Related Experiment Video
Updated: Jun 22, 2026
09:31
Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
Published on: March 7, 2019
Ultrastructural analysis of amyloidoma
Christopher A Garcia1, Patrice C Abell-Aleff, Scott I Gamb
1University of Illinois-Peoria Medical School, Peoria, Illinois, USA.
Ultrastructural Pathology
|May 30, 2009
Summary
Localized amyloidomas, mass-forming amyloid deposits, were examined ultrastructurally. Findings reveal unique fibril structures and tangles, expanding the understanding of paraprotein deposition diseases.
Area of Science:
- Pathology
- Electron Microscopy
- Materials Science
Background:
- Amyloidomas are localized amyloid deposits, potentially linked to systemic amyloidosis.
- Primary systemic AL amyloidosis involves abnormal protein deposition.
Observation:
- Ultrastructural analysis of 3 amyloidomas from 2 autopsy patients with AL amyloidosis was performed.
- Transmission electron microscopy revealed randomly oriented, nonbranching amyloid fibrils.
- Fibrils exhibited unusual curvilinear forms and significant diameter variability (12-14 nm and 28-30 nm).
Findings:
- Larger amyloid fibrils (28-30 nm) displayed characteristics resembling microtubule formation.
- Scanning electron microscopy showed intricate three-dimensional fibril tangles.
- These ultrastructural features contribute to the known spectrum of amyloidomas.
Implications:
- The study enhances the understanding of amyloidoma morphology at the ultrastructural level.
- Findings provide insights into the structural organization of amyloid deposits in paraprotein deposition diseases.
- This detailed morphologic characterization aids in differentiating amyloidomas from other mass-forming lesions.
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...