Related Experiment Video
Updated: Aug 11, 2026
09:41
Performing and Processing FNA of Anterior Fat Pad for Amyloid
Published on: October 31, 2010
Primary cardiac amyloidosis with pathologic hip fracture secondary to bone amyloid
A S Sundar1, K K Talwar, P Chopra
1Department of Cardiology, All India Institute of Medical Sciences, New Delhi.
International Journal of Cardiology
|February 1, 1989
Insights
A rare case of cardiac and bone amyloidosis occurred in a 39-year-old female, presenting with restrictive heart disease and bone lesions. Diagnosis was confirmed via endomyocardial and bone biopsy.
Area of Science:
- Cardiology
- Oncology
- Pathology
Background:
- Amyloidosis is a rare condition characterized by the buildup of abnormal proteins (amyloid) in organs.
- Primary amyloidosis can affect the heart (cardiac amyloidosis) or bone, but concurrent presentation is exceptionally uncommon.
Observation:
- A 39-year-old female presented with symptoms indicative of restrictive heart disease.
- She also exhibited a destructive bone lesion, raising suspicion for systemic involvement.
Findings:
- The patient was diagnosed with a rare co-occurrence of primary cardiac amyloidosis and bone amyloidosis.
- Diagnostic confirmation was achieved through endomyocardial biopsy and bone biopsy, revealing amyloid deposition in both tissues.
Implications:
- This case highlights the importance of considering systemic amyloidosis in patients with unexplained cardiac and bone abnormalities.
- Further research into the pathogenesis and treatment of combined cardiac and bone amyloidosis is warranted.
Abstract:
A rare combination of primary cardiac amyloidosis and bone amyloidosis is described in a 39-year-old female. The presenting features were restrictive heart disease and a destructive bone lesion. The diagnosis was confirmed with the help of endomyocardial and bone biopsy.
Related Concept Videos
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
01:29Cardiomyopathy III: Hypertrophic Cardiomyopathy
Hypertrophic cardiomyopathy, or HCM, is an autosomal dominant genetic disorder characterized by asymmetric left ventricular hypertrophy without ventricular dilation. It is more common in men and is typically diagnosed in young, athletic adults.EtiologyHCM is primarily genetic and is caused by mutations in genes encoding sarcomeric proteins. Researchers have identified over 1400 mutations across at least 11 different genes. Among these, the most frequently occurring mutations are found in the...
01:29Cardiomyopathy IV: Restrictive Cardiomyopathy
Restrictive cardiomyopathy (RCM) is a rare heart muscle disease characterized by impaired ventricular filling due to stiffened ventricular walls, leading to significant diastolic dysfunction.EtiologyRestrictive cardiomyopathy can arise from both inherited and acquired diseases, many of which are systemic. It is categorized into four main types: infiltrative, storage, non-infiltrative, and endomyocardial diseases.Infiltrative diseases, such as amyloidosis, lead to RCM by depositing amyloid...
01:23Alzheimer Disease ll: Pathophysiology
Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...
01:25Secondary Spinal Cord Injury llI: Pathophysiology
Early Ischemia and Ionic ImbalanceWithin minutes of spinal cord injury, a secondary cascade begins, progressing over hours to weeks. Vascular damage reduces blood flow, causing ischemia and mitochondrial dysfunction. ATP depletion leads to ion pump failure, membrane depolarization, sodium influx, potassium efflux, and water accumulation, resulting in cellular swelling. Increased intracellular calcium further disrupts mitochondria and accelerates cellular injury.Excitotoxicity and Neuronal...