RESUMEN
The Nomenclature Committee of the International Society of Amyloidosis met at the XVIII International Symposium on Amyloidosis in September and virtually in October 2022 with discussions resulting in this upgraded nomenclature recommendation. The nomenclature principles remain unchanged but there is an ongoing discussion regarding the importance and varying nature of intracellular protein aggregates, particularly those associated with neurodegenerative diseases. Six novel proteins were added to the list of human amyloid fibril proteins. Of these, three are polypeptide hormones and two currently utilised peptide drugs, making the number of known iatrogenic amyloid forms four, all appearing as subcutaneous nodules at the injection site. The sixth novel amyloid fibril protein is the transmembrane 106B protein, forming intracellular amyloid fibrils in disorders associated with frontotemporal dementia. The number of known human amyloid fibril proteins is now 42.
Asunto(s)
Amiloide , Amiloidosis , Humanos , Amiloide/metabolismo , Amiloidosis/metabolismo , Proteínas Amiloidogénicas/metabolismo , Proteínas de la MembranaRESUMEN
The ISA Nomenclature Committee met electronically before and directly after the XVII ISA International Symposium on Amyloidosis, which, unfortunately, had to be virtual in September 2020 due to the ongoing COVID-19 pandemic instead of a planned meeting in Tarragona in March. In addition to confirmation of basic nomenclature, several additional concepts were discussed, which are used in scientific amyloid literature. Among such concepts are cytotoxic oligomers, protofibrils, primary and secondary nucleation, seeding and cross-seeding, amyloid signature proteins, and amyloid plaques. Recommendations for their use are given. Definitions of amyloid and amyloidosis are confirmed. Possible novel human amyloid fibril proteins, appearing as 'classical' in vivo amyloid, were discussed. It was decided to include fibulin-like extracellular matrix protein 1 (amyloid protein: AEFEMP1), which appears as localised amyloid in portal veins. There are several possible amyloid proteins under investigation, and these are included in a new Table.
Asunto(s)
Amiloide/clasificación , Proteínas Amiloidogénicas/clasificación , Amiloidosis/clasificación , Terminología como Asunto , Amiloide/genética , Amiloide/metabolismo , Proteínas Amiloidogénicas/genética , Proteínas Amiloidogénicas/metabolismo , Amiloidosis/diagnóstico , Amiloidosis/genética , Amiloidosis/patología , COVID-19 , Congresos como Asunto , Infecciones por Coronavirus , Educación a Distancia/organización & administración , Expresión Génica , Humanos , Pandemias , Neumonía ViralRESUMEN
Enquadramento: O Acidente Vascular Cerebral (AVC) representa, atualmente a primeira causa de morte em Portugal, constituindo um dos problemas mais importantes de saúde pública, pelas graves consequências que acarreta, contribuindo para um elevado índice de incapacidade e dependência funcional e, consequentemente, de forma significativa, para uma diminuição da Qualidade de Vida (QV). O enfermeiro de família surge neste contexto como um interveniente com papel ativo, enquanto educador da pessoa após AVC e do cuidador principal/família, de forma a minimizar as incapacidades, promover o autocuidado e a sua readaptação, contribuindo para a melhoria da sua QV. Objetivo: Avaliar a qualidade de vida da pessoa após AVC, em contexto domiciliário. Métodos: Estudo de natureza quantitativa, descritivo-correlacional e transversal, numa amostra não probabilística, constituída por 24 pessoas com AVC referenciadas numa Equipa de Cuidados Continuados Integrados (ECCI) da região Centro de Portugal. Após a obtenção das autorizações e do consentimento informado, procedeu-se à colheita de dados através de um questionário de caraterização sociodemográfica e perfil clínico, aplicação do Índice de Barthel e da Escala Stroke Specific Quality of Life: SS-QoL (para avaliar a qualidade de vida da pessoa após AVC, validada e testada para a população Portuguesa por Malheiro, Nicola e Pereira (2009). O tratamento estatístico foi efetuado informaticamente, recorrendo ao programa de Statistical Package for Science Social (SPSS), versão 24. Resultados: No presente estudo a amostra é maioritariamente do sexo masculino (75%), com uma média de idade de 71 anos, em que a maioria (87,5%) sofreu um AVC Isquémico, com hemiparesia à esquerda (33,3%) e com dependência grave (54,2%). Constatou-se, também, que percecionam pior Qualidade de Vida, nos domínios: "trabalho/produtividade" (5,41%), "papel familiar" (5,54%) e "energia" (6,87%). Os resultados do estudo sugerem que a QV foi influenciada pela variável sexo no domínio "personalidade" (p=0,047) e "trabalho/produtividade" (p=0,050), pela variável com quem vive no domínio "papel social" (p=0,046), pelas habilitações literárias no domínio "trabalho/produtividade" (p=0,046) e "autocuidado" (p=0,050), pelo tipo de AVC no domínio "energia" (p=0,006), pelo tipo de comprometimento neurológico no domínio "mobilidade" (p=0,038), pelo Índice de Barthel nos domínios "mobilidade" (p=0,012), "função do membro superior" (p=0,000), "trabalho/produtividade" (p=0,002) e "autocuidado" (p=0,000). Conclusões: Os resultados encontrados neste estudo apontam para a necessidade de uma intervenção do Enfermeiro de Família junto das pessoas após AVC em contexto domiciliário, que permita desenvolver estratégias de cuidados que otimizem a capacidade funcional da pessoa, com diferentes níveis de dependência, promovam o autocuidado e a reintegração familiar e social, de modo a melhorar a QV da pessoa e dos que a rodeiam.
Asunto(s)
Humanos , Masculino , Anciano , Anciano de 80 o más Años , Autocuidado , Accidente Cerebrovascular , Enfermería en Salud Comunitaria , Atención Domiciliaria de SaludRESUMEN
The nomenclature committee of the International Society of Amyloidosis (ISA) meets every second year to discuss and formulate recommendations. The conclusions from the discussion at the XVI International Symposium on Amyloidosis in Kumamoto, Japan, 25-29 March 2018 and afterwards are summarized in this Nomenclature Article. From having recommended the use of the designation "amyloid fibril" for in vivo material only, ISA's nomenclature committee now accepts its use more broadly following the international scientific literature. However, it is important always to stress the origin of the ß-fibrils in order to avoid misunderstanding. Given the more broad use of the word "amyloid" several classes of amyloid fibrils may be distinguished. For the medical in vivo situation, and to be included in the amyloid nomenclature list, "amyloid" still means mainly extracellular tissue deposits of protein fibrils, recognized by specific properties, such as green-yellow birefringence after staining with Congo red. It should also be underlined that in vivo amyloid fibrils, in addition to the main protein contain associated compounds, particularly serum amyloid P-component (SAP) and proteoglycans, mainly heparan sulfate proteoglycan. With this definition there are presently 36 human amyloid proteins of which 14 appear only associated with systemic amyloidosis and 19 as localized forms. Three proteins can occur both as localized and systemic amyloidosis. Strictly intracellular aggregates are not included in this list.
Asunto(s)
Amiloide/clasificación , Amiloidosis/clasificación , Terminología como Asunto , Humanos , Agencias Internacionales , Sociedades CientíficasRESUMEN
The Nomenclature Committee of the International Society of Amyloidosis (ISA) met during the XVth Symposium of the Society, 3 July-7 July 2016, Uppsala, Sweden, to assess and formulate recommendations for nomenclature for amyloid fibril proteins and the clinical classification of the amyloidoses. An amyloid fibril must exhibit affinity for Congo red and with green, yellow or orange birefringence when the Congo red-stained deposits are viewed with polarized light. While congophilia and birefringence remain the gold standard for demonstration of amyloid deposits, new staining and imaging techniques are proving useful. To be included in the nomenclature list, in addition to congophilia and birefringence, the chemical identity of the protein must be unambiguously characterized by protein sequence analysis when possible. In general, it is insufficient to identify a mutation in the gene of a candidate amyloid protein without confirming the variant changes in the amyloid fibril protein. Each distinct form of amyloidosis is uniquely characterized by the chemical identity of the amyloid fibril protein that deposits in the extracellular spaces of tissues and organs and gives rise to the disease syndrome. The fibril proteins are designated as protein A followed by a suffix that is an abbreviation of the parent or precursor protein name. To date, there are 36 known extracellular fibril proteins in humans, 2 of which are iatrogenic in nature and 9 of which have also been identified in animals. Two newly recognized fibril proteins, AApoCII derived from apolipoprotein CII and AApoCIII derived from apolipoprotein CIII, have been added. AApoCII amyloidosis and AApoCIII amyloidosis are hereditary systemic amyloidoses. Intracellular protein inclusions displaying some of the properties of amyloid, "intracellular amyloid" have been reported. Two proteins which were previously characterized as intracellular inclusions, tau and α-synuclein, are now recognized to form extracellular deposits upon cell death and thus have been included in Table 1 as ATau and AαSyn.
Asunto(s)
Proteínas Amiloidogénicas/química , Amiloidosis/diagnóstico , Amiloidosis/genética , Prealbúmina/química , Precursores de Proteínas/química , Terminología como Asunto , Proteínas Amiloidogénicas/genética , Proteínas Amiloidogénicas/metabolismo , Amiloidosis/clasificación , Amiloidosis/patología , Apolipoproteína C-II/química , Apolipoproteína C-II/genética , Apolipoproteína C-II/metabolismo , Apolipoproteína C-III/química , Apolipoproteína C-III/genética , Apolipoproteína C-III/metabolismo , Biomarcadores/metabolismo , Birrefringencia , Colorantes/química , Rojo Congo/química , Expresión Génica , Guías como Asunto , Humanos , Prealbúmina/genética , Prealbúmina/metabolismo , Precursores de Proteínas/genética , Precursores de Proteínas/metabolismo , Análisis de Secuencia de Proteína , Coloración y Etiquetado/métodos , alfa-Sinucleína/química , alfa-Sinucleína/genética , alfa-Sinucleína/metabolismo , Proteínas tau/química , Proteínas tau/genética , Proteínas tau/metabolismoRESUMEN
The Nomenclature Committee of the International Society of Amyloidosis (ISA) met during the XIIIth International Symposium, May 6-10, 2012, Groningen, The Netherlands, to formulate recommendations on amyloid fibril protein nomenclature and to consider newly identified candidate amyloid fibril proteins for inclusion in the ISA Amyloid Fibril Protein Nomenclature List. The need to promote utilization of consistent and up to date terminology for both fibril chemistry and clinical classification of the resultant disease syndrome was emphasized. Amyloid fibril nomenclature is based on the chemical identity of the amyloid fibril forming protein; clinical classification of the amyloidosis should be as well. Although the importance of fibril chemistry to the disease process has been recognized for more than 40 years, to this day the literature contains clinical and histochemical designations that were used when the chemical diversity of amyloid diseases was poorly understood. Thus, the continued use of disease classifications such as familial amyloid neuropathy and familial amyloid cardiomyopathy generates confusion. An amyloid fibril protein is defined as follows: the protein must occur in body tissue deposits and exhibit both affinity for Congo red and green birefringence when Congo red stained deposits are viewed by polarization microscopy. Furthermore, the chemical identity of the protein must have been unambiguously characterized by protein sequence analysis when so is practically possible. Thus, in nearly all cases, it is insufficient to demonstrate mutation in the gene of a candidate amyloid protein; the protein itself must be identified as an amyloid fibril protein. Current ISA Amyloid Fibril Protein Nomenclature Lists of 30 human and 10 animal fibril proteins are provided together with a list of inclusion bodies that, although intracellular, exhibit some or all of the properties of the mainly extracellular amyloid fibrils.
Asunto(s)
Proteínas Amiloidogénicas/clasificación , Amiloidosis/clasificación , Rojo Congo , Histocitoquímica , Humanos , Microscopía de PolarizaciónRESUMEN
A system of amyloid fibril nomenclature based on the chemical identity of the amyloid fibril forming protein is recommended. This system has been in use for approximately 40 years, but current literature remains confused with clinical and histochemical designations used when the amyloid disease processes were poorly understood. To be designated an amyloid fibril protein, the protein must occur in tissue deposits and exhibit affinity for Congo red and green birefringence when viewed by polarisation microscopy. Furthermore, the protein must have been unambiguously characterised by protein sequence analysis (DNA sequencing in the case of familial diseases). Current nomenclature lists of 27 human and nine animal fibril proteins are provided together with a list of eight inclusion bodies that exhibit some of the properties of amyloid fibrils.
Asunto(s)
Amiloide/clasificación , Amiloidosis/clasificación , Amiloide/metabolismo , Amiloidosis/metabolismo , Animales , Humanos , Sociedades CientíficasRESUMEN
We present two families, from Spain and Portugal, with familial amyloid polyneuropathy (FAP) associated with the mutation TTRSer50Arg. This mutation was first described in two Japanese patients from independent families and later in a French-Italian patient and a Vietnamese family. The two families presented here, are the first to be diagnosed with this mutation in the Iberian Peninsula. In the patients of both families, FAP was very aggressive as they rapidly developed multiple symptoms with progressive deterioration; we emphasize the presence of severe orthostatic hypotension in the Spanish proband which confined him to a wheelchair. This proband was the first patient with this mutation to have undergone liver transplantation and results were encouraging. The mutation was detected in four patients and one disease-free relative by DNA sequencing of exon 3 and induced mutation restriction analysis. The most outstanding feature was the single base transversion A to C in codon 50 (CGT instead of AGT), whereas in both Japanese patients and the French-Italian patient it was T to G (AGG instead of AGT). To our knowledge only six FAP mutations with more than one single nucleotide mutation for the same codon have been reported to date.
Asunto(s)
Neuropatías Amiloides Familiares/genética , Mutación Puntual , Prealbúmina/genética , Adulto , Anciano , Sustitución de Aminoácidos , Secuencia de Bases , Codón/genética , ADN/genética , Femenino , Humanos , Masculino , Persona de Mediana Edad , Linaje , Portugal , EspañaRESUMEN
Between 1976 and 2003, we diagnosed 144 patients with familial amyloid polyneuropathy (FAP) in the Balearic Islands (Spain). Analysis of genetic epidemiological data from 102 confirmed patients showed 62% were men. Parental transmission was paternal in 38, maternal in 25, and unknown in 39. No family history of FAP was found in 32 patients. TTRVal30Met associated with haplotype I was present in the individuals studied. Mean age-at-onset was 45.7 years which lies between that of Sweden and those of Portugal, Japan and Brazil. Duration of FAP was of 9.7 years. Age-at-onset, age-at-death, duration and fertility were similar between sexes. Twenty-nine intergeneration familial pairs of patients were ascertained. Raw anticipation was positive in twenty-four pairs, zero in one, and negative in four. Differences greater than 9 years between age-at-onset of the first and second member were considered relevant; positive relevant anticipation was found in 76% of the whole pairs. The frequency of positive anticipation of parent-child pairs was not significantly different than those described in the Swedish and Portuguese series. Significant positive correlation in age-at-onset was confirmed in twenty-seven types of pairs supporting the hypothesis that a genetic factor may modulate age-at-onset. The Balearic focus of FAP is expanding and constitutes a public health problem.