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Infiltrative Diseases
Published in Andreas P. Kalogeropoulos, Hal A. Skopicki, Javed Butler, Heart Failure, 2023
The characteristic appearance of cardiac amyloidosis is increased biventricular wall thickness and severe diastolic dysfunction. Common symptoms associated with cardiac amyloidosis include fatigue and dyspnea, along with other non-specific findings of HF. Physical examination findings are often consistent with right-sided HF, including elevated jugular venous distention, abdominal ascites, and lower extremity edema.
Diabetes Mellitus, Obesity, Lipoprotein Disorders and other Metabolic Diseases
Published in John S. Axford, Chris A. O'Callaghan, Medicine for Finals and Beyond, 2023
Amyloid light-chain (AL) amyloidosis, the commonest type of amyloidosis, complicates 5–10% of cases of myeloma and other monoclonal B-cell dyscrasias. Amyloid A (AA) amyloidosis develops in 1–5% of patients with chronic inflammatory disorders. β2-microglobulin amyloid deposition in the bones and joints can arise with long-term dialysis. Hereditary systemic amyloidosis can be caused by mutations in various genes and accounts for up to 5% of cases.
Metabolic Myopathy
Published in Maher Kurdi, Neuromuscular Pathology Made Easy, 2021
Amyloid myopathy is an uncommon metabolic disease characterized by abnormal deposition of amyloid proteins in muscle fibers. Patients may present with early peripheral neuropathy followed by myopathy. Widespread deposition of amyloid may cause systemic amyloidosis that ends with organ damage. The diagnosis is always difficult in clinical ground as amyloidosis is rarely suspected in clinician thoughts. Amyloidosis could be primary due to sporadic or inherited gene mutations or secondary, resulting from underlying chronic illness. A rare example of inherited or sporadic cases is amyloid deposition due to transthyretin. Muscle biopsy demonstrates perivascular and perimysial amyloid deposition. With using EM, the vessels and muscle fibers are lined with elongated and thin amyloid fibrils, frequently seen on the basal lamina.
Spontaneous periocular ecchymosis: a major review
Published in Orbit, 2023
Matthew J. Hartley, Pav Gounder, Huw Oliphant
Amyloidosis encompasses a group of rare diseases of abnormal synthesis and deposition of proteinaceous aggregates throughout the body.18 When these misfolded proteins accumulate, known as amyloid fibrils, they can become toxic to tissues within the kidneys and heart, liver, brain, gastrointestinal tract, and vascular architecture. Light-chain (AL) amyloidosis is the most common form, where dysplastic plasma cells of the bone marrow synthesize abnormal proteins. Although light-chain amyloidosis is not a true malignancy, multiple myeloma can co-exist in 10% of these patients due to a similar pathophysiological derivation.19 Despite improvements in recent decades, there is still significant mortality associated with amyloidosis, with overall survival being 48% at 5 years in one longitudinal study.20
Tissue biopsy for the diagnosis of amyloidosis: experience from some centres
Published in Amyloid, 2022
Merrill D. Benson, John L. Berk, Angela Dispenzieri, Thibaud Damy, Julian D. Gillmore, Bouke P. Hazenberg, Francesca Lavatelli, Maria M. Picken, Christoph Röcken, Stefan Schönland, Mitsuharu Ueda, Per Westermark
Diagnosis of amyloidosis is usually based on demonstration of amyloid deposits in a tissue biopsy. A definitive diagnosis has become increasingly important since a number of impactful treatment options have developed. The clinical and biologic diversity of amyloidosis conditions emphasises the need for refined and exact analysis of the deposited material. Evolution of such analyses has occurred independently at the relatively few different specialised centres around the world. In this way, a number of distinct but partially complementary methods have emerged. The purpose of this clinical practice summary of experts is to describe some important steps in biopsy procedures and diagnostic tools in the diagnostic work-up of amyloid and amyloidosis and provide examples of alternative methods. In addition, we wish to point out some challenges and pitfalls. The specific signs, symptoms and conditions warranting suspicion of amyloidosis that underlie the decision to obtain a biopsy fall beyond the scope of this article.
Incidence rate of hospitalization and mortality in the first year following initial diagnosis of cardiac amyloidosis in the US claims databases
Published in Current Medical Research and Opinion, 2021
Lu Wang, Joel N. Swerdel, James Weaver, Brendan Weiss, Guohua Pan, Zhong Yuan, Peter M. DiBattiste
Amyloidosis is a group of rare diseases in which amyloid fibrils, composed of low-molecular-weight subunits (5–25 kD) of unrelated proteins, build up in extracellular tissue1. The pathophysiology involves the mis-folding of native proteins resulting from excess production, cleavage, or denaturation of precursor proteins, which eventually form insoluble amyloid fibrils2,3 and disrupt the structure and function of involved organs and tissues4. Systemic amyloidosis are classified into subtypes based on precursor proteins that form the fibril deposits: immunoglobulin light chain amyloidosis (AL), secondary amyloidosis (AA), transthyretin amyloidosis (ATTR) which is divided into a mutant or variant-type (ATTRm) and a wild-type (ATTRwt), and dialysis-related amyloidosis (Aβ2M)5, are among the most common. The prognosis of amyloidosis is generally poor, but varies by the amount of amyloidogenic protein and the extent and the number of organs involved6. Different subtypes of amyloidosis tend to have different natural history. Of the major subtypes, AL and ATTR commonly involve the heart, and the prognoses are worse than other subtypes7.