed mouse. These results suggest that the detection system constitutes important new technology for highly sensitive detection of microscopic amounts of ATTR amyloid deposited in tissue.

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“…ent sources have been identified [2]. Three entities constitute the most common forms of systemic amyloidosis: AL (light chain amyloidosis), ATTRwt (wild type transthyretin amyloidosis) and AA (serum amyloid A amyloidosis).…”

Section: Introductionmentioning

confidence: 99%

Immunoglobulin light chain amyloidosis

Agis

Krauth

2021

memo

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SummaryImmunoglobulin light chain (AL) amyloidosis is a rare and underdiagnosed life-threatening systemic disease, primarily caused by insoluble depositions of misfolded monoclonal light chains. The monoclonal light chain paraprotein originates from a small clonal B‑cell or a clonal plasma cell population. If left undetected the paraprotein can induce a number of complications based on organ damage. The most dangerous and life-threatening organ dysfunction emerges from cardiac involvement. Thus, patients overall survival depends on early detection. Establishing the correct diagnosis and clear characterization of the amyloid-forming protein, staging, risk assessment and treatment are crucial and depend on a highly experienced interdisciplinary, multiprofessional team.

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Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee

Cited by 286 publications

References 15 publications

A structural analysis of amyloid polymorphism in disease: clues for selective vulnerability?

A structural analysis of amyloid polymorphism in disease: clues for selective vulnerability?

Enhanced detection of ATTR amyloid using a nanofibril-based assay

Immunoglobulin light chain amyloidosis

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