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Journal articles on the topic 'Cardiac amyloidosi'

Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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1

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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2

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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3

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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4

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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5

Ruiz-Mori, Enrique, Leonor Ayala-Bustamante, Luis Taxa-Rojas, Cristian Pacheco-Román, Javier Alarcón-Santos, and Jorge Burgos-Bustamante. "Amiloidosis cardiaca: reporte de un caso." Horizonte Médico (Lima) 18, no. 4 (December 31, 2018): 81–89. http://dx.doi.org/10.24265/horizmed.2018.v18n4.12.

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6

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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7

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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8

Merlini, Giampaolo, David C. Seldin, and Morie A. Gertz. "Amyloidosis: Pathogenesis and New Therapeutic Options." Journal of Clinical Oncology 29, no. 14 (May 10, 2011): 1924–33. http://dx.doi.org/10.1200/jco.2010.32.2271.

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The systemic amyloidoses are a group of complex diseases caused by tissue deposition of misfolded proteins that results in progressive organ damage. The most common type, immunoglobulin light chain amyloidosis (AL), is caused by clonal plasma cells that produce misfolded light chains. The purpose of this review is to provide up-to-date information on diagnosis and treatment options for AL amyloidosis. Early, accurate diagnosis is the key to effective therapy, and unequivocal identification of the amyloidogenic protein may require advanced technologies and expertise. Prognosis is dominated by the extent of cardiac involvement, and cardiac staging directs the choice of therapy. Treatment for AL amyloidosis is highly individualized, determined on the basis of age, organ dysfunction, and regimen toxicities, and should be guided by biomarkers of hematologic and cardiac response. Alkylator-based chemotherapy is effective in almost two thirds of patients. Novel agents are also active, and trials are ongoing to establish their optimal use. Treatment algorithms will continue to be refined through controlled trials. Advances in basic research have led to the identification of new drug targets and therapeutic approaches, which will be integrated with chemotherapy in the future.

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9

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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10

Rameeva, A. S., V. V. Rameev, I. N. Bobkova, A. F. Safarova, Zh D. Kobalava, and S. V. Moiseev. "Leading Factors of Progression in Patients with Cardiac Amyloidosis." Rational Pharmacotherapy in Cardiology 18, no. 2 (May 5, 2022): 143–52. http://dx.doi.org/10.20996/1819-6446-2022-04-02.

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Aim. To describe prognostic meaning of cardiac and other principal clinical manifestations of systemic AL-amyloidosis in their interrelations.Material and methods. It has been made long-time survival analysis of 147 patients with systemic AL-amyloidosis. In the special investigation group (n=58) of AL (n=55) and ATTR (n=3) amyloidotic cardiopathy patients there were evaluated prognostically important structural and functional changes in myocardium with standard and impulse-wave tissue dopplerometric echocardiography in comparison with NTproBNP serum levels.Results. Even though significantly increased nowadays surviving of AL-amylodotic patients (Me=90 months) it has been found that as at previously time orthostatic hypotension and amyloid cardiopathy are being most severe initial syndromes (median 25 months), but after 1 year from diagnosis influence of these syndromes on surviving had decreased and most low surviving was more common in patients with CKD 3-5 (median 28 months). Influence of CKD 3-5 on surviving was associated predominantly with intracardial hemodynamics deterioration. Together with decreased systolic shortening strain rate (48,5%) decreased filtration rate (47,9%) was second of main factors contributing into NTproBNP increasing in effective multiple regression model (R=0,702, F(4,21)=5,095, p=0,005). NTproBNP level in less degree depended on renal clearance.Conclusion. Heart damage is one of the most prognostically unfavorable manifestations of systemic amyloidosis due to a sharp deterioration in the elastic properties of the myocardium, in the process of further development of amyloidosis, the leading factor in progression is the deterioration of the profile of cardiorenal interactions, the marker of which is the level of NTproBNP.

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11

Danková, M., and E. Gonçalvesová. "Amyloidová kardiomyopatia – zriedkavá alebo neodhalená? / Cardiac amyloidosis – rare or underdiagnosed?" Cardiology letters 29, no. 01 (2020): 17–25. http://dx.doi.org/10.4149/cardiol_2020_1_17.

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12

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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13

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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14

D'Souza, Anita, Keren Osman, Cristiana Costa Chase, Azah Borham, and Marianna Bruno. "The Hematologist's Role in Amyloidosis Management: Disease Awareness, Diagnostic Workup, and Practice Patterns." Blood 136, Supplement 1 (November 5, 2020): 28–29. http://dx.doi.org/10.1182/blood-2020-137740.

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Introduction: Systemic amyloidoses are progressive, life-threatening diseases characterized by the deposition of amyloid protein fibrils of varying origin in different tissues/organ systems (Merlini G, et al. N Engl J Med 2003;349:583-96). The precursor amyloidogenic protein influences the disease's clinical course, and identification of the specific protein is essential because treatment varies substantially by subtype. While there are 36 known proteins that can aggregate as amyloid in humans (Benson MD, et al. Amyloid 2018;25:215-9), the two most prevalent protein subtypes causing cardiac amyloidosis are derived from immunoglobulin light chains (AL) and transthyretin (ATTR) (Kittleson MM, et al. Circulation 2020;141:e7-22). Both AL and ATTR subtypes often infiltrate the heart, resulting in a restrictive cardiomyopathy along with other multiorgan involvement. Appropriate classification, early identification, and prompt treatment may substantially improve clinical outcomes. Because AL disease occurs in the context of plasma cell dyscrasia, hematologists can play an important role in amyloidosis suspicion, diagnostic workup, and management. However, differentiation of AL and ATTR amyloidoses in patients with signs of cardiac dysfunction is often challenging, and a multidisciplinary approach, including referral to cardiologists, is recommended early in the patient diagnostic workup. To gain insights into hematologists' disease awareness and practices, we interviewed hematologists involved in amyloidosis patient care across the US. Methods: A qualitative double-blind telephone survey was conducted between November 2019 and February 2020 of US hematologists who had diagnosed and/or treated at least 2 patients with AL amyloidosis over the past 2 years. The participants differed based on their experience in various clinical practice settings, including community hospital and private practices, academic institutions, and amyloidosis centers. Results: A total of 16 hematologists participated in the survey (community hospital, n=3; community private practice, n=5; academic institution, n=3; amyloidosis center, n=5). Hematologists at amyloidosis/academic centers (AAC) reported that the AL amyloidosis patient's journey typically involved visits to multiple primary care physicians and specialists in the community over a prolonged period (approximately 1 to 1.5 years) before the patient received a diagnosis (Figure [A]). Community specialists' referrals to academic physicians within the same specialty, due to lack of familiarity with amyloidosis centers, contributed in part to the delay. Several differences were found between hematologists in the community and those at AAC in level of disease awareness and referral/testing practices (Table; Figure [B]). Hematologists in community practice were less likely to be aware of ATTR amyloidosis, refer patients with suspected amyloid to cardiologists, or conduct recommended screening/diagnostic testing. In contrast, hematologists at AAC were highly aware of ATTR amyloidosis, collaborated closely with cardiologists, and used recommended amyloidosis tests. Across practice settings, hematologists consistently conducted biopsies of bone marrow and fat pad in patients with suspected AL amyloidosis to confirm the presence of amyloid. After amyloid was confirmed with Congo red staining, 75% of community hematologists discontinued testing, without establishing the amyloid protein subtype; hematologists at AAC consistently assessed amyloid protein subtype using immunohistochemistry and/or mass spectrometry to differentiate AL and ATTR prior to initiating treatment. Diagnostic algorithms supporting AL and ATTR differentiation were consistently in place and followed at AAC but not in community-based practices. Conclusions: Disease awareness, referral practices, and screening/testing procedures can differ between hematologists in the community setting and those in AAC. Community hematologists may benefit from additional education and wider use of diagnostic algorithms on AL/ATTR amyloidosis. Reinforcing the importance of cardiology referral and guidance on best practices for screening/biopsies/subtyping in patients with suspected amyloidosis who have cardiac symptoms should be prioritized. Disclosures D'Souza: Amgen, Merck, TenoBio: Research Funding; Akcea, Imbrium, Janssen, Pfizer: Consultancy. Costa Chase:Celgene: Speakers Bureau. Borham:Pfizer: Current Employment, Current equity holder in publicly-traded company. Bruno:Pfizer: Current Employment, Current equity holder in publicly-traded company.

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Itzhaki Ben Zadok, Osnat, and Ran Kornowski. "Cardiac Care of Patients with Cardiac Amyloidosis." Acta Haematologica 143, no. 4 (2020): 343–51. http://dx.doi.org/10.1159/000506919.

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Cardiac amyloidosis, the majority of cases of which are due to immunoglobulin light chain amyloidosis (AL) and transthyretin amyloidosis (ATTR), affects different aspects of the heart and cardiovascular system. Amyloid-induced cardiomyopathy, clinically manifesting with heart failure and electrophysiological abnormalities, has distinct characteristics compared to non-amyloid cardiomyopathies. Accordingly, specific management strategies are required. This paper will review the cardiovascular manifestations of patients with cardiac amyloidosis and their suggested treatment strategies, emphasizing the importance of multidisciplinary care.

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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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Butorov, Ekaterina A., and Olga V. Stukalova. "Role of cardiac MRI in the diagnosis of cardiac amyloidosis. Clinical cases." Clinical review for general practice 2, no. 2 (March 1, 2021): 16–20. http://dx.doi.org/10.47407/kr2021.2.2.00037.

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Purpose. The aim of this work is to show the capabilities of late gadolinium enhancement cardiac magnetic resonance imaging (MRI) in the diagnosis of a rare disease such as cardiac amyloidosis. Materials and methods. Demonstration of clinical cases detecting cardiac amyloidosis using MRI. Results. Contrast-enhanced cardiac MRI revealed patterns characteristic of cardiac amyloidosis. Conclusion. Cardiac MRI with late gadloinium enhancement is the method of choice in the diagnosis of cardiac amyloidosis.

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Abe, Temidayo, Eric Y. Chang, Gabrielle De Allie, Taiwo Ajose, Chukwuemeka Nwokike, and Nicolas Bakinde. "Rapid decline in ejection fraction and persistent elevation of troponin associated with cardiac amyloidosis." SAGE Open Medical Case Reports 8 (January 2020): 2050313X2092325. http://dx.doi.org/10.1177/2050313x20923259.

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Cardiac amyloidosis is an increasingly recognized cause of heart failure. It remains underdiagnosed despite a significant morbidity and mortality rate. The mean survival in patients with cardiac amyloidosis is less than 1 year in untreated primary light-chain amyloidosis and less than 4 years in wild-type transthyretin amyloidosis. We report a unique case of a 78-year-old male with transthyretin cardiac amyloidosis, who presented with persistently elevated troponin and progressive heart failure unresponsive to conventional therapy. With this case, we would like to highlight the role of cardiac biomarkers in the early diagnosis of cardiac amyloidosis.

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Li, Weijia, Dipan Uppal, Yu Chiang Wang, Xiaobo Xu, Damianos G. Kokkinidis, Mark I. Travin, and James M. Tauras. "Nuclear Imaging for the Diagnosis of Cardiac Amyloidosis in 2021." Diagnostics 11, no. 6 (May 30, 2021): 996. http://dx.doi.org/10.3390/diagnostics11060996.

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Cardiac amyloidosis is caused by the deposition of misfolded protein fibrils into the extracellular space of the heart. The diagnosis of cardiac amyloidosis remains challenging because of the heterogeneous manifestations of the disease. There are many different types of amyloidosis with light-chain (AL) amyloidosis and transthyretin (ATTR) amyloidosis being the most common types of cardiac amyloidosis. Endomyocardial biopsy is considered the gold standard for diagnosing cardiac amyloidosis and differentiating amyloid subtypes, but its use is limited because of the invasive nature of the procedure, with risks for complications and the need for specialized training and centers to perform the procedure. Radionuclide cardiac imaging has recently become the most commonly performed test for the diagnosis of ATTR amyloidosis but is of limited value for the diagnosis of AL amyloidosis. Positron emission tomography has been increasingly used for the diagnosis of cardiac amyloidosis and its applications are expected to expand in the future. Imaging protocols are under refinement to achieve better quantification of the disease burden and prediction of prognosis.

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Wechalekar, Ashutosh D., Helen J. Lachmann, Hugh J. B. Goodman, Arthur Bradwell, Philip N. Hawkins, and Julian D. Gillmore. "AL amyloidosis associated with IgM paraproteinemia: clinical profile and treatment outcome." Blood 112, no. 10 (November 15, 2008): 4009–16. http://dx.doi.org/10.1182/blood-2008-02-138156.

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AbstractAL amyloidosis associated with immunoglobulin M (IgM) paraproteinemia is rare. We report 103 consecutive such patients evaluated at the National Amyloidosis Centre (London, United Kingdom) between 1988 and 2006. Renal, cardiac, and lymph node amyloid was present in 53%, 35%, and 21% of patients, respectively, at presentation and 2 or more organs were involved in 54%. Seventy-three percent had an abnormal bone marrow infiltrate (lymphoid in 87%). The median IgM paraprotein was 8 g/L and serum free light chain (FLC) ratio was abnormal in 77 (88%) of 87. The abnormal FLC component was more than 100 mg/L in only 31% cases. Thirty-two percent achieved a partial hematologic response to treatment with no complete responders, and there appeared to be a greater response to combination regimens than single-agent oral alkylators (59% vs 20%, respectively; P = .003). Four achieved amyloidotic organ responses; organ function remained stable in 68%. None with lymph node involvement showed nodal improvement. Median overall survival was 49 months. AL amyloidosis with IgM paraproteinemia represents a distinctive subset of patients with AL amyloidosis who have a wider variety of underlying clonal disorders (often lymphoid) than AL in general, have low-level FLC abnormality, and should be treated with appropriately tailored chemotherapeutic regimens for the underlying clonal disorder.

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Di Nora, Concetta, Sandro Sponga, Chiara Nalli, Mauro Driussi, Igor Vendramin, Giovanni Benedetti, Giorgio Guzzi, Massimo Imazio, and Ugolino Livi. "Heart transplantation in cardiac amyloidosis." Vessel Plus 6 (2022): 46. http://dx.doi.org/10.20517/2574-1209.2021.126.

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It is known that the prognosis of patients affected by light-chain (AL) or transthyretin-related (TTR) amyloidosis is poor. TTR amyloidosis has usually shown a slower progression than AL amyloidosis, both hereditary TTR amyloidosis, where there is an inherited mutation in the DNA, and wild-type TTR amyloidosis, which usually affects the elderly. In this paper, the current literature about heart transplantation on cardiac amyloidosis patients is extensively reviewed. The two most frequent types of cardiac amyloidosis have been considered for heart transplantation: AL amyloidosis and wild-type TTR amyloidosis. According to this analysis, it is reasonable that heart transplantation may represent a valuable option in carefully selected patients. Moreover, it could improve prognosis, enabling autologous stem cell transplantation in the AL amyloidosis subgroup. In our humble opinion, it is mandatory to define a multidisciplinary approach to help select candidates to obtain the most effective results.

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Bonderman, Diana, Gerhard Pölzl, Klemens Ablasser, Hermine Agis, Stefan Aschauer, Michaela Auer-Grumbach, Christina Binder, et al. "Diagnosis and treatment of cardiac amyloidosis: an interdisciplinary consensus statement." Wiener klinische Wochenschrift 132, no. 23-24 (December 2020): 742–61. http://dx.doi.org/10.1007/s00508-020-01781-z.

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SummaryThe prevalence and significance of cardiac amyloidosis have been considerably underestimated in the past; however, the number of patients diagnosed with cardiac amyloidosis has increased significantly recently due to growing awareness of the disease, improved diagnostic capabilities and demographic trends. Specific therapies that improve patient prognosis have become available for certain types of cardiac amyloidosis. Thus, the earliest possible referral of patients with suspicion of cardiac amyloidosis to an experienced center is crucial to ensure rapid diagnosis, early initiation of treatment, and structured patient care. This requires intensive collaboration across several disciplines, and between resident physicians and specialized centers. The aim of this consensus statement is to provide guidance for the rapid and efficient diagnosis and treatment of light-chain amyloidosis and transthyretin amyloidosis, which are the most common forms of cardiac amyloidosis.

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23

Demko, I. V., L. I. Pelinovskaya, Irina A. Soloveva, A. Yu Kraposhina, N. V. Gordeeva, and V. A. Mosina. "Primary cardiac amyloidosis." Clinical Medicine (Russian Journal) 95, no. 11 (March 12, 2018): 971–76. http://dx.doi.org/10.18821/0023-2149-2017-95-11-971-976.

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Cardiac amyloidosis - the disease which is characterized by deposition of insoluble protein amyloid in intercellular space is one of the most severe implications of systemic amyloidosis. Primary cardiac amyloidosis possesses a wide range of clinical implications that complicates well-timed diagnostics and, respectively, treatment. The long latent current and the adverse forecast do extremely important diagnostics of cardiac amyloidosis at early stages of a disease. The modern concept of pathogenesis and morphology of an amyloidosis is covered in article, the clinical options of a current, diagnostic methods of dysfunction of heart including bio- and immunochemical blood analysis and urine, a complex of tool methods of a research and «the gold standard» of verification of deposits of amyloid - a biopsy of various organs and tissues are described.

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24

Lu, P., H. Van Acker, and P. Waer. "Cardiac amyloidosis." Journal of the Belgian Society of Radiology 98, no. 1 (February 1, 2015): 48. http://dx.doi.org/10.5334/jbr-btr.755.

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25

Yusuf, Syed Wamique, Amirreza Solhpour, Jose Banchs, Juan C. Lopez-Mattei, Jean-Bernard Durand, Cezar Iliescu, Saamir A. Hassan, and Muzaffar H. Qazilbash. "Cardiac amyloidosis." Expert Review of Cardiovascular Therapy 12, no. 2 (January 6, 2014): 265–77. http://dx.doi.org/10.1586/14779072.2014.876363.

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Gertz, Morie A. "Cardiac Amyloidosis." Heart Failure Clinics 18, no. 3 (July 2022): 479–88. http://dx.doi.org/10.1016/j.hfc.2022.02.005.

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Witteles, Ronald, and Bonnie Ky. "Cardiac Amyloidosis." JACC: CardioOncology 3, no. 4 (October 2021): 617–18. http://dx.doi.org/10.1016/j.jaccao.2021.09.002.

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Le, Dan, Rasheed Zaid, Jeffrey Dela Cruz, Faisal Nabi, and Dipan Shah. "Cardiac Amyloidosis." Methodist DeBakey Cardiovascular Journal 9, no. 4 (October 1, 2013): 237. http://dx.doi.org/10.14797/mdcvj.454.

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Le, Dan, Rasheed Zaid, Jeffrey Dela Cruz, Faisal Nabi, Stephen Little, and Dipan Shah. "Cardiac Amyloidosis." Methodist DeBakey Cardiovascular Journal 10, no. 2 (April 1, 2014): 130. http://dx.doi.org/10.14797/mdcvj.491.

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Elbdri, Salah, and Rachel Hajar. "Cardiac amyloidosis." Heart Views 22, no. 3 (2021): 231. http://dx.doi.org/10.4103/heartviews.heartviews_94_21.

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31

Kendall, Heather. "Cardiac Amyloidosis." Critical Care Nurse 30, no. 2 (April 1, 2010): 16–23. http://dx.doi.org/10.4037/ccn2009202.

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Martinez-Naharro, Ana, Philip N. Hawkins, and Marianna Fontana. "Cardiac amyloidosis." Clinical Medicine 18, Suppl 2 (April 1, 2018): s30—s35. http://dx.doi.org/10.7861/clinmedicine.18-2-s30.

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Maredia, Neil, and Simon G. Ray. "Cardiac amyloidosis." Clinical Medicine 5, no. 5 (September 1, 2005): 504–9. http://dx.doi.org/10.7861/clinmedicine.5-5-504.

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Myers, Bethan. "Cardiac amyloidosis." Clinical Medicine 5, no. 6 (November 1, 2005): 661.3–662. http://dx.doi.org/10.7861/clinmedicine.5-6-661b.

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Desai, Harit V., Wilbert S. Aronow, Stephen J. Peterson, and William H. Frishman. "Cardiac Amyloidosis." Cardiology in Review 18, no. 1 (January 2010): 1–11. http://dx.doi.org/10.1097/crd.0b013e3181bdba8f.

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REISINGER, JOHANN, SIMON W. DUBREY, and RODNEY H. FALK. "Cardiac Amyloidosis." Cardiology in Review 5, no. 6 (November 1997): 317–25. http://dx.doi.org/10.1097/00045415-199711000-00010.

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Eagle, Kim, and Pamela S. Douglas. "Cardiac Amyloidosis." New England Journal of Medicine 327, no. 22 (November 26, 1992): 1574. http://dx.doi.org/10.1056/nejm199211263272206.

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Yu, C. H., Y. H. Lu, and J. H. Lu. "Cardiac amyloidosis." QJM: An International Journal of Medicine 112, no. 2 (November 22, 2018): 131–32. http://dx.doi.org/10.1093/qjmed/hcy269.

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39

Le, Dan, Rasheed Zaid, Jeffrey Dela Cruz, Faisal Nabi, Stephen Little, and Dipan Shah. "Cardiac Amyloidosis." Methodist DeBakey Cardiovascular Journal 10, no. 2 (April 2014): 130. http://dx.doi.org/10.14797/mdcj-10-2-130.

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Le, Dan, Rasheed Zaid, Jeffrey Dela Cruz, Faisal Nabi, and Dipan Shah. "Cardiac Amyloidosis." Methodist DeBakey Cardiovascular Journal 9, no. 4 (October 2013): 237. http://dx.doi.org/10.14797/mdcj-9-4-237.

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41

Shabanova, S., and V. Huseynov. "Cardiac amyloidosis." Leukemia Research 85 (October 2019): S63. http://dx.doi.org/10.1016/s0145-2126(19)30360-1.

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Salah, Ali K., Agha Ahmed, Kunal N. Bodiwala, Elizabeth J. Manaloor, John W. Thornton, and David J. Moliterno. "Cardiac amyloidosis." Canadian Journal of Cardiology 24, no. 5 (May 2008): e35. http://dx.doi.org/10.1016/s0828-282x(08)70612-3.

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Dörler, J., and G. Pölzl. "Cardiac amyloidosis." memo - Magazine of European Medical Oncology 5, no. 1 (April 2012): 4–10. http://dx.doi.org/10.1007/s12254-012-0340-5.

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Giorgetti, Assuero, Dario Genovesi, Elisa Milan, Wanda Acampa, Raffaele Giubbini, Alberto Cuocolo, and Paolo Marzullo. "Cardiac amyloidosis." Clinical and Translational Imaging 7, no. 1 (January 2, 2019): 21–32. http://dx.doi.org/10.1007/s40336-018-00311-2.

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Kyle, Robert A., and Morie A. Gertz. "Cardiac amyloidosis." International Journal of Cardiology 28, no. 2 (August 1990): 139–41. http://dx.doi.org/10.1016/0167-5273(90)90053-8.

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Falk, Rodney H. "Cardiac Amyloidosis." Circulation 124, no. 9 (August 30, 2011): 1079–85. http://dx.doi.org/10.1161/circulationaha.110.010447.

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LEINONEN, HANNU, and SINIKKA POHJOLA-SINTONEN. "Cardiac Amyloidosis." Acta Medica Scandinavica 219, no. 1 (April 24, 2009): 125–28. http://dx.doi.org/10.1111/j.0954-6820.1986.tb03285.x.

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Joynt Maddox, Karen E., and Kathleen W. Zhang. "Cardiac Amyloidosis." JACC: CardioOncology 2, no. 5 (December 2020): 719–20. http://dx.doi.org/10.1016/j.jaccao.2020.10.008.

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Ananthakrishna, Rajiv, Rachael Lloyd, Bryone J. Kuss, and Joseph B. Selvanayagam. "Cardiac Amyloidosis." JACC: Case Reports 2, no. 2 (February 2020): 282–85. http://dx.doi.org/10.1016/j.jaccas.2019.11.041.

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Hare, James L. "Cardiac Amyloidosis." JACC: Cardiovascular Imaging 13, no. 4 (April 2020): 921–23. http://dx.doi.org/10.1016/j.jcmg.2019.11.004.

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