Related Experiment Video
Updated: Aug 8, 2026
09:41
Performing and Processing FNA of Anterior Fat Pad for Amyloid
Published on: October 30, 2010
[Systemic amyloidosis: clinico-pathologic study of 69 cases]
J I García Morán1, A Barat Cascante, H Oliva Aldámiz
1Departamento de Anatomía Patológica, Fundación Jiménez Díaz, Madrid.
Revista Clinica Espanola
|September 1, 1992
Summary
This study differentiates systemic amyloidosis types using the potassium permanganate technique. The histochemical method aids classification when clinical signs overlap, aiding diagnosis.
Area of Science:
- Nephrology
- Hematology
- Pathology
Context:
- Systemic amyloidosis presents diagnostic challenges due to overlapping clinical features across its subtypes.
- Accurate classification is crucial for appropriate patient management and treatment strategies.
Purpose:
- To evaluate the utility of the potassium permanganate technique in differentiating five types of systemic amyloidosis.
- To correlate histochemical findings with clinical presentation and topographical distribution of amyloid deposits.
Summary:
- A series of 69 systemic amyloidosis cases (primary, myeloma-related, reactive, familial Mediterranean fever, and Portuguese familial polyneuropathy) were analyzed.
- Clinical presentation and deposit topography showed significant overlap; macroglossia was more frequent in primary amyloidosis.
- The potassium permanganate technique demonstrated differential staining: primary and myeloma-related amyloidosis were largely resistant, while reactive and familial Mediterranean fever amyloidosis were sensitive.
Impact:
- The potassium permanganate technique offers a valuable adjunctive tool for classifying systemic amyloidosis, improving diagnostic accuracy.
- This histochemical approach can guide therapeutic decisions by distinguishing between amyloid subtypes with different prognoses and treatment responses.
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...
01:23Alzheimer 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...