Systemic Amyloidosis: A Clinical Challenge from the Palliative Care Perspective.
John Lidemberto Cárdenas Cárdenas1, Verónica Elena Páez Avendaño2, Fabián Andrés Charry Monsalve3
1Internal Medicine and Specialist in Pain Medicine and Palliative Care, Pablo Tobón Uribe Hospital, Medellín, Colombia.
Journal of Pain & Palliative Care Pharmacotherapy
|July 6, 2026
Summary
Palliative care is crucial for managing amyloidosis, a rare disease causing organ dysfunction. An interdisciplinary approach improves symptom control and quality of life for patients with amyloidosis.
Area of Science:
- Palliative Care
- Amyloidosis
- Internal Medicine
Background:
- Amyloidosis involves extracellular deposition of misfolded proteins, leading to progressive organ dysfunction.
- Management is complex, with high symptom burden and uncertain prognosis.
- Palliative care is essential for comprehensive management and improving patient quality of life.
Purpose of the Study:
- To review evidence on palliative interventions for amyloidosis patients.
- Focus on symptom control, psychosocial support, and shared decision-making.
- Examine the role of palliative care in improving quality of life.
Main Methods:
- Narrative review of existing literature.
- Examination of palliative interventions for symptom management.
- Analysis of psychosocial support and shared decision-making strategies.
Main Results:
- A patient-centered, interdisciplinary approach effectively manages pain, dyspnea, fatigue, and other symptoms.
- Palliative care enhances emotional well-being and facilitates advance care planning.
- Early integration of palliative care teams is vital for optimal support.
Conclusions:
- Palliative care significantly improves quality of life for amyloidosis patients.
- Early and integrated palliative care optimizes symptom management and family support.
- Further research is needed to address gaps in specific interventions and long-term impact.
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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.
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Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
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