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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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).
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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.
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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.
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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.
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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.
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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.
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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.
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Lohani, Sadichhya, Emily Schuiteman, Lohit Garg, Dhiraj Yadav, and Sami Zarouk. "Apolipoprotein C-II Deposition Amyloidosis: A Potential Misdiagnosis as Light Chain Amyloidosis." Case Reports in Nephrology 2016 (2016): 1–5. http://dx.doi.org/10.1155/2016/8690642.
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Hereditary amyloidoses are rare and pose a diagnostic challenge. We report a case of hereditary amyloidosis associated with apolipoprotein C-II deposition in a 61-year-old female presenting with renal failure and nephrotic syndrome misdiagnosed as light chain amyloidosis. Renal biopsy was consistent with amyloidosis on microscopy; however, immunofluorescence was inconclusive for the type of amyloid protein. Monoclonal gammopathy evaluation revealed kappa light chain. Bone marrow biopsy revealed minimal involvement with amyloidosis with kappa monotypic plasma cells on flow cytometry. She was started on chemotherapy for light chain amyloidosis. She was referred to the Mayo clinic where laser microdissection and liquid chromatography mass spectrometry detected high levels of apolipoprotein C-II, making a definitive diagnosis. Apolipoprotein C-II is a component of very low-density lipoprotein and aggregates in lipid-free conditions to form amyloid fibrils. The identification of apolipoprotein C-II as the cause of amyloidosis cannot be solely made with routine microscopy or immunofluorescence. Further evaluation of biopsy specimens with laser microdissection and mass spectrometry and DNA sequencing of exons should be done routinely in patients with amyloidoses for definitive diagnosis. Our case highlights the importance of determining the subtype of amyloidosis that is critical for avoiding unnecessary therapy such as chemotherapy.
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Guan, Jian, Shikha Mishra, Rodney H. Falk, and Ronglih Liao. "Current perspectives on cardiac amyloidosis." American Journal of Physiology-Heart and Circulatory Physiology 302, no. 3 (February 2012): H544—H552. http://dx.doi.org/10.1152/ajpheart.00815.2011.
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Amyloidosis represents a group of diseases in which proteins undergo misfolding to form insoluble fibrils with subsequent tissue deposition. While almost all deposited amyloid fibers share a common nonbranched morphology, the affected end organs, clinical presentation, treatment strategies, and prognosis vary greatly among this group of diseases and are largely dependent on the specific amyloid precursor protein. To date, at least 27 precursor proteins have been identified to result in either local tissue or systemic amyloidosis, with nine of them manifesting in cardiac deposition and resulting in a syndrome termed “cardiac amyloidosis” or “amyloid cardiomyopathy.” Although cardiac amyloidosis has been traditionally considered to be a rare disorder, as clinical appreciation and understanding continues to grow, so too has the prevalence, suggesting that this disease may be greatly underdiagnosed. The most common form of cardiac amyloidosis is associated with circulating amyloidogenic monoclonal immunoglobulin light chain proteins. Other major cardiac amyloidoses result from a misfolding of products of mutated or wild-type transthyretin protein. While the various cardiac amyloidoses share a common functional consequence, namely, an infiltrative cardiomyopathy with restrictive pathophysiology leading to progressive heart failure, the underlying pathophysiology and clinical syndrome varies with each precursor protein. Herein, we aim to provide an up-to-date overview of cardiac amyloidosis from nomenclature to molecular mechanisms and treatment options, with a particular focus on amyloidogenic immunoglobulin light chain protein cardiac amyloidosis.
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Musetti, Veronica, Francesco Greco, Vincenzo Castiglione, Alberto Aimo, Cataldo Palmieri, Dario Genovesi, Assuero Giorgetti, et al. "Tissue Characterization in Cardiac Amyloidosis." Biomedicines 10, no. 12 (November 28, 2022): 3054. http://dx.doi.org/10.3390/biomedicines10123054.
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Cardiac amyloidosis (CA) has long been considered a rare disease, but recent advancements in diagnostic tools have led to a reconsideration of the epidemiology of CA. Amyloid light-chain (AL) and transthyretin (ATTR) amyloidoses are the most common forms of cardiac amyloidosis. Due to the distinct treatments and the different prognoses, amyloid typing is crucial. Although a non-biopsy diagnosis can be obtained in ATTR amyloidosis when certain diagnostic criteria are fulfilled, tissue characterization still represents the gold standard for the diagnosis and typing of CA, particularly in AL amyloidosis. The present review focuses on the status of tissue characterization in cardiac amyloidosis, from histochemistry to immunohistochemistry and mass spectrometry, as well as on its future directions.
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Alkukhun, Abedalrazaq, Issa Rezek, Saber Ghiassi, Xuchen Zhang, and Margarita V. Revzin. "Mesenteric Amyloidosis: Radiologic Imaging with Pathologic Correlation." Journal of Clinical Imaging Science 10 (May 2, 2020): 24. http://dx.doi.org/10.25259/jcis_10_2020.
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Amyloidosis is a rare disease that is characterized by abnormal deposition of amyloid proteins in tissues, resulting in local, or systemic disease. When localized, it can present as an amyloidoma. We report a case of mesenteric amyloidosis in an 80-year-old male who was found to have an incidental mesenteric mass that was biopsy-proven to represent non-light chain amyloid tissue.
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Ilgen, Ufuk, Zeynep Kendi Celebi, Gulsah Kaygusuz, Sim Kutlay, Gokhan Nergizoglu, and Kenan Ates. "Primary Amyloidosis Presenting with Nephrotic Syndrome and Atypical Intrahepatic Cholestasis: Report of 2 Cases." BANTAO Journal 13, no. 2 (December 1, 2015): 90–94. http://dx.doi.org/10.1515/bj-2015-0020.
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Abstract Liver is one of the most commonly involved organs in both primary and secondary systemic amyloidoses, but hepatic amyloidosis, manifested as mild to moderate enlargement, is usually not symptomatic nor it is clinically problematic. Rarely, massive hepatomegaly, severe cholestatic hepatitis or liver failure may be encountered in patients with systemic amyloidosis. Two cases with lambda light-chain amyloidosis presenting with nephrotic syndrome and atypical intrahepatic cholestasis are discussed with clinical features, laboratory and kidney, liver and bone marrow biopsy findings in view of the relevant literature.
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Binmadi, Nada, Chidan Intapa, Risa Chaisuparat, Sara Akeel, Amal Sindi, and Timothy Meiller. "Immunophenotyping Oral Amyloidosis for the Precise Identification of the Biochemical Forms: A Retrospective Study." Open Dentistry Journal 12, no. 1 (November 30, 2018): 1036–42. http://dx.doi.org/10.2174/1874210601812011036.
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Background: Amyloidosis refers to a group of systemic and localized disorders associated with the accumulation of misfolded protein aggregates called amyloids in different parts of the body. Owing to the existence of multiple forms of amyloids with similar tertiary structures, precise identification of their biochemical form is critical for correct therapy. Objective: This retrospective study aimed to determine whether typing of oral amyloid deposits can help diagnose a serious systemic condition in the early phase of the disease Methods: All histopathologically confirmed cases of amyloidosis managed over a 14-year period (January 1, 1997 to December 31, 2011) were retrieved for analysis. Two board-certified oral and maxillofacial pathologists reviewed the histopathological findings of amyloidosis on the basis of its classic Congo red staining characteristics. This was followed by immunohistochemical analysis of biopsy samples using a panel of antibodies specific for different forms of amyloidosis. Results: The most common location of amyloidosis was the tongue, and women were more commonly affected than men. The patient age ranged from 11 to 83 years (average 59.3 years). In patient 9, light-chain and pre-albumin (transthyretin) antibodies were related to arthritis and senile amyloidosis, respectively. The biopsy sample of patient 10, who was reported to have multiple myeloma, was positive for light chains and β2 microglobulin. All other samples exhibited localized (solitary) amyloidosis. Conclusion: Histological analysis coupled with immunostaining with a panel of specific antibodies might assist in identifying early systemic amyloidosis in patients with localized oral forms of the disease.
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Raymond, A. Kevin, Nour Sneige, and John G. Batsakis. "Amyloidosis in the Upper Aerodigestive Tracts." Annals of Otology, Rhinology & Laryngology 101, no. 9 (September 1992): 794–96. http://dx.doi.org/10.1177/000348949210100915.
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The upper aerodigestive tracts, particularly the larynx, are not uncommon repositories for amyloid. In most instances amyloidosis of the larynx is localized and is not associated with or followed by systemic disease. Oral and nasopharyngeal amyloidoses, on the other hand, are very often manifestations of systemic predisposing disorders. Laryngeal amyloidosis is treated, when indicated, by surgical removal, often repeated because of persistence or multifocal deposits.
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Alraawi, Zeina, Nayan Banerjee, Srujana Mohanty, and Thallapuranam Krishnaswamy Suresh Kumar. "Amyloidogenesis: What Do We Know So Far?" International Journal of Molecular Sciences 23, no. 22 (November 12, 2022): 13970. http://dx.doi.org/10.3390/ijms232213970.
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The study of protein aggregation, and amyloidosis in particular, has gained considerable interest in recent times. Several neurodegenerative diseases, such as Alzheimer’s (AD) and Parkinson’s (PD) show a characteristic buildup of proteinaceous aggregates in several organs, especially the brain. Despite the enormous upsurge in research articles in this arena, it would not be incorrect to say that we still lack a crystal-clear idea surrounding these notorious aggregates. In this review, we attempt to present a holistic picture on protein aggregation and amyloids in particular. Using a chronological order of discoveries, we present the case of amyloids right from the onset of their discovery, various biophysical techniques, including analysis of the structure, the mechanisms and kinetics of the formation of amyloids. We have discussed important questions on whether aggregation and amyloidosis are restricted to a subset of specific proteins or more broadly influenced by the biophysiochemical and cellular environment. The therapeutic strategies and the significant failure rate of drugs in clinical trials pertaining to these neurodegenerative diseases have been also discussed at length. At a time when the COVID-19 pandemic has hit the globe hard, the review also discusses the plausibility of the far-reaching consequences posed by the virus, such as triggering early onset of amyloidosis. Finally, the application(s) of amyloids as useful biomaterials has also been discussed briefly in this review.
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Mikic, Dragan, Slobodan Forcan, Milos Kostov, Lidija Popovic, and Goran Brajuskovic. "Primary-localized-cutaneous-amyloidosis: Lichen amyloidosus." Vojnosanitetski pregled 61, no. 1 (2004): 83–87. http://dx.doi.org/10.2298/vsp0401083m.
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This case report presented a female patient with primary-localized-cutaneous--amyloidosis in the form of lichen amyloidosus. Primary-localized-cutaneous--amyloidosis is a rare idiopathic dermatosis caused by abnormal deposition of amyloid composed primarily of degenerated keratin filaments. In order to establish the final diagnosis, detailed clinical and laboratory investigations were performed, with a particular emphasis on pathohistological analysis of skin specimens, special stains, and electron microscopy.
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Almeida, Zaida L., and Rui M. M. Brito. "Amyloid Disassembly: What Can We Learn from Chaperones?" Biomedicines 10, no. 12 (December 17, 2022): 3276. http://dx.doi.org/10.3390/biomedicines10123276.
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Protein aggregation and subsequent accumulation of insoluble amyloid fibrils with cross-β structure is an intrinsic characteristic of amyloid diseases, i.e., amyloidoses. Amyloid formation involves a series of on-pathway and off-pathway protein aggregation events, leading to mature insoluble fibrils that eventually accumulate in multiple tissues. In this cascade of events, soluble oligomeric species are formed, which are among the most cytotoxic molecular entities along the amyloid cascade. The direct or indirect action of these amyloid soluble oligomers and amyloid protofibrils and fibrils in several tissues and organs lead to cell death in some cases and organ disfunction in general. There are dozens of different proteins and peptides causing multiple amyloid pathologies, chief among them Alzheimer’s, Parkinson’s, Huntington’s, and several other neurodegenerative diseases. Amyloid fibril disassembly is among the disease-modifying therapeutic strategies being pursued to overcome amyloid pathologies. The clearance of preformed amyloids and consequently the arresting of the progression of organ deterioration may increase patient survival and quality of life. In this review, we compiled from the literature many examples of chemical and biochemical agents able to disaggregate preformed amyloids, which have been classified as molecular chaperones, chemical chaperones, and pharmacological chaperones. We focused on their mode of action, chemical structure, interactions with the fibrillar structures, morphology and toxicity of the disaggregation products, and the potential use of disaggregation agents as a treatment option in amyloidosis.
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Rognoni, Paola, Giulia Mazzini, Serena Caminito, Giovanni Palladini, and Francesca Lavatelli. "Dissecting the Molecular Features of Systemic Light Chain (AL) Amyloidosis: Contributions from Proteomics." Medicina 57, no. 9 (August 31, 2021): 916. http://dx.doi.org/10.3390/medicina57090916.
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Amyloidoses are characterized by aggregation of proteins into highly ordered amyloid fibrils, which deposit in the extracellular space of tissues, leading to organ dysfunction. In AL (amyloid light chain) amyloidosis, the most common form in Western countries, the amyloidogenic precursor is a misfolding-prone immunoglobulin light chain (LC), which, in the systemic form, is produced in excess by a plasma cell clone and transported to target organs though blood. Due to the primary role that proteins play in the pathogenesis of amyloidoses, mass spectrometry (MS)-based proteomic studies have gained an established position in the clinical management and research of these diseases. In AL amyloidosis, in particular, proteomics has provided important contributions for characterizing the precursor light chain, the composition of the amyloid deposits and the mechanisms of proteotoxicity in target organ cells and experimental models of disease. This review will provide an overview of the major achievements of proteomic studies in AL amyloidosis, with a presentation of the most recent acquisitions and a critical discussion of open issues and ongoing trends.
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Karitzky, P. C., C. Trautmann-Grill, J. Laske, S. Beissert, and F. Meier. "Kutane Manifestation einer AL-Amyloidose mit Plasmazellmyelom vom Lambda-Leichtkettentyp." Aktuelle Dermatologie 47, no. 05 (May 2021): 211–15. http://dx.doi.org/10.1055/a-1406-8002.
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ZusammenfassungDie mit einem multiplen Myelom assoziierte Immunoglobulin-Leichtketten (AL)-Amyloidose ist unter den systemischen Amyloidosen die häufigste Form, als Entität selbst jedoch relativ selten. Die durch den monoklonalen Plasmazellklon sezernierten instabilen Leichtketten führen als Amyloidablagerungen im Gewebe zu manifesten Organschäden, v. a. die renalen und kardialen Organmanifestationen führen häufig zu einer sehr schlechten Prognose. Besonders kutane Manifestationen wie beidseitige periorbitale Ödeme, Ekchymosen und eine Makroglossie können als pathognomonisch für die systemische AL-Amyloidose betrachtet werden und sollten zu einer raschen Abklärung führen. Wir berichten über einen Patienten mit einer kutanen Manifestation einer AL-Amyloidose mit assoziiertem „smouldering Myelom“.
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Miyazaki, Shinya, Yuki Kobayashi, Fuyuki Kametani, Kyoko Kobayashi, Susumu Iwaide, Tokuma Yanai, and Tomoaki Murakami. "Systemic amyloidosis derived from EFEMP1 in a captive Tsushima leopard cat." Veterinary Pathology 59, no. 1 (November 11, 2021): 152–56. http://dx.doi.org/10.1177/03009858211048650.
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In animals, most cases of systemic amyloidosis are of amyloid A type, and the other types of systemic amyloidoses are rare. This study analyzed systemic amyloidosis in a 15-year-old female Tsushima leopard cat. Amyloid deposits strongly positive for Congo red staining were observed in the arterial walls as well as the interstitium in multiple organs. Mass spectrometry–based proteomic analysis with laser microdissection of amyloid deposits identified epidermal growth factor–containing fibulin-like extracellular matrix protein 1 (EFEMP1) as a prime amyloidogenic protein candidate. Immunohistochemistry showed that the amyloid deposits were positive for the N-terminal region of EFEMP1. From these results, the present case was diagnosed as EFEMP1-derived amyloidosis. It is the first such case in an animal. EFEMP1-derived amyloidosis in humans has recently been reported as a systemic amyloidosis, and it is known as an age-related venous amyloidosis. The present case showed different characteristics from human EFEMP1-derived amyloidosis, including the amyloid deposition sites and the amyloidogenic region of the EFEMP1 protein, suggesting a different pathogenesis between Tsushima leopard cat and human EFEMP1-derived amyloidosis.
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Yilmaz, A., J. Bauersachs, F. Bengel, R. Büchel, I. Kindermann, K. Klingel, F. Knebel, et al. "Diagnosis and treatment of cardiac amyloidosis: position statement of the German Cardiac Society (DGK)." Clinical Research in Cardiology 110, no. 4 (January 18, 2021): 479–506. http://dx.doi.org/10.1007/s00392-020-01799-3.
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AbstractSystemic forms of amyloidosis affecting the heart are mostly light-chain (AL) and transthyretin (ATTR) amyloidoses. The latter is caused by deposition of misfolded transthyretin, either in wild-type (ATTRwt) or mutant (ATTRv) conformation. For diagnostics, specific serum biomarkers and modern non-invasive imaging techniques, such as cardiovascular magnetic resonance imaging (CMR) and scintigraphic methods, are available today. These imaging techniques do not only complement conventional echocardiography, but also allow for accurate assessment of the extent of cardiac involvement, in addition to diagnosing cardiac amyloidosis. Endomyocardial biopsy still plays a major role in the histopathological diagnosis and subtyping of cardiac amyloidosis. The main objective of the diagnostic algorithm outlined in this position statement is to detect cardiac amyloidosis as reliably and early as possible, to accurately determine its extent, and to reliably identify the underlying subtype of amyloidosis, thereby enabling subsequent targeted treatment.
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KIM, Duck-Hwanb, Kenichiro ONO, Kazuo YASUDA, Atsuhiko HASEGAWA, and Isamu TOMODA. "Urinary amyloids in bovine amyloidosis." Japanese Journal of Veterinary Science 47, no. 1 (1985): 129–32. http://dx.doi.org/10.1292/jvms1939.47.129.
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Czyżewska, Emilia, Agnieszka Wiśniewska, Anna Waszczuk-Gajda, and Olga Ciepiela. "The Role of Light Kappa and Lambda Chains in Heart Function Assessment in Patients with AL Amyloidosis." Journal of Clinical Medicine 10, no. 6 (March 18, 2021): 1274. http://dx.doi.org/10.3390/jcm10061274.
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There are reports indicating that myocardial dysfunction in systemic immunoglobulin light chain amyloidosis (AL amyloidosis) stems not only from the amyloid deposit in the organ but also the cardiotoxicity of the amyloid precursor free light chains (FLCs) circulating in the blood. The aim of the study is to analyze the role of sFLC κ and λ in the assessment of heart involvement and the degree of myocardial damage in AL amyloidosis. The study involved 71 patients diagnosed with primary AL amyloidosis. The relationship between sFLC concentrations and cardiac biochemical and echocardiographic parameters was assessed. The median concentrations of N-terminal pro b-type natriuretic peptide(NT-proBNP) and troponin I (TnI) were significantly higher in patients with amyloids formed from monoclonal λ chains compared to patients with monoclonal κ proliferation. In patients with heart involvement by amyloids formed from monoclonal FLC, the study demonstrated a statistically significant positive correlation between the concentration of monoclonal antibody λ chain and TnI (R = 0.688; p < 0.05), NT-proBNP (R = 0.449; p < 0.05), and the value of diastolic dimension of the interventricular septum (IVS; R = 0.496, p < 0.05). The above data indicate that the presence of monoclonal λ chains in patients with AL amyloidosis may be associated with more severe damage to cardiomyocytes and dysfunction of the myocardium.
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Ablasser, Klemens, Nicolas Verheyen, Theresa Glantschnig, Giulio Agnetti, and Peter P. Rainer. "Unfolding Cardiac Amyloidosis –From Pathophysiology to Cure." Current Medicinal Chemistry 26, no. 16 (August 26, 2019): 2865–78. http://dx.doi.org/10.2174/0929867325666180104153338.
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Deposition of amyloidogenic proteins leading to the formation of amyloid fibrils in the myocardium causes cardiac amyloidosis. Although any form of systemic amyloidosis can affect the heart, light-chain (AL) or transthyretin amyloidosis (ATTR) account for the majority of diagnosed cardiac amyloid deposition. The extent of cardiac disease independently predicts mortality. Thus, the reversal of arrest of adverse cardiac remodeling is the target of current therapies. Here, we provide a condensed overview on the pathophysiology of AL and ATTR cardiac amyloidoses and describe treatments that are currently used or investigated in clinical or preclinical trials. We also briefly discuss acquired amyloid deposition in cardiovascular disease other than AL or ATTR.
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Khoor, Andras, and Thomas V. Colby. "Amyloidosis of the Lung." Archives of Pathology & Laboratory Medicine 141, no. 2 (February 1, 2017): 247–54. http://dx.doi.org/10.5858/arpa.2016-0102-ra.
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Context.—Amyloidosis is a heterogeneous group of diseases characterized by the deposition of congophilic amyloid fibrils in the extracellular matrix of tissues and organs. To date, 31 fibril proteins have been identified in humans, and it is now recommended that amyloidoses be named after these fibril proteins. Based on this classification scheme, the most common forms of amyloidosis include systemic AL (formerly primary), systemic AA (formerly secondary), systemic wild-type ATTR (formerly age-related or senile systemic), and systemic hereditary ATTR amyloidosis (formerly familial amyloid polyneuropathy). Three different clinicopathologic forms of amyloidosis can be seen in the lungs: diffuse alveolar-septal amyloidosis, nodular pulmonary amyloidosis, and tracheobronchial amyloidosis. Objective.—To clarify the relationship between the fibril protein–based amyloidosis classification system and the clinicopathologic forms of pulmonary amyloidosis and to provide a useful guide for diagnosing these entities for the practicing pathologist. Data Sources.—This is a narrative review based on PubMed searches and the authors' own experiences. Conclusions.—Diffuse alveolar-septal amyloidosis is usually caused by systemic AL amyloidosis, whereas nodular pulmonary amyloidosis and tracheobronchial amyloidosis usually represent localized AL amyloidosis. However, these generalized scenarios cannot always be applied to individual cases. Because the treatment options for amyloidosis are dependent on the fibril protein–based classifications and whether the process is systemic or localized, the workup of new clinically relevant cases should include amyloid subtyping (preferably with mass spectrometry–based proteomic analysis) and further clinical investigation.
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Hund, Ernst, Arnt Kristen, Michaela Auer-Grumbach, Christian Geber, Frank Birklein, Wilhelm Schulte-Mattler, Claudia Sommer, Hartmut Schmidt, and Christoph Röcken. "Transthyretin-Amyloidose (ATTR-Amyloidose): Empfehlungen zum Management in Deutschland und Österreich." Aktuelle Neurologie 45, no. 08 (September 14, 2018): 605–16. http://dx.doi.org/10.1055/a-0649-0724.
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ZusammenfassungDie Transthyretin-Amyloidose (ATTR-Amyloidose) ist eine seltene, rasch verlaufende neurodegenerative Erkrankung, verursacht durch Mutationen im Transthyretin-Gen. Aufgrund der Seltenheit ist sie wenig bekannt mit der Folge, dass die Diagnose in vielen Fällen nicht oder für eine effektive Therapie zu spät gestellt wird. Therapeutisch steht seit Anfang der 1990er-Jahre die Lebertransplantation zur Verfügung, seit 2011 der oral einzunehmende Transthyretinstabilisator Tafamidis. Weitere Substanzen sind in der klinischen Prüfung oder stehen vor der Zulassung. Hierzu zählen die gentherapeutischen Substanzen Inotersen und Patisiran, die auf dem Boden der RNA-Interferenz wirken, für die Behandlung der Polyneuropathie und Tafamidis zur Behandlung der Kardiomyopathie bei ATTR-Amyloidosen. Die vorliegende Arbeit deutschsprachiger Experten gibt Empfehlungen zu Diagnostik, Management und Therapie von ATTR-Amyloidosen und soll helfen, diese erbliche, heute aber gut behandelbare, Erkrankung einem weiteren Kreis von Ärzten bekannt zu machen.
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Mukhopadhyay, Sanjay, Timothy A. Damron, and Alfredo L. Valente. "Recurrent Amyloidoma of Soft Tissue With Exuberant Giant Cell Reaction." Archives of Pathology & Laboratory Medicine 127, no. 12 (December 1, 2003): 1609–11. http://dx.doi.org/10.5858/2003-127-1609-raostw.
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Abstract Amyloidoma (localized tumorlike amyloidosis) in the soft tissues is rare. We present an instructive case of recurrent amyloidoma in the soft tissue of the ankle in a 45-year-old man with multiple surgical procedures and chronic osteomyelitis of the underlying bones. The lesion evaded diagnosis because of a florid giant cell reaction that led to various misdiagnoses, including giant cell tumor of tendon sheath, foreign body reaction secondary to surgery, and pseudogout. This case demonstrates the importance of considering the possibility of amyloidoma when a giant cell–rich lesion is encountered in the soft tissues.
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Sedwick, Lyn A. "Vitreous Amyloidosis in Familial Amyloidotic Polyneuropathy." Journal of Neuro-Ophthalmology 16, no. 3 (September 1996): 227. http://dx.doi.org/10.1097/00041327-199609000-00019.
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Tschöpe, Carsten, Ahmed Elsanhoury, Sonja Diekmann, and Uwe Kühl. "Hypertrophe Kardiomyopathien und die kardiale ATTR-Amyloidose – eine aktuelle Übersicht für den klinischen Alltag." DMW - Deutsche Medizinische Wochenschrift 147, no. 17 (August 28, 2022): 1127–34. http://dx.doi.org/10.1055/a-1744-3126.
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Was ist neu? Hypertrophe obstruktive Kardiomyopathie Mavacamten, der erste Myosin-Aktivator, konnte erfolgreich in dem EXPLORER-HCM-Studienprogramm getestet werden. Lebensqualität und linksventrikuläre Druckgradienten-Abnahme wurden optimiert. Ob damit jedoch auch die Überlebensrate und Prognose der betroffenen Patienten verbessert wird, kann bis heute noch nicht gesagt werden. Die europäischen Zulassungsbehörden sehen allerdings bisher die Ergebnisse als so bedeutsam an, dass mit einer Führung der Substanzklasse vielleicht schon in den nächsten 6–8 Monaten zu rechnen ist. In den USA ist die Substanz bereits seit April 2022 zugelassen. Der Einsatz der Substanz bei HCM-Patienten ohne Obstruktion wird ebenfalls zurzeit untersucht. Kardiale Transthyretin-Amyloidosen Kardiale Amyloidosen haben meist eine gute Ejektionsfraktion, jedoch sind auch EF mit 40 oder < 30 % möglich. Das Auftreten einer kardialen Amyloidose bei Patienten mit der Symptomatik einer Herzinsuffizienz mit erhaltener Ejektionsfraktion (HFpEF) ist in bis zu 15 % der Fälle nachzuweisen. Tafamidis ist die einzige zurzeit zugelassene erfolgreiche Therapiemöglichkeit bei Patienten mit kardialer ATTR-Amyloidose. Dies wurde auch durch weitere Beobachtungsregister der ATTR-ACT-Studie gezeigt. Für die Klinik ist zusätzlich wichtig, dass die Amyloidose auch die Aortenklappe befällt. Zahlreiche Patienten entwickeln somit auch eine Aortenstenose, die erkannt und meist interventionell zu behandeln ist.
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Cowan, Andrew J., Martha Skinner, J. Mark Sloan, John L. Berk, Carl J. O'Hara, David C. Seldin, and Vaishali Sanchorawala. "Macroglossia – Not Always AL Amyloidosis." Blood 116, no. 21 (November 19, 2010): 5007. http://dx.doi.org/10.1182/blood.v116.21.5007.5007.
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Abstract Abstract 5007 Introduction: Amyloidosis is characterized by extracellular deposition of abnormal insoluble fibrillar proteins. The two most frequent systemic amyloidoses are the light-chain (AL amyloidosis) and familial transthyretin (ATTR) forms. Clinical presentations often vary between the two types. Macroglossia is viewed as pathognomic of AL amyloidosis, and has not previously been described in patients with hereditary TTR amyloidosis. Here, we describe two cases of systemic amyloidosis with macroglossia in which immuno-electron microscopy diagnosed ATTR in one and AL in the other. Case Presentations: A 61 year old woman presented initially to her general internist with weight loss, difficulty swallowing, and tongue numbness. Her clinical exam revealed macroglossia and peripheral neuropathy. Tongue and axillary lymph node biopsies demonstrated amyloid deposits by Congo red staining. There was no evidence of renal, cardiac or other vital organ involvement. She had no evidence of a plasma cell dyscrasia with negative serum and urine immunofixation electrophoresis, normal serum free light chain concentration and ratio as well as polytypic plasma cells in the bone marrow. Immuno-electron microscopy using gold-labeled antibodies was performed on the tongue biopsy. The fibrils were immunoreactive with anti-TTR but not anti-kappa, anti-lambda, or anti-AA antibodies. DNA sequencing identified a known amyloidogenic T60A TTR mutation in exon 3 of chromosome 18, confirming the diagnosis of ATTR with amyloidotic polyneuropathy and macroglossia. The second case involved a 59 year old man with renal insufficiency. He complained of fatigue, weight loss, and tongue swelling. Physical examination was significant for macroglossia and submandibular gland enlargement. Tongue biopsy demonstrated amyloid deposits by Congo red staining. As in the previous case, markers of plasma cell dyscrasia with clonal plasma cells in the bone marrow, blood, and urine were absent. Immuno-electron microscopy of the tongue biopsy documented antibody reactivity to lambda light chain and not TTR, kappa light chain or AA proteins, confirming the diagnosis of AL amyloidosis. He subsequently underwent treatment with high dose intravenous melphalan followed by stem cell transplantation achieving a good clinical response sustained for 2 years to date. Discussion: While macroglossia is thought to be pathognomonic of AL amyloidosis, we report a case of macroglossia with fibrillar ATTR amyloid deposits diagnosed by immuno-electron microscopy. This is contrasted with a clinical presentation consistent with AL in which routine laboratory testing failed to identify evidence of a plasma cell dyscrasia. In both cases, electron microscopy demonstrated immunoreactivity for the fibrils of a single pathogenic protein. The first case was confirmed by DNA sequencing, and the second had a typical response to anti-plasma cell chemotherapy, in spite of the lack of identifiable markers of disease. Disclosures: No relevant conflicts of interest to declare.
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Huang, Hsien-Po, and Shang-Feng Tsai. "A Rare Case of Amyloidoma of the Chest Wall Presented with Fever of Unknown Origin." Diagnostics 12, no. 4 (April 6, 2022): 906. http://dx.doi.org/10.3390/diagnostics12040906.
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Amyloidoma of the chest wall is an uncommon entity, consisting of a solitary tumor-like deposit of amyloid. Until now, while rarely reported, it was mostly presented with back pain and swelling. Here, we report the first case of a chest wall amyloidoma initially presented with fever of unknown origin. Due to the rarity of the lesion as a primary entity, protein electrophoresis and long-term follow-up are required. In addition, patients undergoing long-term hemodialysis are particularly at risk for such acquired amyloidosis. However, soft-tissue tumors, considered as amyloidoma, is also rare in patients with long-term hemodialysis. For patients with a fever of unknown primary origin, clinicians should keep amyloidoma in mind, especially in high-risk populations.
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Amado, Manuel López, María José Lorenzo Patiño, Gonzalo López Blanco, and Francisco Arnal Monreal. "Giant primary amyloidoma of the tonsil." Journal of Laryngology & Otology 110, no. 6 (June 1996): 613–15. http://dx.doi.org/10.1017/s0022215100134413.
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AbstractA case of giant amyloidoma in the left tonsil with extensive osseous metaplasia and a scanty and patchy monoclonal population of IgG Kappa plasma cells, is presented.Localized tumoral amyloidosis is a rare, benign tumour of the upper aerodigestive tract. Organ-limited amyloidosis has been shown to be confined to various systems but, since the lesion was first described, only four cases situated in the tonsils have been reported in the English literature, and none of these had either osseous metaplasia or a monoclonal population of IgG Kappaplasma cells.
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Gambichler, Thilo, Laura Susok, and Marc H. Segert. "Friction-Induced Biphasic Cutaneous Amyloidosis." Dermato 1, no. 1 (August 19, 2021): 31–34. http://dx.doi.org/10.3390/dermato1010005.
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Primary cutaneous amyloidoses (PCA) are a group of conditions characterized by deposition of amyloid in previously normal skin, without association with other skin or systemic diseases. We describe a Kazakhstani female with a 30-year history of increasingly spreading hyperpigmented macular as well papular skin lesions on her upper trunk accompanied by pruritus. Moreover, her medical history included intensely rubbing her skin with a cotton towel following bathing and showering. On the basis of the clinical and histopathological findings, the diagnosis of biphasic cutaneous amyloidosis was made. The present unusual case of biphasic cutaneous amyloidosis can be subsumed under mechanically-induced forms of cutaneous amyloidosis. In conclusion, the present case underscores the necessity to explore carefully the patient’s history in order to discover the cause of PCA.
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Brambilla, Francesca, Francesca Lavatelli, Dario Di Silvestre, Veronica Valentini, Rossana Rossi, Giovanni Palladini, Laura Obici, Laura Verga, Pierluigi Mauri, and Giampaolo Merlini. "Reliable typing of systemic amyloidoses through proteomic analysis of subcutaneous adipose tissue." Blood 119, no. 8 (February 23, 2012): 1844–47. http://dx.doi.org/10.1182/blood-2011-07-365510.
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Abstract Considering the important advances in treating specific types of systemic amyloidoses, unequivocal typing of amyloid deposits is now essential. Subcutaneous abdominal fat aspiration is the easiest, most common diagnostic procedure. We developed a novel, automated approach, based on Multidimensional Protein Identification Technology, for typing amyloidosis. Fat aspirates were obtained from patients with the most common systemic amyloidoses (ALλ, ALκ, transthyretin, and reactive amyloidosis), with Congo red score more than or equal to 3+, and nonaffected controls. Peptides from extracted and digested proteins were analyzed by Multidimensional Protein Identification Technology. On semiquantitative differential analysis (patients vs controls) of mass spectrometry data, specific proteins up-represented in patients were identified and used as deposit biomarkers. An algorithm was developed to classify patients according to type and abundance of amyloidogenic proteins in samples; in all cases, proteomic characterization was concordant with fibril identification by immunoelectron microscopy and consistent with clinical presentation. Our approach allows reliable amyloid classification using readily available fat aspirates.
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Gioeva, Z. V., R. A. Vandysheva, A. A. Ephiev, A. A. Gabueva, N. G. Dzadzieva, L. M. Erofeeva, and L. M. Mikhaleva. "Clinical and morphological features of localized laryngeal amyloidosis." CLINICAL AND EXPERIMENTAL MORPHOLOGY 11, no. 4 (2022): 38–47. http://dx.doi.org/10.31088/cem2022.11.4.38-47.
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Introduction. Amyloidosis is a disease characterized by extracellular deposition of insoluble fibrils composed of an abnormal protein, amyloid. This protein builds up in various tissues and organs and interferes with their function leading to atrophy and sclerosis. Amyloidosis is usually a systemic disease. However, there are case reports of localized amyloidosis. Localized laryngeal amyloidosis is a rare condition accounting for approximately 15% of localized amyloidosis. The aim of the research was to describe morphological features of localized laryngeal amyloidosis. Materials and methods. We analyzed clinical findings, biopsy, and surgical specimens of 6 patients with localized laryngeal amyloidosis. Amyloid deposits were detected in tissue sections with Congo red stain with polarized light microscopy. We performed immunohistochemical analysis with monoclonal and polyclonal antibodies to detect different amyloid types. Results. Laryngeal amyloidosis was diagnosed in 4 male and 2 female patients aged from 44 to 62 (the mean age was 54 years). We found amyloid deposits in the interstitial spaces and tumor-like masses; in polarized light, amyloid showed a bright apple-green birefringence. Inflammatory cell infiltrate and multinucleated giant cells were visualized in most cases. Based on the immunohistochemical typing results, 4 patients had AL-kappa amyloidosis and 2 patients were diagnosed with AL-lambda amyloidosis. The disease recurrence was reported in 2 cases. Conclusion. In the head and neck area, the larynx is the most common site affected by localized amyloidosis. AL-kappa amyloidosis prevailed in our study, most of them being in men. In view of high recurrence rates, a long-term follow-up is needed after the amyloid deposit excision. Keywords: amyloidosis, larynx, amyloidoma, localized amyloidosis, immunohistochemistry
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Myssiorek, David, Aijaz Alvi, and Tawfiqul Bhuiya. "Primary Salivary Gland Amyloidosis Causing Sicca Syndrome." Annals of Otology, Rhinology & Laryngology 101, no. 6 (June 1992): 487–90. http://dx.doi.org/10.1177/000348949210100607.
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Sicca syndrome (SS), consisting of xerostomia and xerophthalmia, may be caused by various disease processes. We present a unique case of SS secondary to primary amyloidosis. Amyloidosis is a rare but definite cause of SS and should be included in the differential diagnosis of any patient who presents with sicca symptoms. A literature review comparing amyloidotic patients with SS and patients with amyloidosis only demonstrates that both of these groups of patients present similarly with regard to symptoms. However, the majority of patients with SS present with sicca symptoms initially in addition to symptoms of amyloidosis. These SS patients also present with proteinuria and negative serology test results. Therefore, patients presenting with sicca symptoms, proteinuria, and negative serologic findings should be suspect for amyloidosis. The importance of distinguishing the diagnosis of Sjögren's syndrome from SS in these patients cannot be overemphasized. There is a significantly higher incidence of developing a lymphoma in Sjögren's syndrome patients. This has important implications for the head and neck surgeon treating these patients.
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Picken, Maria M. "Amyloidosis—Where Are We Now and Where Are We Heading?" Archives of Pathology & Laboratory Medicine 134, no. 4 (April 1, 2010): 545–51. http://dx.doi.org/10.5858/134.4.545.
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Abstract Context.—Amyloidoses are disorders of diverse etiology in which deposits of abnormally folded proteins share distinctive staining properties and fibrillar ultrastructural appearance. Amyloidosis ultimately leads to destruction of tissues and progressive disease. With recent advances in the treatment of systemic amyloidoses the importance of an early diagnosis of amyloid, and a correct diagnosis of its type, has been realized. Objective.—To summarize current recommendations for the diagnosis of amyloidosis. Data Sources.—Presentation given at the 4th Annual Renal Pathology Society Satellite meeting in Istanbul based on discussions and recommendations formulated during an interactive diagnostic session held at the XIth International Symposium on Amyloidosis in Woods Hole, Massachusetts. Conclusions.—Congo red stain is currently the gold standard for amyloid detection and the goal is to detect amyloid early. Diagnosis of the amyloid type must be based on the identification of amyloid protein within the deposits and not solely by reliance on clinical or DNA studies. However, the latter are recommended for confirmation of the amyloid type based on evaluation of the protein in deposits. Immunohistochemistry must be performed and interpreted with caution and inconclusive results must be evaluated further using the more sophisticated methods available in referral centers. An adequate amount and quality of tissue must be available for amyloid diagnosis and typing with emphasis on the use of fresh tissue and greater use of abdominal fat biopsy. The development of new technologies underscores the need for regular review of recommendations and standards for the clinical diagnosis of amyloidosis.
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Annaházi, Anita, István Németh, Szabolcs Modok, Károly Szentpáli, László Tiszlavicz, Tibor Wittmann, and László Czakó. "Amyloidosis induced colonic stricture. The first symptom of myeloma multiplex. A case report." Orvosi Hetilap 149, no. 25 (June 1, 2008): 1181–85. http://dx.doi.org/10.1556/oh.2008.28365.
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A szisztémás amyloidosis gyakran érinti a gastrointestinalis rendszert fekély vagy polypoid elváltozás formájában, a vastagbelet körkörösen szűkítő folyamat azonban különösen ritka. Amyloidosis előfordulása a λ-könnyűláncot termelő myeloma multiplexes betegek kb. 10%-ában várható, szövettanilag AL típusú. A hematológiai betegség diagnózisa azonban szinte minden esetben megelőzi a gastrointestinalis tünetek jelentkezését. Esetismertetés: Egy 73 éves nőbeteget anémia, hasi fájdalom, haematochesia miatt vizsgáltunk. A kolonoszkópia során körkörös sigmabélstenosis igazolódott, mely neoplasia gyanúját vetette fel. A szűkület megoldására sigmaresectio történt rectosigmoidealis anastomosissal. A resecatum szövettani vizsgálata AA-amyloidosist állapított meg. A kivizsgálás során a subcutan zsírszöveti biopszia szisztémás amyloidosis lehetőségét vetette fel. Az immunelektroforézis emelkedett gamma-globulin-frakciót, ezen belül IgG-λ-monoclonalis komponenst és egy másik λ-típusú könnyűlánckomponenst állapított meg. Ezért Jamshidi-biopszia történt, mely myeloma multiplexet igazolt. Következtetések: Betegünknél a ritka, vastagbelet obstruáló, tumort utánzó bélfali amyloidosis vezetett el a myeloma multiplex diagnózisához. A hematológiai kórkép célzott kezelése mellett ilyen esetben szükséges lehet a körülírt szűkület endoszkópos stentelése vagy a sebészi terápia.
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Соколовский, N. Sokolovskiy, Козырев, Konstantin Kozyrev, Брин, Vadim Brin, Кабисов, and O. Kabisov. "Comparative Analysis of the Acyzol Effects in the Prevention of Models of Amyloidosis." Journal of New Medical Technologies 22, no. 2 (February 25, 2015): 50–55. http://dx.doi.org/10.12737/11831.
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First, the authors obtained two models of the system cardiopatic amyloidosis in rats. The first model was created by a single injection of equal mixture of native egg albumin and Freund´s complete adjuvant 0.2 ml per five points of injection (subcutaneously in the axillary and inguinal region, left and right intraperitoneally). The second model was created with a single introduction of a mixture of native egg albumin (40%), Freund´s complete adjuvant (40%), and myocardial homogenate of rats (20%) at a dose of 0.2 ml in a similar five-point-injection.
To prevent cardiac amyloidosis, the Acyzol (3% solution at 0.1 ml / lOOg body weight) was introduced intragastri-cally - through the probe, daily for 2 months with the first day of administration amyloidogenic mixtures.
The authors analyzed the changes of hemodynamic parameters and proved the positive impact of the acyzol on the functional characteristics of the cardiovascular system in aged rats on the background of experimental models of amyloid cardiopathy. The discovery in the heart the amyloidoses and congophilic reduction indicate the activation mechanisms of amyloidoses.
Comparison of prophylactic effects of acyzol on the background of different models of system cardiopatic amyloidosis was found that more pronounced corrective changes were observed in the acyzol use on the background model with the addition of myocardial homogenate of rats.
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Pihlamaa, Tiia, Sinikka Suominen, and Sari Kiuru-Enari. "Familial amyloidotic polyneuropathy type IV – gelsolin amyloidosis." Amyloid 19, sup1 (April 18, 2012): 30–33. http://dx.doi.org/10.3109/13506129.2012.674076.
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Nalcacioglu, H., G. Genc, S. Ayyildiz, M. Kefeli, O. Aydin, M. Elli, M. Ceyhan, and O. Ozkaya. "P01-036 – Systemic amyloidosis presenting with amyloidoma." Pediatric Rheumatology 11, Suppl 1 (2013): A40. http://dx.doi.org/10.1186/1546-0096-11-s1-a40.
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Samlaska, Curt, Sara Reber, and Todd Murry. "Insulin-derived amyloidosis: The insulin ball, amyloidoma." JAAD Case Reports 6, no. 4 (April 2020): 351–53. http://dx.doi.org/10.1016/j.jdcr.2020.02.011.
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Koike, Haruki, and Masahisa Katsuno. "The Ultrastructure of Tissue Damage by Amyloid Fibrils." Molecules 26, no. 15 (July 29, 2021): 4611. http://dx.doi.org/10.3390/molecules26154611.
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Amyloidosis is a group of diseases that includes Alzheimer’s disease, prion diseases, transthyretin (ATTR) amyloidosis, and immunoglobulin light chain (AL) amyloidosis. The mechanism of organ dysfunction resulting from amyloidosis has been a topic of debate. This review focuses on the ultrastructure of tissue damage resulting from amyloid deposition and therapeutic insights based on the pathophysiology of amyloidosis. Studies of nerve biopsy or cardiac autopsy specimens from patients with ATTR and AL amyloidoses show atrophy of cells near amyloid fibril aggregates. In addition to the stress or toxicity attributable to amyloid fibrils themselves, the toxicity of non-fibrillar states of amyloidogenic proteins, particularly oligomers, may also participate in the mechanisms of tissue damage. The obscuration of the basement and cytoplasmic membranes of cells near amyloid fibrils attributable to an affinity of components constituting these membranes to those of amyloid fibrils may also play an important role in tissue damage. Possible major therapeutic strategies based on pathophysiology of amyloidosis consist of the following: (1) reducing or preventing the production of causative proteins; (2) preventing the causative proteins from participating in the process of amyloid fibril formation; and/or (3) eliminating already-deposited amyloid fibrils. As the development of novel disease-modifying therapies such as short interfering RNA, antisense oligonucleotide, and monoclonal antibodies is remarkable, early diagnosis and appropriate selection of treatment is becoming more and more important for patients with amyloidosis.
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Faust, Dominik, Bora Akoglu, Gordana Ristic, and Vladan Milovic. "Ursodeoxycholic acid for treatment of cholestasis in patients with hepatic amyloidosis." Vojnosanitetski pregled 66, no. 6 (2009): 482–86. http://dx.doi.org/10.2298/vsp0906482f.
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Background. Amyloidosis represents a group of different diseases characterized by extracellular accumulation of pathologic fibrillar proteins in various tissues and organs. Severe amyloid deposition in the liver parenchyma has extrahepatic involvement predominantly in the kidney or heart. We evaluated the effect of ursodeoxycholic acid, in four patients with severe hepatic amyloidosis of different etiologies, who presented with increased alkaline phosphatase and ?-glutamyl transferase. Case report. The study included four patients who presented with amyloidosis-associated intrahepatic cholestasis. Three of them had renal amyloidosis which developed 1-3 years before cholestasis occurred, the remaining one having intrahepatic cholestasis as the primary sign of the disease. Amyloidosis was identified from liver biopsies in all patients by its specific binding to Congo red and green birefringence in polarized light. The biochemical nature and the class of amyloid deposits were identified immunohistochemically. In addition to their regular treatment, the patients received 750 mg ursodeoxycholic acid per day. After 2-4 weeks all patients had a significant decrease of serum alkaline phosphatase and ?-glutamyl transferase, and their general status significantly improved. Conclusion. Treatment with ursodeoxycholic acid may be beneficial in patients with hepatic amyloidosis, and do extend indications for the use of ursodeoxycholic acid in amyloidotic cholestatic liver disease.
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Maingi, Sahil, Nishi Sharma, Ankur Gupta, and Ancy S. Sofia. "A rare case of amyloidoma of parotid gland." International Journal of Otorhinolaryngology and Head and Neck Surgery 6, no. 8 (July 22, 2020): 1556. http://dx.doi.org/10.18203/issn.2454-5929.ijohns20203216.
Full textAbstract:
<p class="abstract">Amyloidoma is a solitary, localized tumor like deposit of amyloid. Amyloidosis can be hereditary or acquired, and it may either be systemic or localized. Amyloidoma of the parotid is a very rare condition, and only a few cases have been described in the literature so far. We report a case of 62 years old male presented with right parotid swelling from last 7 months. Till date only 1 case have been reported so far in the literature. This case has been reported due to rarity of its presentation.</p>
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Ahn, Dongbin, Eun Jung Oh, Ji Hye Kwak, and Jin Ho Sohn. "A Case of Laryngeal Amyloidosis: Role of US and US-CNB for Preoperative Diagnosis." Korean Journal of Otorhinolaryngology-Head and Neck Surgery 65, no. 7 (July 21, 2022): 414–18. http://dx.doi.org/10.3342/kjorl-hns.2021.01137.
Full textAbstract:
Amyloidosis is a rare benign disease characterized by the extracellular deposition of nonsoluble fibrillar proteins (amyloids) within organs. Laryngeal amyloidosis (LA) accounts for only 9%-15% of all cases of amyloidosis. Since clinical manifestations and laryngoscopic findings often overlap with those of laryngeal cancer, it is challenging to differentiate LA from laryngeal cancer prior to surgical biopsy. We report a case of LA mimicking laryngeal cancer, in which the diagnosis was facilitated by preoperative ultrasonography (US) and US-guided core-needle biopsy (US-CNB) prior to surgical biopsy. The US findings of this case were distinguishable from those of laryngeal cancer, which enabled us to consider a diagnosis other than laryngeal cancer. Amyloidosis was diagnosed preoperatively using office-based percutaneous US-CNB, avoiding general anesthesia needed for suspension laryngoscopic examination. This case suggests that US and US-CNB could be used as supplementary diagnostic modalities to evaluate suspicious laryngeal masses mimicking laryngeal cancer.
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Ryšavá, Romana. "AL amyloidosis: advances in diagnostics and treatment." Nephrology Dialysis Transplantation 34, no. 9 (October 8, 2018): 1460–66. http://dx.doi.org/10.1093/ndt/gfy291.
Full textAbstract:
Abstract AL amyloidosis (light chain; previously also called primary amyloidosis) is a systemic disease characterized by an amyloid deposition process affecting many organs, and which still has unsatisfactory survival of patients. The monoclonal light chains kappa (κ) or lambda (λ) or their fragments form the fibrils that deposit and accumulate in different tissues. Renal involvement is very frequent in AL amyloidosis and can lead to the development of nephrotic syndrome followed by renal failure in some cases. AL amyloidosis ultimately leads to destruction of tissues and progressive disease. With recent advances in the treatment, the importance of an early diagnosis of amyloidosis and correct assessment of its type is high. Histologic confirmation is based on Congo red detection of amyloid deposits in tissues but AL amyloidosis must also be distinguished from other systemic forms of amyloidoses with renal involvement, such as AA amyloidosis, amyloidosis with heavy chain deposition, fibrinogen Aα or ALECT2 (leukocyte chemotactic factor 2) deposition. Immunofluorescence (IF) plays a key role here. IF on formalin-fixed paraffin-embedded tissue after protease digestion, immunohistochemistry or laser microdissection with mass spectrometry should complete the diagnosis in unclear cases. Standard treatment with melphalan and prednisolone or with cyclophosphamide and dexamethasone has been replaced with newer drugs used for the treatment of multiple myeloma—bortezomib, carfilzomib and ixazomib or thalidomide, lenalidomide and pomalidomide. High-dose melphalan supported by autologous stem cell transplantation remains the therapeutic option for patients with low-risk status. These new treatment options prolong survival from months to years and improve the prognosis in a majority of patients.