Relevant bibliographies by topics / Amyloidosi

Academic literature on the topic 'Amyloidosi'

Author: Grafiati
Published: 9 March 2023
Last updated: 10 March 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Amyloidosi.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Amyloidosi"

1

Grzeszczak, Wladyslaw, Edward Franek, Agnieszka Szypowska, Winicjusz Filipow, Mariusz Zięba, Paweł Kabicz, and Barbara Więckowska. "Incidence of non-hereditary amyloidosis in Poland." Annales Academiae Medicae Silesiensis 75 (October 27, 2021): 99–106. http://dx.doi.org/10.18794/aams/141603.

Full text
Abstract:
WstępW pracy przedstawiono przypadki niedziedzicznej amyloidozy na podstawie danych z publicznej służby zdrowia w Polsce, obejmujących zarówno pacjentów hospitalizowanych, jak i ambulatoryjnych. Dane przedstawiono według podtypów amyloidozy rozpoznanych w okresie od 2013 r. do 2015 r.Materiał i metodyPacjenci z amyloidozą zostali wyłonieni z bazy danych Narodowego Funduszu Zdrowia. W celu zapewnienia, że zgłaszane dane dotyczące zachorowalności obejmowały tylko nowych pacjentów, osoby już wcześniej wpisane do rejestru z rozpoznaniem amyloidozy zostały wykluczone. Do badania włączono dzieci i dorosłych obojga płci. Obszar geograficzny (miejsce zamieszkania badanych) podzielono na sześć regionów. We wszystkich regionach Polski mieszkają osoby o porównywalnym genomie.WynikiW latach 2013–2015 amyloidozę stwierdzono łącznie u 287 pacjentów, z częstością 2,49 na milion osobolat. Najczęstszą z chorób była amyloidoza nieokreślona, cierpiało z jej powodu 169 pacjentów (1,46 na milion osobolat). Druga co do częstości występowania była amyloidoza ograniczona do określonego narządu – 60 pacjentów (0,52 na milion osobolat). Biorąc pod uwagę wszystkie analizowane podtypy amyloidozy, mężczyźni chorowali częściej niż kobiety. Nie stwierdzono statystycznie istotnej różnicy między zarejestrowaną zapadalnością w analizowanych regionach. Brak istotnych różnic między mężczyznami i kobietami z amyloidozą starczą.WnioskiCzęstość występowania amyloidozy w Polsce wynosi około 2,49 na milion osobolat, z nieco większym ryzykiem zachorowań u mężczyzn niż u kobiet. Badani chorowali najczęściej na amyloidozę o nieokreślonej przyczynie niezwiązaną z dziedziczeniem. Na drugim miejscu pod względem częstości występowania była amyloidoza ograniczona narządowo. Brak istotnych statystycznie różnic pomiędzy zarejestrowaną zapadalnością na amyloidozę w analizowanych regionach Polski. Nie wykazano istotnych różnic pomiędzy kobietami i mężczyznami chorującymi na amyloidozę starczą.
APA, Harvard, Vancouver, ISO, and other styles
2

Fedotov, Sergei A., Maria S. Khrabrova, Anastasia O. Anpilova, Vladimir A. Dobronravov, and Aleksandr A. Rubel. "Noninvasive Diagnostics of Renal Amyloidosis: Current State and Perspectives." International Journal of Molecular Sciences 23, no. 20 (October 21, 2022): 12662. http://dx.doi.org/10.3390/ijms232012662.

Full text
Abstract:
Amyloidoses is a group of diseases characterized by the accumulation of abnormal proteins (called amyloids) in different organs and tissues. For systemic amyloidoses, the disease is related to increased levels and/or abnormal synthesis of certain proteins in the organism due to pathological processes, e.g., monoclonal gammopathy and chronic inflammation in rheumatic arthritis. Treatment of amyloidoses is focused on reducing amyloidogenic protein production and inhibition of its aggregation. Therapeutic approaches critically depend on the type of amyloidosis, which underlines the importance of early differential diagnostics. In fact, the most accurate diagnostics of amyloidosis and its type requires analysis of a biopsy specimen from the disease-affected organ. However, absence of specific symptoms of amyloidosis and the invasive nature of biomaterial sampling causes the late diagnostics of these diseases, which leads to a delayed treatment, and significantly reduces its efficacy and patient survival. The establishment of noninvasive diagnostic methods and discovery of specific amyloidosis markers are essential for disease detection and identification of its type at earlier stages, which enables timely and targeted treatment. This review focuses on current approaches to the diagnostics of amyloidoses, primarily with renal involvement, and research perspectives in order to design new specific tests for early diagnosis.
APA, Harvard, Vancouver, ISO, and other styles
3

Bajic, Vladan P., Adil Salhi, Katja Lakota, Aleksandar Radovanovic, Rozaimi Razali, Lada Zivkovic, Biljana Spremo-Potparevic, et al. "DES-Amyloidoses “Amyloidoses through the looking-glass”: A knowledgebase developed for exploring and linking information related to human amyloid-related diseases." PLOS ONE 17, no. 7 (July 25, 2022): e0271737. http://dx.doi.org/10.1371/journal.pone.0271737.

Full text
Abstract:
More than 30 types of amyloids are linked to close to 50 diseases in humans, the most prominent being Alzheimer’s disease (AD). AD is brain-related local amyloidosis, while another amyloidosis, such as AA amyloidosis, tends to be more systemic. Therefore, we need to know more about the biological entities’ influencing these amyloidosis processes. However, there is currently no support system developed specifically to handle this extraordinarily complex and demanding task. To acquire a systematic view of amyloidosis and how this may be relevant to the brain and other organs, we needed a means to explore "amyloid network systems" that may underly processes that leads to an amyloid-related disease. In this regard, we developed the DES-Amyloidoses knowledgebase (KB) to obtain fast and relevant information regarding the biological network related to amyloid proteins/peptides and amyloid-related diseases. This KB contains information obtained through text and data mining of available scientific literature and other public repositories. The information compiled into the DES-Amyloidoses system based on 19 topic-specific dictionaries resulted in 796,409 associations between terms from these dictionaries. Users can explore this information through various options, including enriched concepts, enriched pairs, and semantic similarity. We show the usefulness of the KB using an example focused on inflammasome-amyloid associations. To our knowledge, this is the only KB dedicated to human amyloid-related diseases derived primarily through literature text mining and complemented by data mining that provides a novel way of exploring information relevant to amyloidoses.
APA, Harvard, Vancouver, ISO, and other styles
4

Galkin, Alexey P., and Evgeniy I. Sysoev. "Stress Response Is the Main Trigger of Sporadic Amyloidoses." International Journal of Molecular Sciences 22, no. 8 (April 15, 2021): 4092. http://dx.doi.org/10.3390/ijms22084092.

Full text
Abstract:
Amyloidoses are a group of diseases associated with the formation of pathological protein fibrils with cross-β structures. Approximately 5–10% of the cases of these diseases are determined by amyloidogenic mutations, as well as by transmission of infectious amyloids (prions) between organisms. The most common group of so-called sporadic amyloidoses is associated with abnormal aggregation of wild-type proteins. Some sporadic amyloidoses are known to be induced only against the background of certain pathologies, but in some cases the cause of amyloidosis is unclear. It is assumed that these diseases often occur by accident. Here we present facts and hypotheses about the association of sporadic amyloidoses with vascular pathologies, trauma, oxidative stress, cancer, metabolic diseases, chronic infections and COVID-19. Generalization of current data shows that all sporadic amyloidoses can be regarded as a secondary event occurring against the background of diseases provoking a cellular stress response. Various factors causing the stress response provoke protein overproduction, a local increase in the concentration or modifications, which contributes to amyloidogenesis. Progress in the treatment of vascular, metabolic and infectious diseases, as well as cancers, should lead to a significant reduction in the risk of sporadic amyloidoses.
APA, Harvard, Vancouver, ISO, and other styles
5

Czyżewska, Emilia. "Amyloidoses – pathogenesis, classification, diagnosis." Diagnostyka Laboratoryjna 56, no. 4 (July 9, 2021): 1–13. http://dx.doi.org/10.5604/01.3001.0015.0266.

Full text
Abstract:
Amyloidoses – also known as amyloidosis or betafibrillosis – a diverse group of diseases in which amorphous protein with a changed conformational structure is deposited extracellularly, leading to the failure of many organs. The basic classifications of amyloidoses take into account: the type of precursor protein, the division into generalized (systemic) amyloidoses, in which amyloid deposits accumulate in many organs, vessel walls and connective tissue (e.g. AL amyloidosis) and local (localized) amyloidoses – limited to only one organ (e.g. corneal amyloidosis) as well as congenital and acquired diseases. Symptoms of amyloidosis are non-specific and not very characteristic, moreover, their severity depends on the type of disease and organ involvement. The diagnosis of amyloidosis should be considered in patients with heart failure without coronary artery disease, with neuropathy, or proteinuria or hepatomegaly of unclear origin. Diagnosis of amyloidosis is based on the evaluation of tissue biopsy samples and the presence of abnormal proteins, i.e. amyloid, or on the fibrillary evaluation confirmation of the filamentous nature of amyloid deposits using electron microscopy. The next step is differential diagnosis and amyloid differential identification, which is based on immunohistochemical and immunofluorescence studies using labeled antibodies. The "gold standard" used in typing amyloidosis and identifying an amyloidogenic protein is mass spectrometry. Laboratory tests are used to assess organ involvement, which is the basis of the prognostic classification.
APA, Harvard, Vancouver, ISO, and other styles
6

Bandyopadhyay, Arghya, Shubham Bhattacharya, Barnali Maiti, and Koushik Bose. "Calcified Amyloid Tumor of Neck with Exuberant Giant Cell Reaction." Journal of Laboratory Physicians 7, no. 01 (January 2015): 061–63. http://dx.doi.org/10.4103/0974-2727.151694.

Full text
Abstract:
ABSTRACTAmyloidosis is a group of disorders characterized by an extracellular deposition of an abnormal amount of proteins in a variety of organs resulting from abnormal folding of protein. It typically presents as disseminated deposits. Tumor like localized presentation of amyloidosis in the absence of systemic amyloidosis is referred to as amyloidoma or amyloid tumor. Amyloidoma is the least common presentation of tissue amyloid deposition. Amyloidoma of soft tissue is again a very rare entity, especially in the neck region. Calcification and minimum giant cell reaction can occur in amyloidoma. However, extensive calcification and exuberant giant cell reaction in amyloidoma of soft tissue neck make it difficult to diagnose. In this report, we discuss such a rare case with its differential diagnoses.
APA, Harvard, Vancouver, ISO, and other styles
7

Yin, Hong, Nasir Alhasan, Alfonso Ciervo, and Louis Zinterhofer. "Soft Tissue Amyloidoma With Features of Plasmacytoma." Archives of Pathology & Laboratory Medicine 126, no. 8 (August 1, 2002): 969–71. http://dx.doi.org/10.5858/2002-126-0969-stawfo.

Full text
Abstract:
Abstract Soft tissue amyloidoma is rare, and soft tissue amyloidoma associated with plasmacytoma and without evidence of systemic amyloidosis is even more rare. We report a case of soft tissue amyloidoma associated with an apparently localized monoclonal proliferation of plasma cells (plasmacytoma).
APA, Harvard, Vancouver, ISO, and other styles
8

Li, Yinli, Hao Liang, Huiling Zhao, Dong Chen, Bo Liu, Thomas Fuhs, and Mingdong Dong. "Characterization of Inter- and Intramolecular Interactions of Amyloid Fibrils by AFM-Based Single-Molecule Force Spectroscopy." Journal of Nanomaterials 2016 (2016): 1–18. http://dx.doi.org/10.1155/2016/5463201.

Full text
Abstract:
Amyloids are fibrous protein aggregates defined by shared specific structural features. Abnormal accumulation of amyloid in organs leads to amyloidosis, which results in various neurodegenerative diseases. Atomic force microscopy (AFM) has proven to be an excellent tool investigating amyloids; it has been extensively utilized to characterize its morphology, assembly process, and mechanical properties. This review summarizes studies which applied AFM to detect the inter- and intramolecular interactions of amyloid fibrils and classified the influencing factors of amyloid’s nanomechanics in detail. The characteristics of amyloid fibrils driven by inter- and intramolecular interactions, including various morphologies of amyloid fibrils, self-assembly process, and the aggregating pathway, are described. Successful examples where AFM provided abundant information about inter- and intramolecular interactions of amyloid fibrils in different environments are presented. Direct force measurement of intra- or intermolecular interactions utilizing an AFM-based tool, single-molecular force spectroscopy (SMFS), is introduced. Some mechanical information such as elasticity, adhesiveness, and strength was obtained by stretching amyloid fibrils. This review helps researchers in understanding the mechanism of amyloidogenesis and exploring the properties of amyloid using AFM techniques.
APA, Harvard, Vancouver, ISO, and other styles
9

Theodorakakou, Foteini, Despina Fotiou, Meletios A. Dimopoulos, and Efstathios Kastritis. "Solid Organ Transplantation in Amyloidosis." Acta Haematologica 143, no. 4 (2020): 352–64. http://dx.doi.org/10.1159/000508262.

Full text
Abstract:
Amyloidosis comprises a diverse group of diseases characterized by misfolding of precursor proteins which eventually form amyloid aggregates and preceding intermediaries, which are deposited in target tissues causing progressive organ damage. In all forms of amyloidosis, vital organs may fail; depending on the specific amyloidosis type, this may occur rapidly or progress slowly. Beyond therapies to reduce the precursor protein (chemotherapy for light chain [AL] amyloidosis, anti-inflammatory therapy in serum A amyloid­osis [AA], and antisense RNA therapy in transthyretin amyloidosis [ATTR]), organ transplantation may also be a means to reduce amyloidogenic protein, e.g., in types of amyloid­osis in which the variant precursor is produced by the liver. Heart transplantation is a life-saving approach to the treatment of patients with advanced cardiac amyloidosis; however, amyloidosis may still be considered a contraindication to the procedure despite data supporting improved outcomes, similar to patients with other indications. Kidney transplantation is associated with particularly favorable outcomes in patients with amyloidosis, especially if the precursor protein has been eliminated. Overall, outcomes of solid organ transplantation are improving, but more data are needed to refine the selection criteria and the timing for organ transplantation, which should be performed in highly experienced centers involving multidisciplinary teams with close patient follow-up to detect amyloid recurrence.
APA, Harvard, Vancouver, ISO, and other styles
10

Wisniowski, Brendan, and Ashutosh Wechalekar. "Confirming the Diagnosis of Amyloidosis." Acta Haematologica 143, no. 4 (2020): 312–21. http://dx.doi.org/10.1159/000508022.

Full text
Abstract:
Amyloidosis is a general term for diseases characterised by the deposition of insoluble amyloid fibrils in organs or tissues, leading to organ dysfunction and, in many cases, death. Amyloid fibrils are derived from soluble precursor proteins, with the number of known amyloidogenic proteins increasing over time. The identity of the precursor protein often predicts the disease phenotype, although many of the amyloidoses have overlapping clinical features. Most patients with amyloidosis will require biopsy of an involved organ or tissue to confirm the diagnosis. Cardiac transthyretin amyloidosis, however, may be diagnosed without a biopsy provided stringent criteria are met. Where amyloid is confirmed histologically, the identity of the amyloidogenic protein must be determined, given several of the amyloidoses have disease-specific therapies. Laser capture microdissection and tandem mass spectrometry, LCM-MS, has revolutionised amyloid subtyping, being able to identify the amyloidogenic protein more reliably than antibody-based methods such as immunohistochemistry. Here we summarise the biopsy approach to amyloidosis, as well as the non-biopsy diagnosis of cardiac transthyretin amyloidosis. Proteomic and antibody-based methods for amyloid subtyping are reviewed. Finally, an algorithm for confirming the diagnosis of amyloidosis is presented.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Amyloidosi"

1

OBERTI, LUCA. "EXPLORING THE MOLECULAR AND BIOPHYSICAL MECHANISMS OF PROTEOTOXIC IMMUNOGLOBULIN LIGHT CHAINS IN AL AMYLOIDOSIS." Doctoral thesis, Università degli Studi di Milano, 2019. http://hdl.handle.net/2434/630665.

Full text
Abstract:
Herein, immunoglobulin light chains (LCs) native state was studied in the context of the pathology known as light chain amyloidosis (AL). This pathology is characterized by LCs overexpression, which leads to toxicity and aggregation into amyloid fibrils in target organs, with heart being the most affected one. Due to genetic rearrangement and somatic hypermutation, virtually, each AL patient presents a different amyloidogenic LC (Merlini, 2017). Because of such complexity, the fine molecular determinants of LC aggregation propensity and proteotoxicity are, to date, unclear; significantly, their decoding requires investigating large sets of cases. This project is aimed to unravel the molecular determinants linked with LCs toxicity. First, we screened several independent biophysical and structural properties of the LCs native state. In particular, we considered hydrophobicity, fold stability, flexibility and 3D structure. Our experimental approach considered two LCs sets called ‘H’ and ‘M’. The H set is composed of eight LCs from AL patients while the M set by LCs from multiple myeloma (MM) patients. M LCs were chosen as control since they are overexpressed as the toxic H LCs but they do not lead to toxicity or aggregation. To date, the molecular bases leading to LC proteotoxicity remain to be elucidated. Our data show that low fold stability and high protein flexibility correlate with amyloidogenic LCs, while hydrophobicity, structural rearrangements and nature of the LC dimeric association interface (as observed in seven crystal structures here presented) do not appear to play a significant role in protein aggregation. Additionally, it has been demonstrated that the LCs toxicity in vivo is linked to copper (Cu2+) (Diomede et al., 2017a) by increasing the radical oxygen species (ROS) production. We aimed our studied to clarify Cu2+ LCs interaction. Moreover, we wanted to assess whether Cu2+ is able to alter the biophysical properties of the native state to more aggregation prone states. Our findings reveal that H LCs interacts with Cu2+ with a higher affinity than M LCs and that His residues may be involved in Cu2+ binding. Indeed the affinity decreases in presence of protonated His residues. Moreover, data suggest that the interaction with Cu2+ increases the molecular flexibility and decreases the fold stability. These observations suggests that protein aggregation cannot be evaluated through one single parameters but by the co-action of several biophysical traits. Moreover, our results suggest that the presence of Cu2+ can alter the native LCs properties leading to a higher toxicity in vivo.
APA, Harvard, Vancouver, ISO, and other styles
2

Bartlam, Mark Gerrard. "Structural studies of amyloid proteins." Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342536.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

BROGGINI, LUCA. "MOLECULAR DETERMINANTS UNDERLYING PROTEIN MISFOLDING AND AGGREGATION." Doctoral thesis, Università degli Studi di Milano, 2021. http://hdl.handle.net/2434/831967.

Full text
Abstract:
Proteins have evolved to adopt distinctive and well-defined functional states under physiological conditions, either as monomers or complexes. The achievement of a three-dimensional structure allows proteins to exert their physiological functions. Nevertheless, when proteins lose – or fail to acquire – their spatial organization, they can convert into aggregated species that can be harmful to the organism. Conformational diseases gather all those pathologies characterized by the misfolding and aggregation of proteins. Indeed, while the formation and deposition of proteinaceous aggregates can be toxic to cells, the lack of active folded protein disrupts normal physiological pathways. Although considerable progresses have been made in the recent years, to date conformational diseases are still incurable. Indeed, the incomplete understanding of the causes guiding protein misfolding and aggregation prevents the development of efficient treatments. At the same time, the complexity and the diversity of the processes leading to the formation of aggregated species make the task extremely challenging. This PhD project was developed to provide a more comprehensive overview of the molecular bases underlying the conversion of soluble and functional states into aggregated and potentially toxic species. To reach such aims, we applied an integrative approach on two model systems, neuroserpin (NS) and beta-2 microglobulin (2m). In particular, we combined a series of biophysical, biochemical and structural techniques to study these two proteins which have been largely used as model systems for serpin polymerization and amyloid formation, respectively. We found that protein misfolding and aggregation processes depend on several molecular properties, including primary sequence, denatured state compactness, thermal stability, ability to form oligomers under physiological conditions, and the presence of post-translation modifications. The data presented in this PhD thesis add valuable information to depict the complex framework of protein misfolding and aggregation.
APA, Harvard, Vancouver, ISO, and other styles
4

RELLA, VALERIA. "AMILOIDOSI CARDIACA ANALISI DI PREVALENZA IN DUE STUDI MULTICENTRICI ITALIANI." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2022. http://hdl.handle.net/10281/366496.

Full text
Abstract:
Tra i pazienti con diagnosi iniziale di cardiomiopatia ipertrofica afferiti a Centri di Riferimento per le Cardiomiopatie, l’AC è la malattia non riconosciuta più comune con una prevalenza complessiva del 9%, e che aumenta con l'età (dall'1% nella fascia di età tra i 40-49 anni al 26% sopra gli 80 anni). Nella popolazione generale ≥55 anni più del 7% ha almeno un reperto ecocardiografico suggestivo di AC e l’ispessimento del setto interatriale è quello più frequente. I pazienti con elevato sospetto di AC (≥3 reperti) rappresentano l’1% della popolazione generale e il 4,9% di quelli con cuore non dilatato, ipertrofico e con FE normale.
Among patients with initial diagnosis of HCM, cardiac amiloidosis has a prevalence of 9% and it increases with age. In the general population > 55 yo more than 7% has echocardiographic suspicion of the disease and echocardiography has an important role in the early diagnosis of the disease
APA, Harvard, Vancouver, ISO, and other styles
5

Moreira, Carolina Lavigne. "Epidemiologia mutacional da polineuropatia amiloidótica familiar transtiretina em um serviço brasileiro terciário de neuropatias periféricas." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/17/17140/tde-30032017-142719/.

Full text
Abstract:
Introdução: A amiloidose transtiretina é uma doença autossômica dominante decorrente de uma proteína transtiretina (TTR) variante, que sofre uma mudança conformacional e origina um tetrâmero de TTR instável, passo que é decisivo para o início da formação dos depósitos amilóides em diferentes órgãos e tecidos. Na maioria dos pacientes, o sistema nervoso periférico é o alvo principal, resultando na polineuropatia amiloidótica familiar transtiretina (TTR-FAP), classicamente uma neuropatia sensitivo-motora e autonômica progressiva, evoluindo para o óbito em aproximadamente 10 anos. A mutação de ponto mais frequente no mundo, incluindo o Brasil, é a TTRVal30Met, entretanto mais de 100 mutações de ponto diferentes já foram descritas. Objetivos: descrever a epidemiologia mutacional do gene TTR na polineuropatia amiloidótica familiar e correlacionar estas mutações com seus achados clínicos e eletroneuromiográficos. Métodos: estudo de coorte, descritivo e retrospectivo de um grupo de pacientes brasileiros encaminhados para o serviço de neurogenética do HC da FMRP-USP para investigação de neuropatia periférica, cujo estudo genético identificou uma mutação no gene TTR, com posterior análise transversal dos resultados obtidos entre os subgrupos com as diferentes mutações. Resultados: um total de 128 pacientes tiveram uma mutação de ponto no gene TTR identificada, dos quais 12 (9,4%) pacientes apresentaram uma mutação não TTRVal30Met, incluindo 4 patogênicas (6 pacientes, 4,7%) e 2 não patogênicas (6 pacientes, 4,7%). A mutações não TTRVal30Met patogênicas foram TTRAsp38Tyr (2 pacientes), TTRIle107Val (2 pacientes), TTRVal71Ala (1 paciente) e TTRVal122Ile (1 paciente). Dentre as mutações não patogênicas, foram encontradas TTRGly6Ser (5 pacientes) e TTRThr119Thr (1 paciente). A mutação TTRVal30Met estava presente em 116 (90,6%) pacientes, dos quais 52 possuíam dados clínicos e eletroneuromiográficos completos: 39 (75%) tiveram início precoce e 13 (25%), início tardio. O grupo de início precoce apresentou-se como a forma clássica da PAF-TTR, sem predileção de gênero (homens: 53,8%), manifestação inicial como neuropatia de fibras finas e autonômica (82,1%) e história familiar positiva (90,3%). A ENMG estava normal em 36,7% destes pacientes. O envolvimento cardiovascular foi caracterizado mais frequentemente por alterações da condução cardíaca (84,2%), sendo menos prevalente a cardiomiopatia (11,1%). Por outro lado, o grupo de início tardio mostrou uma predominância do sexo masculino (92,3%), presença de sintomas motores na primeira consulta (38,5%), resultando numa neuropatia sensitivo-motora com acometimento de fibras grossas e história familiar negativa (69,2%). Todos apresentaram neuropatia sensitivo-motora na ENMG. Neste grupo, a cardiomiopatia estava presente em 71,4% dos pacientes. Todos os pacientes, em ambos os grupos, tiveram disautonomia em algum momento do seu seguimento clínico. Conclusões: no nosso estudo aproximadamente 5% dos pacientes com FAP-TTR tinham uma mutação não TTRVal30Met, demonstrando a importância do sequenciamento do gene TTR em pacientes com história clínica sugestiva e screening negativo para a mutação TTR Val30Met. Além disso, os pacientes brasileiros com FAP-TTRVal30Met apresentaram achados clínicos e eletroneuromiográficos similares as populações descritas com esta mutação em outros países.
Background: Transthyretin amyloidosis is an autossomal dominant disease caused by variant transthyretin, that is misfolded, originating a unstable transthyretin tetramer, a rate-limiting step in the formation of the amyloid deposits in different organs and tissues. In most patients, the peripheral nervous system is the main target, leading to transtyretin familial amyloid neuropathy (TTR-FAP), classically characterized as a progressive sensory-motor and autonomic neuropathy, that leads to death in about 10 years. TTRVal30Met is the most frequent point mutation worldwide, including Brazil, but more than 100 different point mutations has been described. Objectives: describe the mutational epidemiology of TTR gene in TTR-FAP and characterize its clinical and electrophysiological findings. Methods: a descriptive and retrospective study of a group of Brazilian patients forwarded to the Neurogenetics or Peripheral Nerve Clinics from FMRP-USP whose etiological investigation identified a mutation in the TTR gene. A cross-sectional analysis evaluating the subgroups with different mutations was also carried on. Results: we identified one hundred and twenty eight patients carrying a TTR point mutation, of whom 12 (9,4%) harbored a non-Val30Met mutation, including 4 pathogenic (6 patients, 4,7%) and 2 non-pathogenic abnormalities (6 patients, 4,7%). The non Val30Met pathogenic mutations were TTRAsp38Tyr (2 patients), TTRIle107Val (2 patients), TTRVal71Ala (1 patient) and TTRVal122Ile (1 patient). Among the non-pathogenic mutations, we found the TTRGly6Ser (5 patients) and the TTRThr119Thr (1 patient). The TTRVal30Met mutation was present in 116 (90,6%) patients, of whom 52 had a complete clinical and neurophysiological data: 39 (75%) with early-onset and 13(25%) with late-onset neuropathies. The early-onset group presented as the classic TTRFAP, with no gender predominance (male: 53,8%), the first manifestations were those of a small fiber sensory and autonomic neuropathy (82,1%) and a highly positive family history (90,3%). EMG was normal in 36,7% of these patients. The cardiovascular involvement was characterized by frequent ECG abnormalities (84,2%), less often associated with cardiomayopathy (11,1%). On the other hand, the late-onset TTRVal30Met showed a male predominance (92,3%), presence of motor complaints in the first evaluation (38,5%) resulting in a sensory-motor polyneuropathy with large fiber involvement and a negative family history (69,2%). All patients presented a sensory and motor neuropathy on EMG examination. In this group, cardiomiopathy was frequently associated with the neuropathy (71,4%). All patients, in both groups, had autonomic symptoms at some point in clinical follow up. Conclusions: In our study almost 5% of the patients with TTR-FAP have a non Val30Met pathogenic mutation, highlighting the importance of sequecing the whole TTR gene in patients with a sugestive clinical history and negative screening for TTRVal30Met mutation. In adition, the Brazilian patients we studied with early and late onset TTR-FAP, present similar findings to TTRVal30Met populations from other countries submitted to similar studies.
APA, Harvard, Vancouver, ISO, and other styles
6

Herranz-Trillo, Fatima. "Disentangling structural complexity in proteins by decomposing SAXS data with chemometric approaches." Thesis, Montpellier, 2017. http://www.theses.fr/2017MONTT044/document.

Full text
Abstract:
De nombreux systèmes biologiques sont intrinsèquement polydispersés, présentant de multiples espèces coexistantes, de taille, de forme ou de conformation différentes (c'est-à-dire, mélanges oligomèriques, des complexes faiblement liés se dissociant en composantes individuelles ou des espèces apparaissant lors de processus amyloïdogéniques). L'étude de tels systèmes complexes est une tâche difficile en raison de l'instabilité des espèces concernées, de leurs concentrations relatives faibles et interdépendantes et des difficultés rencontrées pour l'isolation des composantes pures. Dans cette thèse, j'ai développé des approches méthodologiques pour appliquer la diffusion des rayons X aux petits angles (SAXS), une technique de biologie structurale, à l'étude de systèmes polydispersés. SAXS est une technique additive et par conséquent, le diagramme de diffusion mesuré pour un échantillon polydispersé correspond à la somme pondérée en concentration des contributions de chacune des composantes individuelles du mélange. Cependant, la décomposition des données de SAXS en des spectres spécifiques des espèces et de leurs concentrations relatives est extrêmement laborieuse et ambigue. Dans cette thèse, je présente d'abord une approche objective pour solidement décomposer les jeux de données de SAXS en composantes individuelles. Cette approche adapte la méthode chimiométrique « Multivariable Curve Resolution Alternate Least Squares » (MCR-ALS) aux spécificités des données de SAXS. Notre méthode permet une décomposition rigoureuse et robuste des données de SAXS en introduisant simultanément différentes représentations de ces données et par conséquent, en mettant l'accent sur des changements moléculaires à différentes plages de temps et de résolution structurale. Nous avons appliqué cette approche, que nous appelons COSMiCS (Analyse structurelle objective complexe des systèmes multi-composants) pour étudier deux systèmes polydispersés: la fibrillation des protéines, et les fluctuations conformationnelles de protéines grâce à l'analyse de données obtenues à l'aide d’une technique de couplage de chromatographie d'exclusion de taille (SEC) avec le ligne de SAXS (SEC-SAXS). L'importance d'étudier les processus de fibrillation réside dans leur implication dans des pathologies amyloïdogéniques telles que les maladies de Parkinson ou d'Alzheimer. Il existe de fortes indications que les espèces oligomériques solubles, et non les fibrilles matures, sont la cause principale de la cytotoxicité et des dommages neuronaux. Cette observation souligne l'importance de caractériser les premiers stades des processus de fibrillation. Notre approche COSMiCS a permis d'étudier les processus amyloïdogéniques de l'insuline et du mutant familial E46K de l'α-synucléine, une protéine associée à la maladie de Parkinson. Cette analyse permet la caractérisation structurale des espèces présentes (y compris les espèces oligomériques) et la caractérisation cinétique de leurs transformations.La deuxième partie de la thèse est consacrée à l'utilisation de COSMiCS pour analyser des données de SEC-SAXS. Le SEC-SAXS est extrêmement populaire et a été implémenté sur plusieurs lignes de SAXS à travers le monde. En utilisant des données synthétiques, je démontre la capacité des approches chimiométriques à décomposer des profils chromatographiques complexes. À l'aide de cette approche, j'ai décomposé l’ensemble des données SEC-SAXS mesurés pour la Prolyl OligoPeptidase (POP).En résumé, cette thèse présente une nouvelle approche chimiométrique qui peut être généralement appliquée à tout mélange macromoléculaire pouvant subir une modifacation de son équilibre et pouvant être abordé par SAXS. Les complexes biomoleculaires transitoires, les processus de repliement, les réarrangements structuraux dépendants d’un ligand ou la formation de grands ensembles supramoleculaires peuvent être sondés de façon structurale en utilisant l'approche COSMiCS
Many biological systems are inherently polydisperse, presenting multiple coexisting species differing in size, shape or conformation (i.e. oligomeric mixtures, weakly bound complexes, and species appearing along amyloidogenic processes). The study of such complex systems is challenging due to the instability of the species involved, their low and interdependent relative concentrations, and the difficulties to isolate the pure components. In this thesis, I have developed methodological approaches to apply Small-Angle X-ray Scattering (SAXS), a low-resolution structural biology technique, to the study of polydisperse systems. As an additive technique, the SAXS pattern measured for a polydisperse sample corresponds to the concentration-weighted sum of the contributions from each of the individual components. However, decomposition of SAXS data into species-specific spectra and relative concentrations is laborious and burdened by ambiguity. In this thesis, I present an approach to decompose SAXS datasets into the individual components. This approach adapts the chemometrics Multivariate Curve Resolution Alternating Least Squares (MCR-ALS) method to the specificities of SAXS data. Our method enables the rigorous and robust decomposition of SAXS data by simultaneously introducing different representations of these data and, consequently, emphasizing molecular changes at different time and structural resolution ranges. We have applied this approach, which we name COSMiCS (Complex Objective Structural analysis of Multi-Component Systems), to study two polydisperse systems: amyloid fibrillation by analysing time-dependent SAXSdata, and conformational fluctuations through the analysis of data obtained using on-line size-exclusion chromatography coupled to SAXS (SEC-SAXS). The importance of studying fibrillation processes lies in their implication in amyloidogenic pathologies such as Parkinson’s or Alzheimer’s diseases. There exist strong indications that soluble oligomeric species, and not mature fibrils, are the main cause of cytotoxicity and neuronal damage emphasizing the importance of characterizing early stages of fibrillation. The first application of our COSMiCS approach has allowed the study of the amyloidogenic mechanisms of insulin and the familial mutant E46K of ↵-synuclein, a Parkinson’s disease related protein. The analysis enables the structural characterization of all the species present as well as their kinetic transformations. The second part of the thesis is dedicated to the use of COSMiCS to analyze on-line SEC-SAXS experiments. Using synthetic data, I demonstrate the capacity of chemometric approaches to decompose complex chromatographic profiles. Using this approach, I have studied the conformational fluctuations in prolyl oligopeptidase (POP), a protein related to synaptic functions and neuronal development. In summary, this thesis presents a novel chemometrics approach that can be generally applied to any macromolecular mixture with a tuneable equilibrium that is amenableto SAXS. Transient biomolecular complexes, folding processes, or ligand-dependent structural rearrangements can be probed structurally using COSMiCS
APA, Harvard, Vancouver, ISO, and other styles
7

Hazenberg, Bouke Pier Cornelis. "Diagnostic studies in amyloidosis." [S.l. : Groningen : s.n. ; University Library of Groningen] [Host], 2007. http://irs.ub.rug.nl/ppn/30519349X.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Slamova, I. "Modelling amyloidosis in mice." Thesis, University College London (University of London), 2016. http://discovery.ucl.ac.uk/1534595/.

Full text
Abstract:
Amyloidosis is a group of disorders in which specific soluble proteins convert into insoluble extracellular fibrillar deposits. Certain mutations in amyloid prone proteins result in aggressive forms of the disease. β2-microglobulin (β2m), a cell surface protein and transthyretin (TTR), a normal plasma protein, are inherently amyloidogenic. In patients undergoing long-term dialysis, ineffective clearance of β2m from the plasma results in sustained increase of its concentration and its deposition as amyloid. Wild type TTR is the amyloid precursor in senile systemic amyloidosis, a cause of heart failure in the elderly, and various different mutations in the human TTR gene cause the autosomal dominant conditions familial amyloid polyneuropathy and familial amyloid cardiomyopathy. The D76N β2m variant causes highly penetrant hereditary systemic amyloidosis. Similarly, the S52P TTR variant also causes aggressive amyloidosis which is characterised by prominent cardiac ATTR deposits. Animal models for Aβ2m amyloidosis and ATTR amyloidosis have long been sought to enable a better understanding of disease mechanisms and for validation of diagnostic methods and treatments, but previous attempts to model these diseases in vivo have met with limited or no success. The aims of this project were to generate mouse models of: (1) Aβ2m amyloidosis and (2) cardiac ATTR amyloidosis by transgenic expression of these highly amyloidogenic variants. In the work presented here, hβ2mD76N transgenic mice and hTTRS52P transgenic mice were generated. Despite expressing high plasma concentrations of the amyloidogenic proteins, the mice did not spontaneously develop amyloidosis. After priming amyloid deposition with pre formed amyloid fibrils, the hβ2mD76N transgenic mice failed to develop amyloid deposits. It is notable that most of the β2m circulates bound in a complex, potentially limiting the availability of free β2m monomers for conversion into fibrils. In the hTTRS52P transgenic mice, priming of amyloid deposition with amyloid fibrils led to consistent and reproducible development of cardiac ATTR amyloidosis.
APA, Harvard, Vancouver, ISO, and other styles
9

Richon, Jacques. "Amyloidose pulmonaire nodulaire multiple /." [S.l : s.n.], 1985. http://www.ub.unibe.ch/content/bibliotheken_sammlungen/sondersammlungen/dissen_bestellformular/index_ger.html.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Getmans’ka, V. "Amyloidosis in the cardiovascular system." Thesis, Sumy State University, 2016. http://essuir.sumdu.edu.ua/handle/123456789/45034.

Full text
Abstract:
In the most industrialized countries with a high degree of urbanization (including Ukraine), the leading cause of morbidity and mortality is occupied by diseases of the cardiovascular system. Detection of amyloidosis is prognostically the most serious complication for patients with various diseases of the cardiovascular system, causes the development of functional organ failure and patient's death. The aim of the work is a detailed study of amyloidosis problems, especially its etiology and pathogenesis.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Amyloidosi"

1

Marrink, Jan, and Martin H. Van Rijswijk, eds. Amyloidosis. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4309-4.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Glenner, George G., Elliott F. Osserman, Earl P. Benditt, Evan Calkins, Alan S. Cohen, and Dorothea Zucker-Franklin, eds. Amyloidosis. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Gertz, Morie A., and S. Vincent Rajkumar, eds. Amyloidosis. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-631-3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

1927-, Glenner George G., ed. Amyloidosis. New York: Plenum Press, 1986.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
5

Jan, Marrink, and Rijswijk Martin Henri van, eds. Amyloidosis. Dordrecht: M. Nijhoff, 1986.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
6

Thomas, Bardin, Brancaccio Diego, and Gejyo Fumitake, eds. Dialysis amyloidosis. Milan: Wichtig Editore, 1989.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
7

International, Symposium on Amyloidosis (10th 2004 Tours France). Amyloid and amyloidosis. Boca Raton: CRC Press, 2004.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
8

Isobe, Takashi, Shukuro Araki, Fumiya Uchino, Shozo Kito, and Eiro Tsubura, eds. Amyloid and Amyloidosis. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4757-0298-9.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

1935-, Isobe Takashi, ed. Amyloid and amyloidosis. New York: Plenum Press, 1988.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
10

Natvig, Jacob B., Øystein Førre, Gunnar Husby, Anne Husebekk, Bjørn Skogen, Knut Sletten, and Per Westermark, eds. Amyloid and Amyloidosis 1990. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Amyloidosi"

1

Akpolat, Tekin, and Seza Ozen. "Amyloidosis." In Textbook of Clinical Pediatrics, 1721–23. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-02202-9_173.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Gertz, Morie A., and Steven R. Zeldenrust. "Amyloidosis." In Multiple Myeloma, 265–82. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-8520-9_22.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Gillmore, Julian David, and Helen J. Lachmann. "Amyloidosis." In Practical Nephrology, 311–22. London: Springer London, 2014. http://dx.doi.org/10.1007/978-1-4471-5547-8_29.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Gloster, Hugh Morris, Lauren E. Gebauer, and Rachel L. Mistur. "Amyloidosis." In Absolute Dermatology Review, 141–43. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-03218-4_38.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Order, Stanley E., and Sarah S. Donaldson. "Amyloidosis." In Radiation Therapy of Benign Diseases, 18. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-58719-1_11.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Frangione, Blas. "Amyloidosis." In Molecular Mechanisms of Aging, 176–84. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-84224-5_13.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Bartges, Joe, and Jonathan Wall. "Amyloidosis." In Nephrology and Urology of Small Animals, 547–54. West Sussex, UK: John Wiley & Sons, Ltd., 2014. http://dx.doi.org/10.1002/9781118785546.ch54.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Dancygier, Henryk. "Amyloidosis." In Clinical Hepatology, 1105–9. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-04519-6_33.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Raibagkar, Pooja, and Nagagopal Venna. "Amyloidosis." In Neurorheumatology, 249–58. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-16928-2_27.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Fry, Lionel, Fenella T. Wojnarowska, and Parvin Shahrad. "Amyloidosis." In Illustrated Encyclopedia of Dermatology, 17–20. Dordrecht: Springer Netherlands, 1985. http://dx.doi.org/10.1007/978-94-010-9390-3_3.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Amyloidosi"

1

Nastev, A., R. Birk, and BA Stuck. "Dysphonie: Differentialdiagnose Amyloidose." In Abstract- und Posterband – 90. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Digitalisierung in der HNO-Heilkunde. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1685576.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Korkmaz, Pelin, Murat Kiyik, Aysin Durmaz, Naciye Mutlu, Huseyin Cem Tigin, Halide Nur Ürer, and Kemal Karapinar. "Primary Pulmonary Amyloidosis." In ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa4118.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Nastev, A., R. Birk, and BA Stuck. "Dysphonia: differential diagnosis amyloidosis." In Abstract- und Posterband – 90. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Digitalisierung in der HNO-Heilkunde. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1685606.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Kühl, B., S. Gross, U. Siebert, and P. Wohlsein. "Systemische Amyloidose bei einer Kegelrobbe." In 64. Jahrestagung der Fachgruppe Pathologie der Deutschen Veterinärmedizinischen Gesellschaft. Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0041-1729401.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Chung, P., A. Fong, and B. Yaghmour. "Asymptomatic but Lethal Systemic Amyloidosis." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a1737.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Albuquerque, E. L., U. L. Fulco, and L. R. da Silva. "Biosensors to Probe Amyloidosis-Like Diseases." In 2013 29th Southern Biomedical Engineering Conference (SBEC 2013). IEEE, 2013. http://dx.doi.org/10.1109/sbec.2013.89.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Moawad, A., J. Ciancarelli, and A. Daly. "Amyloidosis and Metoclopramide, A Fatal Complication?" In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a1730.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Lourenço, Gustavo Roberto, Rita de Cássia Menin, Iane Tamara Dondé, Patrícia Milani de Moraes, Carlos Augusto Rodrigues Padilha, Juliana de Jesus Boscolo, Renata Vaz de Oliveira, Danielly Dantas Pimentel, and Maria Juliana da Silva Almeida. "HYPERIMMUNOGLOBULIN D SYNDROME WITH SECONDARY AMYLOIDOSIS." In SBR 2021 Congresso Brasileiro de Reumatologia. Sociedade Brasileira de Reumatologia, 2021. http://dx.doi.org/10.47660/cbr.2021.1884.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Kos, M., K. Geibler, K. Ratheiser, I. Pabinger, Ch Korninger, and K. Lechner. "ACQUIRED FACTOR X DEFICIENCY IN MULTIPLE MYELOMA:A COMPLETE RESPONSE TO CHEMOTHERAPY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643292.

Full text
Abstract:
A 64 year old women without any previous history of bleeding diathesis presented with bone pain and gastrointestinal bleeding. An isolated severe factor X deficiency (factor X activity 0.5%, factor X antigen less than 12.5%) was found. No inhibitor that inactivated factor X in vitro or interfered with factor X assay could be demonstrated. Substitution therapy with a prothrombin complex preparation containing factor X (PPSB Biotest) was given. Factor X recovery in the first 2 days was lower than expected (below 20%) and half life of factor X was shortened (150 minutes). Subsequently, a diagnosis of multiple myeloma (light chain myeloma, type kappa) was made. Amyloidosis was excluded by electronmicroscopic examination of rectum biopsies. Chemotherapy according to the M2 protocol (Case et al) was initiated. Factor X recovery improved dramatically within 2 weeks and there was a continuous increase of factor X activity and antigen during chemotherapy. After 6 courses a complete haematological remission (less than 5% plasma cells in the bone marrow, disappearance of light chains) was obtained and factor X activity and antigen returned to normal.Isolated factor X deficiency is a wellknown complication of amyloidosis. To our knowledge, this is the first case of factor X deficiency in multiple myeloma without amyloidosis. The complete normalization of factor X after successful chemotherapy indicates that plasma cell proliferation may have been the cause of the factor X deficiency. Binding of factor X to plasma cells containing light chains could be a possible explanation, and we are currently examining this hypothesis.
APA, Harvard, Vancouver, ISO, and other styles
10

Azevedo, Fernanda Reis de, Michael Polydefkis, Simina Ticau, David Erbe, Anastasia McManus, Emre Aldinc, David Adams, Mary Reilly, Akshay Vaishnaw, and Paul Nio. "Neurofilament Light Chain (NfL) as a Potential Biomarker of Treatment Response in Hereditary TransthyretinMediated (hATTR) Amyloidosis: Patisiran Global OLE Study." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.200.

Full text
Abstract:
Introduction: Patisiran is approved for the treatment of hATTR amyloidosis with polyneuropathy and its long-term efficacy/safety is being studied in a Global OLE. Plasma biomarkers are being investigated for utility in facilitating earlier diagnosis and monitoring disease /treatment response. Objective: Evaluate long-term change in neurofilament light chain (NfL) levels in response to patisiran in patients enrolled in the Global Open-Label Extension (OLE) study. Methods: NfL plasma levels were measured in duplicate in healthy controls and patients with ATTRv amyloidosis with polyneuropathy using the Quanterix Simoa platform. Patient samples were analyzed from the APOLLO study at baseline and 18 months, and also measured at 12 and 24 months following APOLLO in patients who rolled into the Global OLE. Results: NfL levels at APOLLO baseline were 63.2 (placebo) and 72.1 pg/ mL (patisiran). NfL increased during APOLLO in the placebo group (99.5 pg/mL), whereas a significant decrease was observed at 18 months following patisiran (48.8 pg/mL). Reduced NfL levels were maintained in the APOLLO-patisiran group through 24 months of additional patisiran treatment in the Global OLE (44.0 pg/mL), consistent with maintained improvement in mNIS+7. Upon initiation of patisiran in the Global OLE, the APOLLO-placebo group experienced a reduction in NfL levels through 24 months (44.2 pg/mL), reaching a similar level to the APOLLO-patisiran group. Conclusions: NfL may serve as a biomarker of active nerve damage and polyneuropathy, making it useful as a potential biomarker of disease progression, treatment response and for earlier diagnosis of polyneuropathy in patients with ATTRv amyloidosis and monitoring disease.
APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "Amyloidosi"

1

Li, Juan, Xiaohong Wang, and Xin Gao. Diagnosis for Chinese patients with Light Chain Amyloidosis: A scoping review. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, October 2022. http://dx.doi.org/10.37766/inplasy2022.10.0096.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Sun, Chunyan, Xiaohong Wang, Bin Wang, Renyi Zhang, Lingjie Xu, and Jian Li. Efficacy and safety of intravenous Daratumumab for patients with AL Amyloidosis: A systematic review. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, June 2021. http://dx.doi.org/10.37766/inplasy2021.6.0054.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Fu, Chengcheng, Xiaohong Wang, Bin Wang, Lingjie Xu, and Wenming Chen. The clinical characteristics of immunoglobulin light chain amyloidosis in Chinese population: A systematic scoping review. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, September 2021. http://dx.doi.org/10.37766/inplasy2021.9.0086.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Lu, Jin, Xiaohong Wang, Xin Gao, and Bin Wang. Treatment and outcomes of Chinese patients with AL Amyloidosis: a scoping review and meta analysis. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, October 2021. http://dx.doi.org/10.37766/inplasy2021.10.0096.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Elmann, Anat, Orly Lazarov, Joel Kashman, and Rivka Ofir. therapeutic potential of a desert plant and its active compounds for Alzheimer's Disease. United States Department of Agriculture, March 2015. http://dx.doi.org/10.32747/2015.7597913.bard.

Full text
Abstract:
We chose to focus our investigations on the effect of the active forms, TTF and AcA, rather than the whole (crude) extract. 1. To establish cultivation program designed to develop lead cultivar/s (which will be selected from the different Af accessions) with the highest yield of the active compounds TTF and/or achillolide A (AcA). These cultivar/s will be the source for the purification of large amounts of the active compounds when needed in the future for functional foods/drug development. This task was completed. 2. To determine the effect of the Af extract, TTF and AcA on neuronal vulnerability to oxidative stress in cultured neurons expressing FAD-linked mutants.Compounds were tested in N2a neuroblastoma cell line. In addition, we have tested the effects of TTF and AcA on signaling events promoted by H₂O₂ in astrocytes and by β-amyloid in neuronal N2a cells. 3. To determine the effect of the Af extract, TTF and AcA on neuropathology (amyloidosis and tau phosphorylation) in cultured neurons expressing FAD-linked mutants. 4. To determine the effect of A¦ extract, AcA and TTF on FAD-linked neuropathology (amyloidosis, tau phosphorylation and inflammation) in transgenic mice. 5. To examine whether A¦ extract, TTF and AcA can reverse behavioral deficits in APPswe/PS1DE9 mice, and affect learning and memory and cognitive performance in these FAD-linked transgenic mice. Background to the topic.Neuroinflammation, oxidative stress, glutamate toxicity and amyloid beta (Ab) toxicity are involved in the pathogenesis of Alzheimer's diseases. We have previously purified from Achilleafragrantissimatwo active compounds: a protective flavonoid named 3,5,4’-trihydroxy-6,7,3’-trimethoxyflavone (TTF, Fl-72/2) and an anti-inflammatory sesquiterpenelactone named achillolide A (AcA). Major conclusions, solutions, achievements. In this study we could show that TTF and AcA protected cultured astrocytes from H₂O₂ –induced cell death via interference with cell signaling events. TTF inhibited SAPK/JNK, ERK1/2, MEK1 and CREBphosphorylation, while AcA inhibited only ERK1/2 and MEK1 phosphorylation. In addition to its protective activities, TTF had also anti-inflammatory activities, and inhibited the LPS-elicited secretion of the proinflammatorycytokinesInterleukin 6 (IL-6) and IL-1b from cultured microglial cells. Moreover, TTF and AcA protected neuronal cells from glutamate and Abcytotoxicity by reducing the glutamate and amyloid beta induced levels of intracellular reactive oxygen species (ROS) and via interference with cell signaling events induced by Ab. These compounds also reduced amyloid precursor protein net processing in vitro and in vivo in a mouse model for Alzheimer’s disease and improvedperformance in the novel object recognition learning and memory task. Conclusion: TTF and AcA are potential candidates to be developed as drugs or food additives to prevent, postpone or ameliorate Alzheimer’s disease. Implications, both scientific and agricultural.The synthesis ofAcA and TTF is very complicated. Thus, the plant itself will be the source for the isolation of these compounds or their precursors for synthesis. Therefore, Achilleafragrantissima could be developed into a new crop with industrial potential for the Arava-Negev area in Israel, and will generate more working places in this region.
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Amyloidosi' for particular source types:
Journal articles Dissertations / Theses Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography