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1.
Rev Fac Cien Med Univ Nac Cordoba ; 78(3): 313-316, 2021 09 18.
Artigo em Espanhol | MEDLINE | ID: mdl-34617706

RESUMO

The increasing complexity in the approach to diseases challenges the development of a new paradigm of care that crosses disciplinary limits, where professionals from different disciplines approach a problem applying their expertise, respecting the knowledge of the other and contributing to the global view of the problem. Amyloidoses are rare diseases. The diagnosis is based on the biopsy of those organs in which amyloid infiltration is suspected. There is an increased risk of bleeding associated with these procedures. Therefore, the availability of obtaining samples from certain sites with less invasive accesses, such as the minor salivary glands (GSM), represent an alternative. Objectives: Describe the experiences of GSM biopsies as a diagnostic tool in the detection of amyloidosis and its intra and postoperative complications. - Estimate the diagnostic performance. The design is a cross-sectional cohort. All patients with a suspected diagnosis of amyloidosis were consecutively included, between August 2018-September 2020. Results: 23 biopsies were performed with minimally invasive procedures. 60.86% were male and the average age was 66 years. The prevalence of amyloidosis was 33%. The sensitivity was 55% and the specificity 100%. One patient had more bleeding than usual during the procedure and none had postoperative complications. Conclusions: GSM biopsy experiences were described as a diagnostic tool for amyloidosis, reporting a slight intraoperative complication and no postoperative complication. The test achieved a sensitivity of 55% and a specificity of 100%.


Assuntos
Amiloidose , Humanos
2.
Arkh Patol ; 83(5): 21-26, 2021.
Artigo em Russo | MEDLINE | ID: mdl-34609800

RESUMO

The cardiovascular system is a common target of systemic amyloidosis (SA); amyloid light chain (AL) cardiac amyloidosis (AL-CA), the wild-type transthyretin (ATTRwt-CA), and mutant-type transthyretin (ATTRmt-CA) are the most studied types of SA. The literature describes only single cases of two types of SA in the same patient. OBJECTIVE: To identify and determine the clinical and morphological characteristics of combined types of SA in patients with biventricular chronic heart failure (CHF). MATERIAL AND METHODS: Eighty autopsy protocols for biventricular CHF deaths were retrospectively analyzed. Immunohistochemistry and confocal laser scanning microscopy (CLCM) with antibodies to amyloid A (AA), serum amyloid-P (SAP), prealbumin, and immunoglobulin kappa (κ) and lambda (λ) light chains were performed. RESULTS: The myocardium showed a combination of different types of SA in 6 (7.5%) cases, including Alλ-CA+ATTR-CA, ALκ-CA+ATTR-CA, and AA-CA+ATTR-CA in 4, 1, and 1 cases, respectively. Macroscopically, the heart mass averaged 470±20 g; the thickness of the left and right ventricular myocardium was 1.5±0.2 and 0.4±0.1 cm, respectively; the interventricular septum averaged 1.2±0.2 cm; and the cardiac index was 0.008. The myocardium was dense, dark red with diffuse layers of whitish dense fibrous connective tissue; the heart cavities were enlarged. Microscopically, in 25% of cases, all heart parts had ALλ-CA that was characterized by massive amyloid deposits localized predominantly in the intramyocardial vessel wall, intermuscular connective tissue, and perivascularly. The myocardium also displayed small amyloid deposits of ALλ-CA and ATTR-CA in the intermuscular connective tissue and intramyocardial vessel wall. Amyloid deposits were located in different parts of the myocardium; there were also areas of co-localization of ALλ-CA+ATTR-CA. CONCLUSION: The combined types of SA occurred under the guise of coronary heart disease and the dilated cardiomyopathy phenotype. The combined amyloid AL-CA and ATTR-CA was generally localized in the interstitium and myocardial vessels. There were also small areas of co-localization of amyloid deposits, which were found mainly in the intramyocardial vessels.


Assuntos
Amiloidose , Traumatismos Cardíacos , Amiloide , Amiloidose/genética , Humanos , Pré-Albumina/genética , Estudos Retrospectivos
3.
Rinsho Ketsueki ; 62(8): 1160-1166, 2021.
Artigo em Japonês | MEDLINE | ID: mdl-34497203

RESUMO

Systemic AL amyloidosis is a disease wherein amyloid proteins derived from monoclonal immunoglobulin light chains produced by abnormal plasma cells are deposited in the tissues through the whole body and cause organ failure. The treatment aims to minimize treatment-related toxicity and mortality to achieve a deeper and more persistent hematologic response as early as possible. Stem cell transplantation is preferred; however, only 20% of patients are eligible. Patients are selected as per strict transplant indication criteria. Transplant-ineligible patients receive chemotherapy with high efficacy, such as melphalan/dexamethasone, bortezomib/cyclophosphamide/dexamethasone, and daratumumab/bortezomib/cyclophosphamide/dexamethasone. The prognosis of advanced cardiac amyloidosis remains poor, and delays in diagnosis are fatal. Early diagnosis and early treatment are important to prevent and minimize organ damage.


Assuntos
Amiloidose , Amiloidose de Cadeia Leve de Imunoglobulina , Amiloidose/diagnóstico , Amiloidose/tratamento farmacológico , Bortezomib/uso terapêutico , Dexametasona , Humanos , Cadeias Leves de Imunoglobulina , Amiloidose de Cadeia Leve de Imunoglobulina/terapia , Melfalan
4.
Arq Bras Cardiol ; 117(3): 561-598, 2021 09.
Artigo em Inglês, Português | MEDLINE | ID: mdl-34550244
5.
Medicina (Kaunas) ; 57(9)2021 Aug 31.
Artigo em Inglês | MEDLINE | ID: mdl-34577839

RESUMO

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.


Assuntos
Amiloidose , Amiloidose de Cadeia Leve de Imunoglobulina , Amiloide , Amiloidose/genética , Humanos , Cadeias Leves de Imunoglobulina , Proteômica
7.
Herz ; 46(5): 485-496, 2021 Oct.
Artigo em Alemão | MEDLINE | ID: mdl-34487196

RESUMO

Aortic valve stenosis in old age has become a topic of interest for cardiology and cardiac surgery after the development of transvascular and transluminal minimally invasive techniques for aortic valve implantation. The observation of amyloid deposits in surgically excised valvular material led to the diagnostics of amyloidosis of the myocardium, which was discovered in up to 20% of the patients who underwent valve implantation. Clinical signs of cardiac amyloidosis, such as carpal tunnel syndrome and ruptured distal biceps tendon should be taken into account. In addition to the electrocardiogram (ECG), echocardiogram and magnetic resonance imaging, 99mtechnetium bone scintigraphy plays a key diagnostic role. The simultaneous occurrence of severe aortic valve stenosis and amyloidosis explains the special hemodynamic situation of a low gradient with low blood flow in high-grade valve stenosis. The interventional or surgical valve implantation improves the prognosis for these patients, similarly to aortic valve stenosis alone, followed by a specific pharmaceutical treatment depending on the type of amyloidosis.


Assuntos
Amiloidose , Estenose da Valva Aórtica , Implante de Prótese de Valva Cardíaca , Amiloidose/diagnóstico por imagem , Valva Aórtica/cirurgia , Estenose da Valva Aórtica/diagnóstico por imagem , Estenose da Valva Aórtica/cirurgia , Ecocardiografia , Humanos , Imageamento por Ressonância Magnética
11.
Am J Case Rep ; 22: e933241, 2021 Aug 23.
Artigo em Inglês | MEDLINE | ID: mdl-34421115

RESUMO

BACKGROUND Immunoglobulin light chain (AL) amyloidosis is a plasma cell disorder in which excess light chain deposits in tissues, resulting in organ dysfunction and damage. Typically, AL amyloidosis presents as a systemic disease affecting multiple organs, and most patients have elevated serum free light chains. However, the presentation of AL amyloidosis is highly variable. The purpose of this case report is to raise awareness of the atypical presentations of AL amyloidosis in order to facilitate more rapid diagnosis, which has the potential to prevent additional organ damage when appropriate therapy is provided. CASE REPORT We describe a case of AL amyloidosis with amyloid deposition confined to the liver and bone marrow and lack of significant serum light chain elevation. The patient initially presented with a spontaneous hepatic hematoma, and was ultimately found to have hepatic AL amyloidosis, with monoclonal plasma cells in the bone marrow and monoclonal protein on serum protein electrophoresis. Our patient responded to treatment with cyclophosphamide-bortezomib-dexamethasone, the anti-CD38 antibody daratumumab, and autologous stem cell transplant, resulting in hematological and organ response. CONCLUSIONS AL amyloidosis can present with end-organ damage confined to isolated organs, and it can present without the expected elevation in serum light chains. Such patients can benefit from appropriate treatment, including traditional chemotherapy, daratumumab, and stem cell transplant. As effective treatments for AL amyloidosis are now available, prompt diagnosis has the potential to limit end-organ damage and potentially improve patient outcomes.


Assuntos
Amiloidose , Amiloidose de Cadeia Leve de Imunoglobulina , Amiloidose/diagnóstico , Amiloidose/tratamento farmacológico , Anticorpos Monoclonais , Humanos , Amiloidose de Cadeia Leve de Imunoglobulina/diagnóstico , Amiloidose de Cadeia Leve de Imunoglobulina/tratamento farmacológico , Fígado
12.
Cells ; 10(7)2021 07 13.
Artigo em Inglês | MEDLINE | ID: mdl-34359938

RESUMO

Transthyretin (TTR) is a tetrameric protein transporting hormones in the plasma and brain, which has many other activities that have not been fully acknowledged. TTR is a positive indicator of nutrition status and is negatively correlated with inflammation. TTR is a neuroprotective and oxidative-stress-suppressing factor. The TTR structure is destabilized by mutations, oxidative modifications, aging, proteolysis, and metal cations, including Ca2+. Destabilized TTR molecules form amyloid deposits, resulting in senile and familial amyloidopathies. This review links structural stability of TTR with the environmental factors, particularly oxidative stress and Ca2+, and the processes involved in the pathogenesis of TTR-related diseases. The roles of TTR in biomineralization, calcification, and osteoarticular and cardiovascular diseases are broadly discussed. The association of TTR-related diseases and vascular and ligament tissue calcification with TTR levels and TTR structure is presented. It is indicated that unaggregated TTR and TTR amyloid are bound by vicious cycles, and that TTR may have an as yet undetermined role(s) at the crossroads of calcification, blood coagulation, and immune response.


Assuntos
Artrite/metabolismo , Doenças Cardiovasculares/metabolismo , Osteoporose/metabolismo , Pré-Albumina/metabolismo , Amiloide/química , Amiloide/metabolismo , Amiloidose/metabolismo , Animais , Humanos , Estresse Oxidativo , Pré-Albumina/química , Conformação Proteica , Estabilidade Proteica
13.
J Phys Chem B ; 125(32): 9155-9167, 2021 08 19.
Artigo em Inglês | MEDLINE | ID: mdl-34370466

RESUMO

A marker for the severeness and disease progress of COVID-19 is overexpression of serum amyloid A (SAA) to levels that in other diseases are associated with a risk for SAA amyloidosis. To understand whether SAA amyloidosis could also be a long-term risk of SARS-CoV-2 infections, we have used long all-atom molecular dynamic simulations to study the effect of a SARS-CoV-2 protein segment on SAA amyloid formation. Sampling over 40 µs, we find that the presence of the nine-residue segment SK9, located at the C-terminus of the envelope protein, increases the propensity for SAA fibril formation by three mechanisms: it reduces the stability of the lipid-transporting hexamer shifting the equilibrium toward monomers, it increases the frequency of aggregation-prone configurations in the resulting chains, and it raises the stability of SAA fibrils. Our results therefore suggest that SAA amyloidosis and related pathologies may be a long-term risk of SARS-CoV-2 infections.


Assuntos
Amiloidose , COVID-19 , Amiloide , Humanos , SARS-CoV-2 , Proteína Amiloide A Sérica
14.
Vestn Oftalmol ; 137(4): 98-103, 2021.
Artigo em Russo | MEDLINE | ID: mdl-34410063

RESUMO

Accumulations of pathological amyloid protein in the vitreous can be a pathognomonic morphological sign of systemic amyloidosis, which is characterized by deposition of insoluble fibrillar protein aggregates (amyloid) in various organs and tissues. The article describes a clinical case of a female 65-year-old patient with bilateral vitreous floaters and histologically confirmed vitreous amyloidosis on the right eye. The patient had undergone YAG laser vitreolysis of the right eye 3 years ago on the Ultra Q Reflex system («Ellex¼, Australia) to treat an atypical Weiss ring. Diagnosis of vitreous amyloidosis was confirmed using the following equipment: video slit lamp SL9900 («CSO¼, Italy), optical coherence tomography system Solix («Optovue¼, USA), B-scan Plus («Accutome¼, USA), microscope CX41RF («Olympus Corporation¼, Japan). Due to significant visual deterioration in the right eye, the patient underwent vitrectomy. Microscopic examination of the surgical sample showed the presence of amyloid deposits revealed by the brick-red specific staining with congo red dye and apple-green birefringence of the stained areas in polarized light.


Assuntos
Amiloidose , Oftalmopatias , Lasers de Estado Sólido , Idoso , Amiloidose/diagnóstico , Oftalmopatias/diagnóstico , Oftalmopatias/cirurgia , Feminino , Humanos , Vitrectomia , Corpo Vítreo
15.
Am J Case Rep ; 22: e933398, 2021 Aug 19.
Artigo em Inglês | MEDLINE | ID: mdl-34413281

RESUMO

BACKGROUND Amyloid light-chain (AL) amyloidosis is a disease that results in systemic amyloid deposition, which may present with multi-organ dysfunction. It carries a poor prognosis at the time of diagnosis. CASE REPORT A 37-year-old patient with a history of Wolff-Parkinson-White syndrome and thyroiditis presented with syncope and hypovolemia. ECG showed non-specific T wave inversions in the lateral leads with no signs of ischemia. Laboratory investigations revealed deranged coagulation parameters with prolonged prothrombin time (PT) and activated partial thromboplastin time (aPTT) and follow-up factor assays revealed severe factor X deficiency. A transthoracic echocardiogram and subsequent cardiac MRI showed signs of cardiac amyloidosis. Bone marrow biopsy was consistent with AL amyloidosis, demonstrating period acid-Schiff (PAS)-positive adipose deposits and interstitial infiltration by clusters of lambda restricted plasma cells with aberrant expression of CD 56 and CD 117.The patient was treated with bortezomib, cyclophosphamide, and dexamethasone, but died early during his treatment due to cardiac arrest, suspected to be secondary to conduction abnormalities caused by cardiac infiltration. CONCLUSIONS This case represents a novel pattern of disease in AL amyloidosis with cardiac, thyroid, and hematological involvement as a result of systemic amyloid deposition.Our report highlights the need for physicians to be aware of cardiac amyloidosis-related complications and the morbidity and mortality associated with concurrent hematological involvement in these cases.


Assuntos
Amiloidose , Deficiência do Fator X , Insuficiência Cardíaca , Amiloidose de Cadeia Leve de Imunoglobulina , Síndromes de Pré-Excitação , Adulto , Amiloidose/complicações , Amiloidose/diagnóstico , Humanos , Amiloidose de Cadeia Leve de Imunoglobulina/complicações , Amiloidose de Cadeia Leve de Imunoglobulina/diagnóstico
16.
Medicine (Baltimore) ; 100(32): e26843, 2021 Aug 13.
Artigo em Inglês | MEDLINE | ID: mdl-34397890

RESUMO

INTRODUCTION: Secondary amyloidosis is a rare complication of rheumatoid arthritis (RA) that is histologically characterized by the deposition of amyloid fibrils in target organs, such as the kidneys and gastrointestinal tract. Controlling the inflammatory response is essential to prevent organ dysfunction in amyloid A (AA) amyloidosis secondary to RA, and no clear treatment strategy exists. PATIENT CONCERNS AND DIAGNOSIS: A 66-year-old woman with RA, who had been treated with disease-modifying anti-rheumatic drugs for 1 year, presented with recurrent abdominal pain and prolonged diarrhea. Endoscopy showed chronic inflammation, and colon tissue histology confirmed AA amyloidosis. INTERVENTIONS AND OUTCOMES: After tocilizumab therapy was begun, her diarrhea and abdominal pain subsided, and articular symptoms improved. Biologic drugs for RA have been used in patients with secondary AA amyloidosis, including tumor necrosis factor and Janus kinase inhibitors, interleukin 6 blockers, and a T cell modulator. Here, we systematically review existing case reports and compare the outcomes of RA-related AA amyloidosis after treatment with various drugs. CONCLUSION: The data indicate that biologic drugs like tocilizumab might be treatments of choice for AA amyloidosis secondary to RA.


Assuntos
Amiloidose , Anticorpos Monoclonais Humanizados/administração & dosagem , Artrite Reumatoide , Terapia Biológica/métodos , Colo , Proteína Amiloide A Sérica/análise , Dor Abdominal/diagnóstico , Dor Abdominal/etiologia , Idoso , Amiloidose/etiologia , Amiloidose/imunologia , Amiloidose/fisiopatologia , Amiloidose/terapia , Antirreumáticos/administração & dosagem , Antirreumáticos/efeitos adversos , Artrite Reumatoide/complicações , Artrite Reumatoide/tratamento farmacológico , Artrite Reumatoide/imunologia , Produtos Biológicos/administração & dosagem , Colo/imunologia , Colo/patologia , Diarreia/diagnóstico , Diarreia/etiologia , Feminino , Humanos , Interleucina-6/antagonistas & inibidores , Resultado do Tratamento
17.
Nat Rev Rheumatol ; 17(9): 510, 2021 09.
Artigo em Inglês | MEDLINE | ID: mdl-34345020
18.
Kyobu Geka ; 74(8): 635-639, 2021 Aug.
Artigo em Japonês | MEDLINE | ID: mdl-34334610

RESUMO

We experienced two cases of primary pulmonary amyloidosis with a localized consolidation. Case 1 is a 80-year-old man, who was found to have an abnormal chest nodular shadow with blurred margin at a medical examination. Chest computed tomography( CT) showed a localized consolidation on the periphery of the upper lobe of the right lung. A CT-guided biopsy was performed. Case 2 is a 66-year-old woman, who was found to have an abnormal chest opacity at a medical examination. Chest CT showed a localized gathering of small nodules in the right lower lobe. Gradual enlargement was noted by follow up CT and the accumulation of fluorodeoxyglucose (FDG) was shown by PET/CT. In consideration of primary lung cancer or malignant lymphoma, right lower lobectomy was performed. Both cases were pathologically diagnosed as pulmonary amyloidosis. Since no findings of amyloid deposits in other organs or of existence of any blood disorders, a diagnosis of primary pulmonary amyloidosis was made.


Assuntos
Amiloidose , Amiloidose de Cadeia Leve de Imunoglobulina , Pneumopatias , Neoplasias Pulmonares , Idoso , Idoso de 80 Anos ou mais , Amiloidose/diagnóstico por imagem , Amiloidose/cirurgia , Feminino , Humanos , Amiloidose de Cadeia Leve de Imunoglobulina/diagnóstico por imagem , Pulmão/diagnóstico por imagem , Pulmão/cirurgia , Pneumopatias/diagnóstico por imagem , Pneumopatias/cirurgia , Neoplasias Pulmonares/diagnóstico por imagem , Neoplasias Pulmonares/cirurgia , Masculino , Tomografia por Emissão de Pósitrons combinada à Tomografia Computadorizada
19.
Orv Hetil ; 162(32): 1303-1308, 2021 08 08.
Artigo em Húngaro | MEDLINE | ID: mdl-34370685

RESUMO

Összefoglaló. A könnyulánc-amyloidosis ritka, multidiszciplináris jelentoségu kórkép, melynek hátterében az esetek dönto hányadában egy amyloidogen fehérje, a csontvelo kóros plazmasejtjeiben termelodo monoklonálisimmunglobulin-molekula lambda típusú könnyuláncának felszaporodása áll. A klinikai tünetek az érintett szervek függvényében igen változatosak és gyakran nem specifikusak, ezért a betegség sok esetben késon kerül felismerésre. A diagnózis felállításának alapfeltétele a szövettani vizsgálat elvégzése és a kóros fehérjelánc kimutatása. A betegség jellegzetes alarmírozó bortüneteinek helyes értékelése fontos szereppel bír a korai diagnózisalkotásban. A jelen közlemény egy myeloma multiplexhez társult könnyulánc-amyloidosis esetét mutatja be. A betegnél a pathognomicus, típusos borgyógyászati tünetek (periorbitalis, axillaris és inguinalis lokalizációjú petechiák, purpurák, ecchymosisok, suffusiók és viaszsárga papulák) mellett szív- és veseérintettség is igazolódott. Az alkalmazott ciklofoszfamid-, bortezomib- és dexametazonkezelési séma hatására a csontveloben komplett morfológiai remisszió következett be, a beteg a jelenleg legjobb túlélést biztosító autológossejt-transzplantáció elott áll. Orv Hetil. 2021; 162(32): 1303-1308. Summary. Amyloid light-chain amyloidosis is a rare disease with diverse signs and symptoms according to the affected organs. The signs are often aspecific which can lead to delayed diagnosis. Considering the characteristic cutaneous manifestations of the disease, dermatologists have an important role in early identification. Additionally, histopathological examination is required for diagnosis. Here we present a rare case of light-chain amyloidosis in association with multiple myeloma. The patient presented with characteristic periocular, axillar and inguinal petechiae, purpurae, ecchymoses, suffusions, yellowish-brown waxy papules and plaques besides cardiovascular and renal involvement. In this case, the amyloidogenic proteins are the lambda-chains of monoclonal immunoglobulins secreted by the clonally expanded plasma cells of the bone marrow. The applied cyclophosphamide, bortezomib and dexamethason treatment induced complete morphological remission in the bone marrow and the patient currently awaits autologous stem cell transplantation which yields the longest possible survival. Orv Hetil. 2021; 162(32): 1303-1308.


Assuntos
Amiloidose , Transplante de Células-Tronco Hematopoéticas , Amiloidose/diagnóstico , Humanos , Masculino , Transplante Autólogo
20.
Molecules ; 26(16)2021 Aug 22.
Artigo em Inglês | MEDLINE | ID: mdl-34443678

RESUMO

Amyloidosis is a term referring to a group of various protein-misfolding diseases wherein normally soluble proteins form aggregates as insoluble amyloid fibrils. How, or whether, amyloid fibrils contribute to tissue damage in amyloidosis has been the topic of debate. In vitro studies have demonstrated the appearance of small globular oligomeric species during the incubation of amyloid beta peptide (Aß). Nerve biopsy specimens from patients with systemic amyloidosis have suggested that globular structures similar to Aß oligomers were generated from amorphous electron-dense materials and later developed into mature amyloid fibrils. Schwann cells adjacent to amyloid fibrils become atrophic and degenerative, suggesting that the direct tissue damage induced by amyloid fibrils plays an important role in systemic amyloidosis. In contrast, there is increasing evidence that oligomers, rather than amyloid fibrils, are responsible for cell death in neurodegenerative diseases, particularly Alzheimer's disease. Disease-modifying therapies based on the pathophysiology of amyloidosis have now become available. Aducanumab, a human monoclonal antibody against the aggregated form of Aß, was recently approved for Alzheimer's disease, and other monoclonal antibodies, including gantenerumab, solanezumab, and lecanemab, could also be up for approval. As many other agents for amyloidosis will be developed in the future, studies to develop sensitive clinical scales for identifying improvement and markers that can act as surrogates for clinical scales should be conducted.


Assuntos
Amiloide/metabolismo , Amiloidose/fisiopatologia , Amiloidose/terapia , Animais , Humanos , Especificidade de Órgãos , Agregados Proteicos , Células de Schwann/patologia
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