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Bone marrow amyloid spherulites in a case of AL amyloidosis
Karthik Bommannan B K1, Mukinkumar Sonai1, Man Updesh Singh Sachdeva1
1Department of Hematology, Postgraduate Institute of Medical Education and Research, Chandigarh, India.
Abstract:
Parallel arrangement of β-pleated sheets by amyloidogenic proteins is a well known phenomenon. Rarely, amyloid fibrils undergo radial orientation to form globular structures called spherulites. These amyloid spherulites show Maltese cross pattern under polarized microscopy. The clinical significance of amyloid spherulites is undetermined. Amyloidogenic proteins like insulin and β-lactoglobulin form spherulites in vitro. The senile plaques of Alzheimer's disease rarely form in vivo spherulites. Amyloid spherulites have been described in the liver and small intestine. For the first time, we document amyloid spherulite formation in the bone marrow biopsy of an AL amyloidosis patient.
Insights
Amyloid spherulites, rare globular amyloid structures, were observed in a bone marrow biopsy from a patient with AL amyloidosis. This finding expands the known locations for in vivo amyloid spherulite formation.
Area of Science:
- Biochemistry
- Pathology
- Microscopy
Background:
- Amyloidogenic proteins typically form parallel β-pleated sheets.
- Amyloid fibrils can rarely form radially oriented globular structures known as spherulites.
- Amyloid spherulites exhibit a characteristic Maltese cross pattern under polarized light microscopy.
Observation:
- Amyloid spherulites have been previously identified in vitro and in specific organs like the liver and small intestine.
- In vivo formation of amyloid spherulites is uncommon, with senile plaques in Alzheimer's disease rarely exhibiting this morphology.
- This study documents, for the first time, the presence of amyloid spherulites in a bone marrow biopsy.
Findings:
- The bone marrow biopsy sample from an AL amyloidosis patient revealed the presence of amyloid spherulites.
- This observation confirms the in vivo formation of amyloid spherulites in a new anatomical site.
- The specific amyloidogenic protein responsible for spherulite formation in this AL amyloidosis case requires further investigation.
Implications:
- The clinical significance of amyloid spherulites remains largely undetermined.
- Documenting amyloid spherulites in bone marrow may offer new insights into AL amyloidosis pathogenesis.
- Further research is needed to understand the formation, clinical relevance, and diagnostic value of amyloid spherulites in various amyloidosis types.
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