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1.
Am J Cardiol ; 160: 96-98, 2021 12 01.
Artigo em Inglês | MEDLINE | ID: mdl-34620488

RESUMO

Cardiac amyloidosis is often preceded by orthopedic manifestations such as carpal tunnel syndrome, and 10% of patients who underwent idiopathic carpal tunnel release surgery will have biopsy-confirmed amyloid deposits in the tenosynovial sheath. Trigger finger is also commonly reported in patients with amyloidosis and involves the same tendon sheath as carpal tunnel syndrome, but the prevalence of amyloid deposition is unclear. This prospective cross-sectional study enrolled 100 patients aged ≥50 years at the time of surgery for idiopathic trigger finger. Patients underwent release surgery, and a sample of the tenosynovium of the affected finger was excised, stained with Congo red, and subtyped with mass spectrometry if amyloid was demonstrated. Further cardiac evaluation was performed in patients with amyloid deposition. Of the 100 patients (mean age 65.5 ± 8.1 years) enrolled, only 2 demonstrated amyloid deposits on Congo red staining. One patient with previous proteinuric kidney disease had fibrinogen A α-chain amyloidosis, and the other patient had untyped amyloidosis. Neither patient had cardiac involvement. A total of 13 of the 100 patients underwent concomitant carpal tunnel release surgery, and 2 of these patients had amyloid deposits in the carpal tunnel with "false-negative" samples from the trigger finger tenosynovium. In conclusion, biopsy during trigger finger release surgery demonstrated a 2% yield for amyloidosis, which is significantly lower than the previously published yield of 10% during carpal tunnel release surgery. This observation has important implications for the development of diagnostic algorithms to screen patients for amyloidosis during orthopedic operations.


Assuntos
Amiloidose/diagnóstico , Cardiomiopatias/diagnóstico , Membrana Sinovial/patologia , Dedo em Gatilho/cirurgia , Idoso , Amiloidose/complicações , Amiloidose/metabolismo , Amiloidose/patologia , Cardiomiopatias/complicações , Cardiomiopatias/metabolismo , Cardiomiopatias/patologia , Síndrome do Túnel Carpal/etiologia , Síndrome do Túnel Carpal/metabolismo , Síndrome do Túnel Carpal/patologia , Síndrome do Túnel Carpal/cirurgia , Feminino , Fibrinogênio/metabolismo , Humanos , Masculino , Programas de Rastreamento , Espectrometria de Massas , Pessoa de Meia-Idade , Membrana Sinovial/metabolismo , Dedo em Gatilho/etiologia , Dedo em Gatilho/metabolismo , Dedo em Gatilho/patologia
2.
Int J Mol Sci ; 22(19)2021 Oct 02.
Artigo em Inglês | MEDLINE | ID: mdl-34639037

RESUMO

Amyloids are self-assembled protein aggregates that take cross-ß fibrillar morphology. Although some amyloid proteins are best known for their association with Alzheimer's and Parkinson's disease, many other amyloids are found across diverse organisms, from bacteria to humans, and they play vital functional roles. The rigidity, chemical stability, high aspect ratio, and sequence programmability of amyloid fibrils have made them attractive candidates for functional materials with applications in environmental sciences, material engineering, and translational medicines. This review focuses on recent advances in fabricating various types of macroscopic functional amyloid materials. We discuss different design strategies for the fabrication of amyloid hydrogels, high-strength materials, composite materials, responsive materials, extracellular matrix mimics, conductive materials, and catalytic materials.


Assuntos
Amiloide/química , Amiloide/metabolismo , Proteínas Amiloidogênicas/metabolismo , Aminoácidos/química , Amiloide/ultraestrutura , Proteínas Amiloidogênicas/química , Amiloidose/etiologia , Amiloidose/metabolismo , Amiloidose/patologia , Matriz Extracelular/metabolismo , Humanos , Interações Hidrofóbicas e Hidrofílicas , Modelos Moleculares , Conformação Proteica , Relação Estrutura-Atividade
3.
Indian J Pathol Microbiol ; 64(3): 464-468, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-34341254

RESUMO

Background: Atrial fibrillation(AF) is as an abnormal irregular rhythm with chaotic generation of electrical signals in the atria of the heart. Various studies in the West have proved that atrial substrates, like isolated atrial amyloidosis can trigger the development of atrial fibrillation. In India, these structural changes have been analyzed on autopsied hearts. Aim: To determine the role of Atrial Amyloid as a substrate for Atrial fibrillation in ante mortem hearts. Methods and Results: Atrial appendages were obtained from seventy five patients undergoing open heart surgery at a tertiary care hospital in south India. They were stained with Hematoxylin &Eosin, Masson's Trichrome and Congo red stains and were examined for myocarditis, fibrosis and amyloidosis, respectively. 30 (40%) patients were in AF. Amyloid deposits were seen in 3 cases. All the three were in AF and had undergone mitral valve replacement (MVR) (P<0.05). 2 out of the 3 amyloid-positive cases showed active myocarditis and severe scarring but there was no statistically significant correlation between these factors. Conclusion: Amyloid and myocarditis, independently act as an arrythmogenic substrates in the development of atrial fibrillation and are also increasingly associated with female gender and MVR. We hypothesize that the amyloid deposits are due to isolated atrial amyloidosis as they were seen only in young individuals. Some patients in sinus rhythm (SR) had large left atria and myocarditis and probably are at a higher risk for developing AF. Hence, follow-up of these patients is required for prevention of severe organ damage and timely therapeutic intervention.


Assuntos
Apêndice Atrial/patologia , Fibrilação Atrial/etiologia , Fibrilação Atrial/patologia , Centros de Atenção Terciária/estatística & dados numéricos , Adolescente , Adulto , Idoso , Amiloidose/complicações , Amiloidose/patologia , Feminino , Átrios do Coração/patologia , Hematoxilina , Humanos , Masculino , Pessoa de Meia-Idade , Fatores Sexuais , Coloração e Rotulagem , Adulto Jovem
4.
Biomolecules ; 11(7)2021 06 23.
Artigo em Inglês | MEDLINE | ID: mdl-34201558

RESUMO

Synucleinopathies are a heterogeneous group of neurodegenerative diseases with amyloid deposits that contain the α-synuclein (SNCA/α-Syn) protein as a common hallmark. It is astonishing that aggregates of a single protein are able to give rise to a whole range of different disease manifestations. The prion strain hypothesis offers a possible explanation for this conundrum. According to this hypothesis, a single protein sequence is able to misfold into distinct amyloid structures that can cause different pathologies. In fact, a growing body of evidence suggests that conformationally distinct α-Syn assemblies might be the causative agents behind different synucleinopathies. In this review, we provide an overview of research on the strain hypothesis as it applies to synucleinopathies and discuss the potential implications for diagnostic and therapeutic purposes.


Assuntos
Amiloide/metabolismo , Encéfalo/metabolismo , Encéfalo/patologia , Sinucleinopatias/metabolismo , alfa-Sinucleína/metabolismo , Amiloide/química , Amiloidose/metabolismo , Amiloidose/patologia , Animais , Humanos , Conformação Proteica , Dobramento de Proteína , Sinucleinopatias/patologia , alfa-Sinucleína/química
7.
Curr Hematol Malig Rep ; 16(4): 357-366, 2021 08.
Artigo em Inglês | MEDLINE | ID: mdl-34106429

RESUMO

PURPOSE OF REVIEW: Amyloidosis is a protein deposition disease whereby a variety of precursor proteins form insoluble fibrils that deposit in tissues, causing organ dysfunction and, many times, death. Accurate characterization of the disease based on the nature of the precursor protein, organ involvement, and extent of disease is paramount to guide management. Cardiac amyloidosis is critical to understand because of its impact on prognosis and new treatment options available. RECENT FINDINGS: New imaging methods have proven to be considerably valuable in the identification of cardiac amyloid infiltration. For treating clinicians, a diagnostic algorithm for patients with suspected amyloidosis with or without cardiomyopathy is shown to help classify disease and to direct appropriate genetic testing and management. For patients with light chain disease, recently introduced treatments adopted from multiple myeloma therapies have significantly extended progression-free and overall survival as well as organ response. In addition, new medical interventions are now available for those with transthyretin amyloidosis. Although cardiac amyloidosis contributes significantly to the morbidity and mortality associated with systemic disease, new tools are available to assist with diagnosis, prognosis, and management.


Assuntos
Amiloidose/complicações , Cardiomiopatias/etiologia , Amiloidose/patologia , Cardiomiopatias/patologia , Humanos
9.
Medicine (Baltimore) ; 100(21): e25961, 2021 May 28.
Artigo em Inglês | MEDLINE | ID: mdl-34032706

RESUMO

RATIONALE: Amyloidosis is a heterogeneous group of diseases characterized by extracellular deposition of amyloid fibrils. Lung carcinoma is rarely reported to be associated with AA amyloidosis. With regard to the manifestation of amyloidosis infiltrating organs, most of the cases focus on the heart, liver, kidneys, and peripheral nervous system. Amyloidosis with diffuse abdominal involvement in combination with pulmonary squamous cell carcinoma carcinoma is an exceptionally rare occurrence. PATIENT CONCERNS: A 70-year-old man was admitted to hospital for a 2-month history of repeated cough, low grade fever, hemoptysis and left back shoulder pain, which was not relieved by nonsteroid anti-inflammatory drugs. Meanwhile, he complained of intermittent diffuse abdominal discomfort and chronic persistent constipation. DIAGNOSES: The patient was diagnosed with poorly differentiated lung squamous cell carcinoma and diffuse peritoneal and mesenteric amyloidosis based on the pathological biopsy. INTERVENTIONS: The patient received surgery and chemotherapy for lung tumor. He did not receive any treatment against amyloidosis. OUTCOMES: The patient died of a severe respiratory infection. LESSONS: This case indicates that lung carcinoma is suspected to play a causative role in the development of amyloidosis. In addition, amyloidosis should be considered in the differential diagnosis in cases in which diffuse greater omentum, peritoneal, and mesenteric calcifications on 18F-2-fluoro-2-deoxy-D-glucose(18F-FDG) photon emission computed tomography (PET/CT).


Assuntos
Amiloidose/diagnóstico , Carcinoma de Células Escamosas/diagnóstico , Neoplasias Pulmonares/diagnóstico , Pulmão/diagnóstico por imagem , Tomografia por Emissão de Pósitrons combinada à Tomografia Computadorizada/métodos , Idoso , Amiloidose/etiologia , Amiloidose/patologia , Carcinoma de Células Escamosas/complicações , Carcinoma de Células Escamosas/terapia , Quimioterapia Adjuvante , Evolução Fatal , Fluordesoxiglucose F18/administração & dosagem , Humanos , Pulmão/patologia , Pulmão/cirurgia , Neoplasias Pulmonares/complicações , Neoplasias Pulmonares/terapia , Masculino , Mesentério/diagnóstico por imagem , Mesentério/patologia , Omento/diagnóstico por imagem , Omento/patologia , Pneumonectomia
10.
Trends Microbiol ; 29(11): 967-969, 2021 11.
Artigo em Inglês | MEDLINE | ID: mdl-33795156

RESUMO

Severe coronavirus disease 2019 (COVID-19) infection leads to multifactorial acute respiratory distress syndrome (ARDS), with little therapeutic success. The pathophysiology associated with ARDS or post-ARDS is not yet well understood. We hypothesize that amyloid formation occurring due to protein homeostasis disruption can be one of the complications associated with COVID-19-induced-ARDS.


Assuntos
Amiloide/metabolismo , COVID-19/complicações , COVID-19/virologia , Síndrome do Desconforto Respiratório/etiologia , Síndrome do Desconforto Respiratório/metabolismo , SARS-CoV-2 , Amiloidose/etiologia , Amiloidose/metabolismo , Amiloidose/patologia , Animais , Gerenciamento Clínico , Suscetibilidade a Doenças , Humanos , Síndrome do Desconforto Respiratório/diagnóstico
11.
Biochem Biophys Res Commun ; 557: 122-126, 2021 06 11.
Artigo em Inglês | MEDLINE | ID: mdl-33862455

RESUMO

Formation of amyloid oligomers and fibrils underlies the pathogenesis of a number of neurodegenerative diseases such as Alzheimer's. One mechanism of action by which Aß aggregates cause neuronal toxicity is through interactions with cellular membranes. Aß aggregates have been shown to disrupt membrane integrity via pore formation, membrane thinning, or lipid extraction. At the same time, lipid membranes also affect the rate of Aß aggregation and remodel pre-formed Aß fibrils. Here we show that Aß42 globulomers, a type of well-characterized and stable Aß oligomers, convert to amyloid fibrils in the presence of DOPC liposomes. Electron paramagnetic resonance studies show that the fibrils converted from Aß42 globulomers adopt the same structure as fibrils formed directly from monomers. Our results suggest that the interactions between Aß oligomers and cellular membranes are dynamic. By converting Aß oligomers to fibrils, the lipid membrane can reduce the membrane-disrupting activities caused by these oligomers. Modulation of Aß-membrane interactions as a therapeutic strategy should take into account the dynamic nature of these interactions.


Assuntos
Doença de Alzheimer/patologia , Peptídeos beta-Amiloides/química , Amiloide/química , Membrana Celular/metabolismo , Lipossomos/metabolismo , Lipídeos de Membrana/metabolismo , Doença de Alzheimer/metabolismo , Proteínas Amiloidogênicas/metabolismo , Amiloidose/metabolismo , Amiloidose/patologia , Espectroscopia de Ressonância de Spin Eletrônica/métodos , Humanos , Microscopia Eletrônica de Varredura , Multimerização Proteica
12.
Commun Biol ; 4(1): 474, 2021 04 15.
Artigo em Inglês | MEDLINE | ID: mdl-33859370

RESUMO

Alzheimer's disease (AD) neuropathology is characterized by hyperphosphorylated tau containing neurofibrillary tangles and amyloid-beta (Aß) plaques. Normally these hallmarks are studied by (immuno-) histological techniques requiring chemical pretreatment and indirect labelling. Label-free imaging enables one to visualize normal tissue and pathology in its native form. Therefore, these techniques could contribute to a better understanding of the disease. Here, we present a comprehensive study of high-resolution fluorescence imaging (before and after staining) and spectroscopic modalities (Raman mapping under pre-resonance conditions and stimulated Raman scattering (SRS)) of amyloid deposits in snap-frozen AD human brain tissue. We performed fluorescence and spectroscopic imaging and subsequent thioflavin-S staining of the same tissue slices to provide direct confirmation of plaque location and correlation of spectroscopic biomarkers with plaque morphology; differences were observed between cored and fibrillar plaques. The SRS results showed a protein peak shift towards the ß-sheet structure in cored amyloid deposits. In the Raman maps recorded with 532 nm excitation we identified the presence of carotenoids as a unique marker to differentiate between a cored amyloid plaque area versus a non-plaque area without prior knowledge of their location. The observed presence of carotenoids suggests a distinct neuroinflammatory response to misfolded protein accumulations.


Assuntos
Doença de Alzheimer/diagnóstico por imagem , Amiloidose/diagnóstico , Placa Amiloide/diagnóstico , Idoso , Idoso de 80 Anos ou mais , Doença de Alzheimer/patologia , Amiloidose/patologia , Feminino , Fluorescência , Secções Congeladas , Humanos , Masculino , Pessoa de Meia-Idade , Placa Amiloide/patologia , Análise Espectral Raman
14.
Life Sci ; 273: 119310, 2021 May 15.
Artigo em Inglês | MEDLINE | ID: mdl-33667517

RESUMO

AIMS: Alzheimer's disease (AD) is a leading health problem in which increased amyloid ß (Aß) accumulation may occur due to abnormal Aß precursor protein processing by ß-secretase 1 (BACE1) enzyme. Lately, neuro-inflammation was recognized as a significant contributor to its pathogenesis. Although the causes of AD are not yet well understood, much evidence has suggested that dyslipidemia has harmful effects on cognitive function and is inextricably involved in AD pathogenesis. Cholesterol is a vital molecule involved in neuronal development. Alteration in neuronal cholesterol levels affects Aß metabolism and results in neurodegeneration. Proprotein-convertase-subtilisin/kexin type-9 (PCSK9) was found to decrease neuronal cholesterol uptake by degradation of LDL-receptor related protein 1 (LRP-1) responsible for neuronal cholesterol uptake. Accordingly, this study was designed to evaluate the effect of PCSK9-inhibition by alirocumab (Aliro) in high-fat-cholesterol-diet (HFCD)-induced-AD-like condition. MAIN METHODS: Wistar Rats were divided into six groups; control; HFCD; HFCD and Memantine; HFCD and Aliro (4, 8 and 16 mg/kg/week) to test for ability of Aliro to modulate cognitive impairment, amyloidosis, brain cholesterol homeostasis and neuro-inflammation in HFCD-induced-AD-like condition. KEY FINDINGS: Our results demonstrated an association between PCSK9 inhibition by Aliro and amelioration of cognitive deficit, cholesterol hemostasis and reduction of neuro-inflammation. Aliro was able to alleviate hippocampal LRP-1expression levels and reduce brain cholesterol, hippocampal BACE1, Aß42, high-mobility-group-box-1 protein, receptor for advanced-glycation-end-products and toll like receptor-4 with subsequent decrease of different inflammatory mediators as nuclear-factor-kappa-B (NF-κB), tumor-necrosis-factor-alpha (TNF-α), interleukin-1beta (IL-1ß) and IL-6. SIGNIFICANCE: PCSK9-inhibition may represent a new therapeutic target in AD especially for HFCD-induced-AD-like condition.


Assuntos
Amiloidose/tratamento farmacológico , Anticorpos Monoclonais Humanizados/farmacologia , Colesterol/toxicidade , Disfunção Cognitiva/tratamento farmacológico , Dieta Hiperlipídica/efeitos adversos , Memantina/farmacologia , Amiloidose/etiologia , Amiloidose/metabolismo , Amiloidose/patologia , Animais , Disfunção Cognitiva/etiologia , Disfunção Cognitiva/metabolismo , Disfunção Cognitiva/patologia , Antagonistas de Aminoácidos Excitatórios/farmacologia , Ácido Glutâmico/metabolismo , Proteína HMGB1/genética , Proteína HMGB1/metabolismo , Hipocampo/efeitos dos fármacos , Hipocampo/metabolismo , Hipocampo/patologia , Masculino , Ratos , Ratos Wistar , Receptor para Produtos Finais de Glicação Avançada/genética , Receptor para Produtos Finais de Glicação Avançada/metabolismo , Receptor 4 Toll-Like/genética , Receptor 4 Toll-Like/metabolismo
16.
Acta Neuropathol Commun ; 9(1): 48, 2021 03 23.
Artigo em Inglês | MEDLINE | ID: mdl-33757599

RESUMO

Although abnormal accumulation of amyloid in the brain is an early biomarker of Alzheimer's disease (AD), wide variation in cognitive trajectories during life can be seen in the setting of brain amyloidosis, ranging from maintenance of normal function to progression to dementia. It is widely presumed that cognitive resilience (i.e., coping) to amyloidosis may be influenced by environmental, lifestyle, and inherited factors, but relatively little in specifics is known about this architecture. Here, we leveraged multimodal longitudinal data from a large, population-based sample of older adults to discover genetic factors associated with differential cognitive resilience to brain amyloidosis determined by positron emission tomography (PET). Among amyloid-PET positive older adults, the AD risk allele APOE ɛ4 was associated with worse longitudinal memory trajectories as expected, and was thus covaried in the main analyses. Through a genome-wide association study (GWAS), we uncovered a novel association with cognitive resilience on chromosome 8 at the MTMR7/CNOT7/ZDHHC2/VPS37A locus (p = 4.66 × 10-8, ß = 0.23), and demonstrated replication in an independent cohort. Post-hoc analyses confirmed this association as specific to the setting of elevated amyloid burden and not explained by differences in tau deposition or cerebrovascular disease. Complementary gene-based analyses and publically available functional data suggested that the causative variant at this locus may tag CNOT7 (CCR4-NOT Transcription Complex Subunit 7), a gene linked to synaptic plasticity and hippocampal-dependent learning and memory. Pathways related to cell adhesion and immune system activation displayed enrichment of association in the GWAS. Our findings, resulting from a unique study design, support the hypothesis that genetic heterogeneity is one of the factors that explains differential cognitive resilience to brain amyloidosis. Further characterization of the underlying biological mechanisms influencing cognitive resilience may facilitate improved prognostic counseling, therapeutic application, and trial enrollment in AD.


Assuntos
Doença de Alzheimer , Amiloidose , Encéfalo/patologia , Cognição/fisiologia , Exorribonucleases/genética , Proteínas Repressoras/genética , Idoso , Idoso de 80 Anos ou mais , Doença de Alzheimer/genética , Doença de Alzheimer/patologia , Amiloide/metabolismo , Amiloidose/genética , Amiloidose/patologia , Disfunção Cognitiva/etiologia , Disfunção Cognitiva/genética , Disfunção Cognitiva/patologia , Estudos de Coortes , Complexos Endossomais de Distribuição Requeridos para Transporte/genética , Feminino , Heterogeneidade Genética , Estudo de Associação Genômica Ampla , Humanos , Masculino , Tomografia por Emissão de Pósitrons , Proteínas Tirosina Fosfatases não Receptoras/genética
17.
Acta Neuropathol Commun ; 9(1): 56, 2021 03 30.
Artigo em Inglês | MEDLINE | ID: mdl-33785065

RESUMO

Amyloid-ß (Aß) misfolding is one of the hallmark pathological features of Alzheimer's disease (AD). AD can manifest with diverse symptomatology including variable rates of cognitive decline, duration of clinical disease, and other detrimental changes. Several reports suggest that conformational diversity in misfolded Aß is a leading factor for clinical variability in AD, analogous to what it has been described for prion strains in prion diseases. Notably, prion strains generate diverse patterns of misfolded protein deposition in the brains of affected individuals. Here, we tested the in vivo prion-like transmission features of four AD brains displaying particular patterns of amyloidosis. AD brains induced different phenotypes in recipient mice, as evaluated by their specific seeding activity, as well as the total amount of Aß deposited surrounding vascular structures and the reactivity of amyloid pathology to thioflavin S. Our results support the notion that AD-subtypes are encoded in disease-associated Aß. Further research exploring whether AD include a spectrum of different clinical conditions or syndromes may pave the way to personalized diagnosis and treatments.


Assuntos
Doença de Alzheimer/metabolismo , Doença de Alzheimer/patologia , Peptídeos beta-Amiloides/metabolismo , Encéfalo/metabolismo , Encéfalo/patologia , Idoso , Idoso de 80 Anos ou mais , Amiloidose/metabolismo , Amiloidose/patologia , Animais , Feminino , Humanos , Masculino , Camundongos , Camundongos Transgênicos , Pessoa de Meia-Idade
18.
Sci Rep ; 11(1): 6857, 2021 03 25.
Artigo em Inglês | MEDLINE | ID: mdl-33767265

RESUMO

Insulin balls, localized insulin amyloids formed at subcutaneous insulin-injection sites in patients with diabetes, cause poor glycemic control owing to impairments in insulin absorption. Our previous study has shown that some insulin balls are cytotoxic, but others are not, implying amyloid polymorphism. Interestingly, the patient with toxic insulin balls had been treated with antibiotic minocycline, suggesting a possible relationship between toxicity of insulin balls and minocycline. However, the direct effect of minocycline on the structure and cytotoxicity of the insulin amyloid is still unclear. Herein, we demonstrated that that minocycline at physiological concentrations induced degradation of insulin amyloids formed from human insulin and insulin drug preparations used for diabetes patients. Interestingly, the process involved the initial appearance of the toxic species, which subsequently changed into less-toxic species. It is also shown that the structure of the toxic species was similar to that of sonicated fragments of human insulin amyloids. Our study shed new light on the clarification of the revelation of insulin balls and the development of the insulin analogs for diabetes therapy.


Assuntos
Amiloide/metabolismo , Amiloidose/patologia , Antibacterianos/farmacologia , Insulina/metabolismo , Minociclina/farmacologia , Amiloide/efeitos dos fármacos , Amiloidose/induzido quimicamente , Antibacterianos/efeitos adversos , Células HeLa , Humanos , Insulina/química , Minociclina/efeitos adversos
19.
Hum Pathol ; 111: 52-58, 2021 05.
Artigo em Inglês | MEDLINE | ID: mdl-33639141

RESUMO

From 2009 to 2017, we identified 9 cases of plasma cell neoplasms on biopsies of the bladder in patients without a history of plasma cell myeloma or transplantation (6 men and 3 women). Four of the nine showed amyloid deposition, of which one additionally revealed a clear cell adenocarcinoma of the bladder. Follow-up was obtained in 7 cases. Of 3 cases (including 2 with amyloid) for which electrophoresis and immunofixation results were obtained, the 2 amyloid cases showed evidence of serum or urine paraproteins: serum IgM kappa in a patient with kappa light chain-restricted plasma cell neoplasm and urine IgA lambda in a patient with lambda light chain-restricted plasma cell neoplasm. By way of contrast, 1 case with kappa light chain-restricted plasma cell neoplasm in the absence of amyloid showed no serum monoclonal protein. Bone marrow biopsy results were obtained in the 2 amyloid cases revealing a population of 5% or less plasma cells with no assessment of clonality and, thus, were not diagnostic of plasma cell myeloma. In congruence, the 2 amyloid cases also showed no radiologic evidence of systemic plasma cell myeloma. One patient with plasma cell neoplasm only received chemotherapy and radiation without subsequent biopsies; one patient with plasma cell neoplasm, amyloid, and clear cell adenocarcinoma received radiation with an absence of neoplastic disease on subsequent biopsies. In addition, no evidence of systemic amyloid was found in the cases with bladder amyloidosis. Plasma cell neoplasms of the bladder, with and without amyloid deposition, are rare; this is the first known case series. In 7 cases with follow-up, plasma cell myeloma did not appear to manifest in a 1- to 127-month follow-up. However, paraproteins were identified on further testing in 2 cases with amyloid. Although bladder plasma cell neoplasms with and without amyloid tend to have a favorable prognosis in short-term follow-up, our study supports the need for additional workup for systemic disease, particularly in those with concurrent amyloidosis.


Assuntos
Neoplasias de Plasmócitos/patologia , Neoplasias da Bexiga Urinária/patologia , Idoso , Idoso de 80 Anos ou mais , Amiloidose/patologia , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Bexiga Urinária/patologia
20.
Sci Rep ; 11(1): 3563, 2021 02 11.
Artigo em Inglês | MEDLINE | ID: mdl-33574429

RESUMO

Telocytes are interstitial cells with long, thin processes by which they contact each other and form a network in the interstitium. Myocardial remodeling of adult patients with different forms of atrial fibrillation (AF) occurs with an increase in fibrosis, age-related isolated atrial amyloidosis (IAA), cardiomyocyte hypertrophy and myolysis. This study aimed to determine the ultrastructural and immunohistochemical features of cardiac telocytes in patients with AF and AF + IAA. IAA associated with accumulation of atrial natriuretic factor was detected in 4.3-25% biopsies of left (LAA) and 21.7-41.7% of right (RAA) atrial appendage myocardium. Telocytes were identified at ultrastructural level more often in AF + IAA, than in AF group and correlated with AF duration and mitral valve regurgitation. Telocytes had ultrastructural signs of synthetic, proliferative, and phagocytic activity. Telocytes corresponded to CD117+, vimentin+, CD34+, CD44+, CD68+, CD16+, S100-, CD105- immunophenotype. No significant differences in telocytes morphology and immunophenotype were found in patients with various forms of AF. CD68-positive cells were detected more often in AF + IAA than AF group. We assume that in aged AF + IAA patients remodeling of atrial myocardium provoked transformation of telocytes into "transitional forms" combining the morphological and immunohistochemical features with signs of fibroblast-, histiocyte- and endotheliocyte-like cells.


Assuntos
Amiloidose/imunologia , Fibrilação Atrial/imunologia , Cardiopatias Congênitas/imunologia , Telócitos/imunologia , Idoso , Amiloidose/complicações , Amiloidose/patologia , Apêndice Atrial/imunologia , Apêndice Atrial/patologia , Fibrilação Atrial/complicações , Fibrilação Atrial/patologia , Feminino , Átrios do Coração/imunologia , Átrios do Coração/patologia , Cardiopatias Congênitas/complicações , Cardiopatias Congênitas/patologia , Humanos , Imunofenotipagem , Masculino , Pessoa de Meia-Idade , Insuficiência da Valva Mitral/imunologia , Insuficiência da Valva Mitral/patologia , Miocárdio/imunologia , Miocárdio/patologia , Telócitos/patologia
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