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  1 / 17410 MEDLINE  
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[PMID]:29505515
[Au] Autor:Matsumoto K; Kikuchi J; Kaneko Y; Yasuoka H; Suzuki K; Tokuyama H; Kameyama K; Yamaoka K; Takeuchi T
[Ad] Endereço:Division of Rheumatology.
[Ti] Título:Persistent fever and destructive arthritis caused by dialysis-related amyloidosis: A case report.
[So] Source:Medicine (Baltimore);97(1):e9359, 2018 Jan.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RATIONALE: Dialysis-related amyloidosis (DRA) can present rheumatic manifestations in patients on long-term hemodialysis. Typical articular symptoms with DRA involve carpal-tunnel syndrome, effusion in large joints, spondyloarthropathy, or cystic bone lesions, which are usually with non-inflammatory processes. PATIENT CONCERNS: A 64-year-old man on hemodialysis for >30 years was admitted because of intermittent fever, polyarthritis, and elevated serum C-reactive protein (CRP) level, which was continuous for 2 years. Several antibiotics were ineffective for 3 months before his admission. On physical examination, joint swelling was observed at bilateral wrists, knees, ankles, and hip joints. Laboratory tests revealed elevation of serum inflammatory markers and ß2-microglobulin (ß2-MG). Synovial fluid showed predominant infiltration of polymorphonuclear leukocytes and the increase of ß2-MG level. DIAGNOSIS: Significant deposition of ß2-MG with inflammatory cell infiltration was found in biopsied samples from synovium, skin, and ileum. INTERVENTIONS: We decided to switch to the hemodialysis column with membrane that can effectively absorb ß2-MG in circulation. OUTCOMES: The relief of symptoms and a decrease of CRP level by changing the membrane lead to the final diagnosis of DRA. LESSONS: Our case demonstrates that DRA arthropathy can be inflammatory and destructive, and also develop systemic inflammatory signs and symptoms. In such cases, aggressive absorption of ß2-MG in circulation might help the amelioration of symptoms.
[Mh] Termos MeSH primário: Amiloidose/complicações
Artrite/etiologia
Diálise Renal/efeitos adversos
[Mh] Termos MeSH secundário: Artrite/diagnóstico por imagem
Seres Humanos
Masculino
Meia-Idade
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:180306
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000009359


  2 / 17410 MEDLINE  
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[PMID]:29400028
[Au] Autor:Huart C; Renaudin Autain K; Barbey C; Lescanne E; Malard O
[Ti] Título:[ENT localisation of amyloidosis: 20 patients report].
[So] Source:Rev Laryngol Otol Rhinol (Bord);136(3):103-7, 2015.
[Is] ISSN:0035-1334
[Cp] País de publicação:France
[La] Idioma:fre
[Ab] Resumo:Background: Amyloidosis is a rare pathology, due to a toxic accumulation of amyloid proteins infiltrating tissues. Published studies have low statistical power. However it seems that ENT localization have favorable prognosis. Management and check up are not well codified. Methods: Bicentric retros­pec­tive study conducted between 1987 and 2015, from patient diagnosed with ENT amyloidosis. The study was performed to the database of the pathology department. People concerned, history, symptoms and diagnostic features were analysed. The immunologic and clinical status, locations, extension check, treatment and prognosis have been evaluated. Results: Twenty patients were evaluated, ten men and ten women, average age was 55.5 year of age. Three patients were afflicted with familial amyloidosis. Main localisation was larynx (80%), main type was immunoglobulinic (AL) (80%). Amyloidosis was mostly localised (90%) and primary form (80%). Dysphonia was the most frequently encountered symptom. Most performed exami­na­tion were local biopsy and creatinine clearance (100%), serum protein electrophoresis (SEP) (89%), myelogram and/or bone marrow aspiration (75%), and trans thoracic echography (TTE) (75%). Surgical removal was performed for 75% of the patients. Global rate of recurrence was 70%, about 4.6 years after diagnosis. In familial forms, overall survival was 66% at ten years. In non-familial forms, overall survival was 100%. Conclusion: ENT amyloidosis are mostly AL, laryngeal, prima­ry and localised. Distant extension check should be managed by internal medicine specialist and associate creati­ni­ne clea­ran­ce, local biopsy, TTE, SEP and myelogram. Head and neck forms treatment is based on surgical removal, familial forms are of poor prognosis.
[Mh] Termos MeSH primário: Amiloidose/diagnóstico
Amiloidose/terapia
Otorrinolaringopatias/diagnóstico
Otorrinolaringopatias/terapia
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Masculino
Meia-Idade
Recidiva
Estudos Retrospectivos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180206
[St] Status:MEDLINE


  3 / 17410 MEDLINE  
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[PMID]:29429161
[Au] Autor:Li L; Duan XJ; Sun Y; Lu Y; Xu HY; Wang QZ; Wang HY
[Ad] Endereço:Department of Pathology, Fuwai Hospital, Chinese Academy of Medical Sciences, Beijing 100037, China.
[Ti] Título:[Classification of cardiac amyloidosis: an immunohistochemical analysis].
[So] Source:Zhonghua Bing Li Xue Za Zhi;47(2):105-109, 2018 Feb 08.
[Is] ISSN:0529-5807
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:To evaluate the sensitivity and specificity of immunohistochemistry (IHC) in the classification of cardiac amyloidosis on endomyocardial biopsy (EMB) and heart allograft. Twenty cardiac tissues from 19 patients at Fuwai Hospital from January, 1990 to April, 2017 with histopathologic features of amyloidosis and Congo red staining positivity were included. IHC was performed with monoclonal antibodies against AA amyloid and polyclonal antibodies against transthyretin (ATTR), λ-light chain (AL-λ), κ-light chain (AL-κ), ApoAâ… , ApoAâ…¡, ApoA â…£ and ß(2)-microglobin. The extent of interstitial staining was evaluated by light microscopy, and three patterns were recognized; these included diffuse pericellular pattern, discrete pericellular pattern, and nodular pattern. Two patterns of vascular deposition were also noted, including arterial pattern and venous pattern. Endocardial involvement was also assessed and recorded. Nineteen cases were divided into three groups according to the pattern of proteins expression in specimens. The first group (5 cases) only showed single protein expression on EMB. The second group (6 cases) showed more than one protein expression, but one of them was intensely stained or any staining of any protein together with ApoA â…£ co-staining. The third group (8 cases) also showed more than one protein expression and all of them had intense staining. Amyloid deposits were successfully subtyped as AL-λ, ATTR, AL-κ and ApoAâ… by IHC in the former two groups with the sensitivity of 11/19. In the third group, amyloid deposits could not be subtyped by immunohistochemistry due to their poor specificity. The pericellular pattern tended to favor AL over ATTR amyloidosis and vascular deposition tended to favor ATTR. Amyloid deposits can be reliably subtyped in diagnostic cardiac specimens using IHC. The co-deposition of chaperon proteins, the distribution of amyloid proteins and clinical features are also auxiliary to subtype cardiac amyloidosis.
[Mh] Termos MeSH primário: Amiloidose/patologia
Cardiomiopatias/patologia
[Mh] Termos MeSH secundário: Amiloide/análise
Neuropatias Amiloides Familiares/patologia
Anticorpos Monoclonais/análise
Apolipoproteína A-I/análise
Apolipoproteínas A/análise
Biópsia
Seres Humanos
Cadeias kappa de Imunoglobulina/análise
Cadeias lambda de Imunoglobulina/análise
Imuno-Histoquímica
Placa Amiloide/patologia
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (APOA1 protein, human); 0 (Amyloid); 0 (Antibodies, Monoclonal); 0 (Apolipoprotein A-I); 0 (Apolipoproteins A); 0 (Immunoglobulin kappa-Chains); 0 (Immunoglobulin lambda-Chains); 0 (apolipoprotein A-IV)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180213
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.0529-5807.2018.02.005


  4 / 17410 MEDLINE  
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[PMID]:29390268
[Au] Autor:Sun L; Zhang L; Hu W; Li TF; Liu S
[Ad] Endereço:Department of Rheumatology and Clinical Immunology, The First Affiliated Hospital of Zhengzhou University, Zhengzhou, China.
[Ti] Título:Case report: One case of primary AL amyloidosis repeatedly misdiagnosed as scleroderma.
[So] Source:Medicine (Baltimore);96(50):e8771, 2017 Dec.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Amyloid light chain (AL) results from the deposition of immunoglobulin light chain fragments, and can affect multiple organs/systems. Our patient was diagnosed as scleroderma repeatedly because of extensive skin thickening and hardening, but the treatment was not effective. We did extensive laboratory examinations including serum/urine protein electrophoresis and flow cytometry assay of bone marrow aspiration. CONCLUSION: A diagnosis of primary AL amyloidosis was established.
[Mh] Termos MeSH primário: Amiloidose/diagnóstico
Erros de Diagnóstico
[Mh] Termos MeSH secundário: Biópsia
Transtornos de Deglutição/etiologia
Feminino
Rouquidão/etiologia
Seres Humanos
Macroglossia/etiologia
Meia-Idade
Esclerodermia Localizada/diagnóstico
Pele/patologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:180203
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000008771


  5 / 17410 MEDLINE  
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[PMID]:29365380
[Au] Autor:Li LJ; Du C; Wang L; Yan Y; Zeng J; Xu CY; Sun SL
[Ad] Endereço:Department of Otorhinolaryngology Head and Neck Surgery, Peking University Third Hospital, Beijing 100191, China.
[Ti] Título:[Application of endoscope assisted curved laryngoscopy technique in transoral laryngopharyngeal minimally invasive surgery].
[So] Source:Zhonghua Er Bi Yan Hou Tou Jing Wai Ke Za Zhi;53(1):45-48, 2018 Jan 07.
[Is] ISSN:1673-0860
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:To explore the possibility of endoscope assisted curved laryngoscopy technique applied in transoral laryngopharyngeal minimally invasive surgery and evaluate the advantages of this technique. Eight patients with huge benign lesions in larynx and pharynx undergoing transoral microsurgery at Peking University Third Hospital between February 2016 and February 2017 were enrolled in this study.The diagnosis included cyst at the base of tongue in two patients, cysts in the epiglottis in two patients, hemangioma in two patients, multiple masses of the hypopharynx and amyloidosis in supraglottic area in one patient each.The time and exposure during surgery, occurrence rate of complication and conditions of following-up were recorded. The mean time of surgery was 20 min, the exposure was satisfying.There was no obvious complication after surgery.No residual or recurrent lesion was observed after 1 to 12 months follow-up(mean time 4.5 months). The endoscope assisted curved laryngoscopy technique has advantages in shortening the time of surgery, improving exposure and reducing the rate of complication and recurrence.
[Mh] Termos MeSH primário: Doenças da Laringe/cirurgia
Laringoscópios
Laringoscopia/instrumentação
Laringoscopia/métodos
[Mh] Termos MeSH secundário: Amiloidose/cirurgia
Cistos/cirurgia
Epiglote/cirurgia
Desenho de Equipamento
Hemangioma/cirurgia
Seres Humanos
Hipofaringe/cirurgia
Microcirurgia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180125
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.1673-0860.2018.01.010


  6 / 17410 MEDLINE  
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[PMID]:28456755
[Au] Autor:Grogan M; Dispenzieri A; Gertz MA
[Ad] Endereço:Division of Cardiovascular Diseases, Department of Medicine, Mayo Clinic, Rochester, Minnesota, USA.
[Ti] Título:Light-chain cardiac amyloidosis: strategies to promote early diagnosis and cardiac response.
[So] Source:Heart;103(14):1065-1072, 2017 07.
[Is] ISSN:1468-201X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Amyloid light chain (AL) amyloidosis is a systemic disease characterised by the aggregation of misfolded immunoglobulin light chain (LC), predominantly in the heart and kidneys, causing organ failure. If untreated, the median survival of patients with cardiac AL amyloidosis is 6 months from the onset of heart failure. Protracted time to establish a diagnosis, often lasting >1 year, is a frequent factor in poor treatment outcomes. Cardiologists, to whom patients are often referred, frequently miss the opportunity to diagnose cardiac AL amyloidosis. Nearly all typical cardiac support measures, with the exception of diuretics, are ineffective and may even worsen clinical symptoms, emphasising the need for accurate diagnosis. Patients with severe cardiac involvement face poor outcomes; heart transplantation is rarely an option because of multiorgan involvement, rapid clinical decline and challenges in predicting which patients will respond to treatment of the underlying plasma cell disorder. Early diagnosis and prompt treatment with ââ'¬ËÅ“source therapiesââ'¬â"¢ that limit the production of amyloidogenic LC are associated with better survival and improvement in organ function after a median of 2.4 months following haematological complete response. However, organ recovery is often incomplete because these source therapies do not directly target deposited amyloid. Emerging amyloid-directed therapies may attenuate, and potentially reverse, organ dysfunction by clearing existing amyloid and inhibiting fibril formation of circulating aggregates. Improved recognition of AL amyloidosis by cardiologists allows for earlier treatment and improved outcomes.
[Mh] Termos MeSH primário: Amiloidose/diagnóstico
Cardiomiopatias/diagnóstico
Diagnóstico Precoce
Insuficiência Cardíaca/etiologia
Cadeias Leves de Imunoglobulina/metabolismo
Guias de Prática Clínica como Assunto
[Mh] Termos MeSH secundário: Amiloidose/complicações
Cardiomiopatias/complicações
Insuficiência Cardíaca/diagnóstico
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Immunoglobulin Light Chains)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180126
[Lr] Data última revisão:
180126
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE
[do] DOI:10.1136/heartjnl-2016-310704


  7 / 17410 MEDLINE  
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[PMID]:29216449
[Au] Autor:Liu CC; Zhao N; Fu Y; Wang N; Linares C; Tsai CW; Bu G
[Ad] Endereço:Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA. Electronic address: liu.chiachen@mayo.edu.
[Ti] Título:ApoE4 Accelerates Early Seeding of Amyloid Pathology.
[So] Source:Neuron;96(5):1024-1032.e3, 2017 Dec 06.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Accumulation and aggregation of amyloid-ß (Aß) in the brain is an initiating step in the pathogenesis of Alzheimer's disease (AD). The ε4 allele of apolipoprotein E (apoE) gene is the strongest genetic risk factor for late-onset AD. Although there is strong evidence showing that apoE4 enhances amyloid pathology, it is not clear what the critical stage(s) is during amyloid development in which apoE4 has the strongest impact. Using apoE inducible mouse models, we show that increased expression of astrocytic apoE4, but not apoE3, during the seeding stage of amyloid development enhanced amyloid deposition and neuritic dystrophy in amyloid model mice. ApoE4, but not apoE3, significantly increased brain Aß half-life measured by in vivo microdialysis. Furthermore, apoE4 expression increased whereas apoE3 reduced amyloid-related gliosis in the mouse brains. Together, our results demonstrate that apoE4 has the greatest impact on amyloid during the seeding stage, likely by perturbing Aß clearance and enhancing Aß aggregation.
[Mh] Termos MeSH primário: Amiloidose/patologia
Apolipoproteína E4/farmacologia
[Mh] Termos MeSH secundário: Doença de Alzheimer/patologia
Amiloidose/genética
Animais
Apolipoproteína E3/farmacologia
Astrócitos/efeitos dos fármacos
Astrócitos/metabolismo
Astrócitos/patologia
Encéfalo/patologia
Técnicas de Introdução de Genes
Gliose/patologia
Seres Humanos
Camundongos
Camundongos Transgênicos
Neuritos/efeitos dos fármacos
Neuritos/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoprotein E3); 0 (Apolipoprotein E4)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180121
[Lr] Data última revisão:
180121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE


  8 / 17410 MEDLINE  
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[PMID]:29176541
[Au] Autor:Junejo S; Ali Y; Singh Lubana S; Tuli SS
[Ad] Endereço:Icahn School of Medicine at Mount Sinai-Queens Hospital Center, Jamaica, NY, USA.
[Ti] Título:Diffuse Peritoneal and Bowel Wall Infiltration by Light Chain-AL Amyloidosis with Omental Calcification Mimicking Abdominal Carcinomatosis - An Elderly Female with Incidental Finding of Light Chain Monoclonal Gammopathy of Undetermined Significance (LC-MGUS).
[So] Source:Am J Case Rep;18:1247-1250, 2017 Nov 25.
[Is] ISSN:1941-5923
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND Amyloidosis is the extracellular tissue deposition of plasma proteins, which after conformational changes, forms antiparallel beta pleated sheets of fibrils. Amyloid light-chain (AL) is a type of amyloidosis that is due to deposition of proteins derived from immunoglobulin (Ig) light chains. Gastrointestinal tract (GIT) involvement most often found in amyloid A (AA) amyloidosis type. There have been no reports of obstructive GIT AL amyloid patients having monoclonal gammopathy of undetermined significance (MGUS). Our case is the first case to show two coinciding conditions; one is the association of GIT AL amyloidosis with the incidental finding of a rare type of MGUS (LC-MGUS) and the other is the radiologic presentation of GIT amyloidosis with omental calcification mimicking the GIT malignancy. CASE REPORT A 68-year-old female presented with symptoms of partial bowel obstruction, including intermittent diffuse abdominal pain and constipation. After computed tomography (CT) abdomen and pelvis, an exploratory laparotomy was needed because of suspicion of abdominal carcinomatosis due to diffuse omental calcification. The tissue sent for biopsy surprisingly showed AL amyloidosis. The patient did not report any systemic symptoms. Further workup was advised to inquire about the plasma cell dyscrasia which eventually turned into a very rare version of MGUS knows as light chain MGUS (LC-MGUS). Following adequate resection of the involved structures, the patient was then placed on chemotherapy and successfully went into remission. CONCLUSIONS This case report illustrates that in an era of evidence based medicine, it is important to show through case reports the association of GIT AL amyloidosis with LC-MGUS, as the literature on this topic is lacking. It also points to the importance of timely intervention that can greatly enhance, not only the only the chances of remission but also prevention of further complications such as malignant transformation.
[Mh] Termos MeSH primário: Amiloidose/diagnóstico
Calcinose/diagnóstico
Gamopatia Monoclonal de Significância Indeterminada/diagnóstico
Omento/patologia
Doenças Peritoneais/diagnóstico
[Mh] Termos MeSH secundário: Neoplasias Abdominais/diagnóstico
Idoso
Diagnóstico Diferencial
Feminino
Seres Humanos
Achados Incidentais
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180109
[Lr] Data última revisão:
180109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


  9 / 17410 MEDLINE  
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[PMID]:28468825
[Au] Autor:Marcinko TM; Dong J; LeBlanc R; Daborowski KV; Vachet RW
[Ad] Endereço:From the Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003.
[Ti] Título:Small molecule-mediated inhibition of ß-2-microglobulin-based amyloid fibril formation.
[So] Source:J Biol Chem;292(25):10630-10638, 2017 06 23.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In dialysis patients, ß-2 microglobulin (ß2m) can aggregate and eventually form amyloid fibrils in a condition known as dialysis-related amyloidosis, which deleteriously affects joint and bone function. Recently, several small molecules have been identified as potential inhibitors of ß2m amyloid formation Here we investigated whether these molecules are more broadly applicable inhibitors of ß2m amyloid formation by studying their effect on Cu(II)-induced ß2m amyloid formation. Using a variety of biophysical techniques, we also examined their inhibitory mechanisms. We found that two molecules, doxycycline and rifamycin SV, can inhibit ß2m amyloid formation by causing the formation of amorphous, redissolvable aggregates. Rather than interfering with ß2m amyloid formation at the monomer stage, we found that doxycycline and rifamycin SV exert their effect by binding to oligomeric species both in solution and in gas phase. Their binding results in a diversion of the expected Cu(II)-induced progression of oligomers toward a heterogeneous collection of oligomers, including trimers and pentamers, that ultimately matures into amorphous aggregates. Using ion mobility mass spectrometry, we show that both inhibitors promote the compaction of the initially formed ß2m dimer, which causes the formation of other off-pathway and amyloid-incompetent oligomers that are isomeric with amyloid-competent oligomers in some cases. Overall, our results suggest that doxycycline and rifamycin are general inhibitors of Cu(II)-induced ß2m amyloid formation. Interestingly, the putative mechanism of their activity is different depending on how amyloid formation is initiated with ß2m, which underscores the complexity of how these structures assemble .
[Mh] Termos MeSH primário: Amiloide/química
Cobre/química
Doxiciclina/química
Agregados Proteicos
Rifampina/química
Microglobulina-2 beta/química
[Mh] Termos MeSH secundário: Amiloide/metabolismo
Amiloidose/etiologia
Amiloidose/metabolismo
Cobre/metabolismo
Seres Humanos
Diálise Renal/efeitos adversos
Microglobulina-2 beta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Amyloid); 0 (Protein Aggregates); 0 (beta 2-Microglobulin); 789U1901C5 (Copper); N12000U13O (Doxycycline); VJT6J7R4TR (Rifampin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.774083


  10 / 17410 MEDLINE  
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[PMID]:29200282
[Au] Autor:Morgan GJ; Usher GA; Kelly JW
[Ad] Endereço:Departments of Chemistry and Molecular Medicine, and ‡The Skaggs Institute for Chemical Biology, The Scripps Research Institute , La Jolla, California 92037, United States.
[Ti] Título:Incomplete Refolding of Antibody Light Chains to Non-Native, Protease-Sensitive Conformations Leads to Aggregation: A Mechanism of Amyloidogenesis in Patients?
[So] Source:Biochemistry;56(50):6597-6614, 2017 Dec 19.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genetic, biochemical, and pharmacologic evidence supports the hypothesis that conformationally altered or misfolded protein states enable aggregation and cytotoxicity in the systemic amyloid diseases. Reversible structural fluctuations of natively folded proteins are involved in the aggregation of many degenerative disease associated proteins. Herein, we use antibody light chains (LCs) that form amyloid fibrils in AL amyloidosis to consider an alternative hypothesis of amyloidogenesis: that transient unfolding and incomplete extracellular refolding of secreted proteins can lead to metastable, alternatively folded states that are more susceptible to aggregation or to endoproteolysis that can release aggregation-prone fragments. Refolding of full-length λ6a LC dimers comprising an interchain disulfide bond from heat- or chaotrope-denatured ensembles in buffers yields the native dimeric state as well as alternatively folded dimers and aggregates. LC variants lacking an interchain disulfide bond appear to refold fully reversibly to the native state. The conformation of a backbone peptidyl-proline amide in the LC constant domain, which is cis in the native state, may determine whether the LC refolds back to the native state. A proline to alanine (P147A) LC variant, which cannot form the native cis-amide conformation, forms amyloid fibrils from the alternatively folded ensemble, whereas all the full-length λ6a LCs we have studied to date do not form amyloid under analogous conditions. P147A LC variants are susceptible to endoproteolysis by thrombin, enabling amyloidogenesis of the fragments released. Thus, non-native LC structural ensembles containing a tyrosine 146-proline 147 trans-amide bond can initiate and propagate amyloid formation, either directly or after aberrant endoproteolysis.
[Mh] Termos MeSH primário: Amiloidose/metabolismo
Cadeias Leves de Imunoglobulina/química
Cadeias Leves de Imunoglobulina/metabolismo
[Mh] Termos MeSH secundário: Alanina/química
Amiloide/química
Dicroísmo Circular
Endopeptidases/metabolismo
Seres Humanos
Cadeias Leves de Imunoglobulina/genética
Cinética
Modelos Moleculares
Prolina/química
Agregados Proteicos/fisiologia
Conformação Proteica
Dobramento de Proteína
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid); 0 (Immunoglobulin Light Chains); 0 (Protein Aggregates); 9DLQ4CIU6V (Proline); EC 3.4.- (Endopeptidases); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00579



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