Isolated Atrial Amyloidosis and the Importance of Molecular Classification

Podduturi, Varsha; Armstrong, Danielle; Hitchcock, Michael A.; Roberts, William C.; Guileyardo, Joseph M.

doi:10.1080/08998280.2013.11929013

Cited by 20 publications

(13 citation statements)

References 5 publications

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“…74,181,182 Amyloidosis is characterized by the presence of extracellular proteinaceous deposits showing characteristic structural and tinctorial properties. The various types of amyloidosis are distinguished based on the fibril protein deposited and the clinical presentation.…”

Section: Section 2: Definitions Mechanisms and Rationale For Af Ablmentioning

confidence: 99%

2012 HRS/EHRA/ECAS Expert Consensus Statement on Catheter and Surgical Ablation of Atrial Fibrillation: Recommendations for Patient Selection, Procedural Techniques, Patient Management and Follow-up, Definitions, Endpoints, and Research Trial Design

Calkins,

Kuck,

Cappato

et al. 2012

Heart Rhythm

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Section: Section 2: Definitions Mechanisms and Rationale For Af Ablmentioning

confidence: 99%

2012 HRS/EHRA/ECAS Expert Consensus Statement on Catheter and Surgical Ablation of Atrial Fibrillation: Recommendations for Patient Selection, Procedural Techniques, Patient Management and Follow-up, Definitions, Endpoints, and Research Trial Design

Calkins,

Kuck,

Cappato

et al. 2012

Heart Rhythm

1,769

1,468

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“…Thus, the relationship [4][5][6] between LA function and the frequently seen atrial arrhythmia in cardiac amyloidosis is not fully elucidated [6,7].…”

Section: Introductionmentioning

confidence: 99%

Reduced left atrial myocardial deformation irrespective of cavity size: a potential cause for atrial arrhythmia in hereditary transthyretin amyloidosis

Henein

Suhr

Arvidsson

et al. 2018

Amyloid

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“…10 Intrinsically disordered protein (IDP) sequences have been shown to contain fewer APRs than the globular proteins with welldefined native conformations. 10,11 The formation of insoluble, highly structured amyloid fibrillary aggregates leads to amyloidosis, which is associated with a broad range of human diseases including chronic (e.g., Type II diabetes 12,13 ), cardiovascular (e.g., Atrial amyloidosis 14,15 ), neurodegenerative (e.g., Alzheimer's and Parkinson's 16 ), prion (e.g., mad cow disease 17 ) diseases, and cancer. 18,19 Protein aggregation is also a major hurdle in the development of biotechnological products, such as monoclonal antibodies, recombinant human proteins and enzymes.…”

Section: Introductionmentioning

confidence: 99%

Aggregation prone regions in human proteome: Insights from large‐scale data analyses

et al. 2017

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Protein aggregation leads to several burdensome human maladies, but a molecular level understanding of how human proteome has tackled the threat of aggregation is currently lacking. In this work, we survey the human proteome for incidence of aggregation prone regions (APRs), by using sequences of experimentally validated amyloid-fibril forming peptides and via computational predictions. While approximately 30 human proteins are currently known to be amyloidogenic, we found that 260 proteins (∼1% of human proteome) contain at least one experimentally validated amyloid-fibril forming segment. Computer predictions suggest that more than 80% of the human proteins contain at least one potential APR and approximately two-thirds (65%) contain two or more APRs; spanning 3-5% of their sequences. Sequence randomizations show that this apparently high incidence of APRs has been actually significantly reduced by unique amino acid composition and sequence patterning of human proteins. The human proteome has utilized a wide repertoire of sequence-structural optimization strategies, most of them already known, to minimize deleterious consequences due to the presence of APRs while simultaneously taking advantage of their order promoting properties. This survey also found that APRs tend to be located near the active and ligand binding sites in human proteins, but not near the post translational modification sites. The APRs in human proteins are also preferentially found at heterotypic interfaces rather than homotypic ones. Interestingly, this survey reveals that APRs play multiple, often opposing, roles in the human protein sequence-structure-function relationships. Insights gained from this work have several interesting implications towards novel drug discovery and development. Proteins 2017; 85:1099-1118. © 2017 Wiley Periodicals, Inc.

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Isolated Atrial Amyloidosis and the Importance of Molecular Classification

Cited by 20 publications

References 5 publications

2012 HRS/EHRA/ECAS Expert Consensus Statement on Catheter and Surgical Ablation of Atrial Fibrillation: Recommendations for Patient Selection, Procedural Techniques, Patient Management and Follow-up, Definitions, Endpoints, and Research Trial Design

2012 HRS/EHRA/ECAS Expert Consensus Statement on Catheter and Surgical Ablation of Atrial Fibrillation: Recommendations for Patient Selection, Procedural Techniques, Patient Management and Follow-up, Definitions, Endpoints, and Research Trial Design

Reduced left atrial myocardial deformation irrespective of cavity size: a potential cause for atrial arrhythmia in hereditary transthyretin amyloidosis

Aggregation prone regions in human proteome: Insights from large‐scale data analyses

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