Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines

Sipe, Jean D.; Benson, Merrill D.; Buxbaum, Joel N.; Ikeda, Shu Ichi; Merlini, Giampaolo; Saraiva, Maria João; Westermark, Per

doi:10.1080/13506129.2016.1257986

Cited by 528 publications

(462 citation statements)

References 19 publications

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“…Light chain amyloidosis is the most common type of systemic amyloidosis, and appears to be more common than previously believed [12,13]. To date, 36 distinct proteins have been identified as amyloid fibril proteins in humans [14]. Major organ involvement, disease prognoses, and treatments can differ among the different subtypes of amyloidosis.…”

Section: Discussionmentioning

confidence: 99%

Primary Laryngo-Tracheobronchial Amyloidosis: A Case Report and Literature Review

Jiao¹,

Liu²,

Liu³

et al. 2017

J Clin Case Rep

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Primary laryngo-tracheobronchial amyloidosis is a rare pulmonary disease for which there is currently no established treatment. Herein, we report a case involving a 51-year-old woman who was admitted to hospital primarily due to intermittent hoarseness. Botryoidal masses were visible at the entrance of the throat. On chest computed tomography, eccentric soft tissue density shadows were apparent in the tracheal bifurcation of the proximal segment of the trachea, and the lumen was narrowed. Electronic bronchoscopy revealed extensive new biological invasive growth from the nasopharynx to the glottis. The glottis and larynx were irregularly shaped with clear characteristics and congestion. New biological growth was also observed in the right upper lobe, right middle bronchus, and right lower lobe mucosa. The patient was ultimately diagnosed with primary laryngo-tracheobronchial amyloidosis via pathological analysis. Although amyloidosis is a benign lesion, to date, there are no curative treatments. The present article briefly highlights the pertinent literature, and discusses the clinical manifestations and progress of treatment in primary laryngo-tracheobronchial amyloidosis.

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Section: Discussionmentioning

confidence: 99%

Primary Laryngo-Tracheobronchial Amyloidosis: A Case Report and Literature Review

Jiao¹,

Liu²,

Liu³

et al. 2017

J Clin Case Rep

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“…These findings indicated ATTR amyloidosis to be present. Wild-type ATTR amyloidosis was excluded because subsequent TTR gene analysis showed a novel mutation c.194C N G that encodes the primary translation product (p.A65G) and the mature protein TTR A45G [11]. SRM-MS proteomics confirmed the specific TTR mutation in the amyloid extracted from fat tissue.…”

Section: Casementioning

confidence: 99%

Late onset cardiomyopathy as presenting sign of ATTR A45G amyloidosis caused by a novel TTR mutation (p.A65G)

Klaassen

Lemmink

Bijzet

et al. 2017

Cardiovascular Pathology

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Objective: The clinical description of a novel TTR gene mutation characterized by a late onset amyloid cardiomyopathy. Methods and Results: A 78-year-old man of Dutch origin with recent surgery for bilateral carpal tunnel syndrome (CTS) was admitted to our hospital because of heart failure with preserved ejection fraction (55%). Cardiac ultrasound showed thickened biventricular walls, and cardiac magnetic resonance imaging also showed late gadolinium enhancement. Early signs of a polyneuropathy were found by neurophysiological testing. A few months later, his 72-year-old sister was admitted to an affiliated hospital because of heart failure caused by a restrictive cardiomyopathy. In both patients, a subcutaneous abdominal fat aspirate was stained with Congo red and DNA was analyzed by direct sequencing of exons 1 to 4 of the transthyretin (TTR) gene. Both fat aspirates revealed transthyretin-derived (ATTR) amyloid. Tc-diphosphonate scintigraphy further confirmed cardiac ATTR amyloidosis in the male patient. DNA analysis of both patients showed a novel TTR mutation c.194C N G that encodes for the gene product TTR (p.A65G) ending up as the mature protein TTR A45G. The 56-year-old daughter of the male patient had the same TTR mutation. A full diagnostic workup did not reveal any signs of amyloidosis yet. Conclusions: A novel amyloidogenic TTR mutation was found in a Dutch family. The clinical presentation of ATTR A45G amyloidosis in the affected family members was heart failure due to a late-onset cardiomyopathy. The systemic nature of this disease was reflected by bilateral CTS and by early signs of a polyneuropathy in the index patient.

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“…The amyloid state of a peptide is more stable thermodynamically, and its native state is the metastable state [5]. Peptide amyloidosis is considered as a cause of a variety of pathologies [6]. Misfolding of peptides, self-assembly into insoluble amyloid fibrillar structure, and formation of strictly ordered accumulations underlie many amyloid-related diseases (the amyloid proteins are indicated in brackets): Alzheimer's disease (amyloid β-peptides, tau protein);…”

Section: Introductionmentioning

confidence: 99%

Effects of Extract and Phenol Glycoside from Rose Petals on the Amylin Fibrils

Hovnanyan¹,

Sharoyan²,

Antonyan³

et al. 2017

OALib

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Peptide amyloidoses are considered as causes of a variety of pathologies (Alzheimer's disease, Parkinson's disease, type 2 diabetes, etc.). In the present work, the results of the transmission and scanning electron microscopy (TEM and SEM) were used to study the effects of the ethanol extract of rose petals and phenol glycoside fraction, isolated from it, on the fibrillation of the amyloid polypeptide amylin (AIAPP), which is toxic for islet cells. At TEM and SEM visualization of amylin fibrils, the size, form-factor, distribution by dimension and by polymorphism degree were taken into account. The nature of conformational diversity of aggregates of varying degree was analyzed. The analyses showed simultaneous presence of various structural forms: protofibrils, mature fibrils and ribbon-like forms. In case of plant preparations, a) inclusions of their particles caused increase of fibril dimention; b) amorphous bundles without clear configuration of the structure appeared, etc. These observations are in concordance with the earlier observed ability of these plant preparations to hinder the amylin fibrillation and to protect the islet cells from the toxicity of aggregated amylin. The findings of the present work demonstrate TEM and SEM as reasonable approaches in seeking effective antiamyloidogenic agents.

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Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines

Cited by 528 publications

References 19 publications

Primary Laryngo-Tracheobronchial Amyloidosis: A Case Report and Literature Review

Primary Laryngo-Tracheobronchial Amyloidosis: A Case Report and Literature Review

Late onset cardiomyopathy as presenting sign of ATTR A45G amyloidosis caused by a novel TTR mutation (p.A65G)

Effects of Extract and Phenol Glycoside from Rose Petals on the Amylin Fibrils

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