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Updated: Nov 11, 2025

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
Published on: April 28, 2022
A systemic apolipoprotein A-IV-associated amyloidosis confirmed by proteome analysis
Taro Murakami1, Akira Takasawa2, Asako Moriki1,3
1Department of Pathology, Sapporo Medical University School of Medicine, S1 W17, Chuo-ku, Sapporo, 060-8556, Japan.
Systemic apolipoprotein A-IV amyloidosis, a rare condition, was diagnosed using proteome analysis. This method aids in identifying specific amyloid proteins in tissues, crucial for patient therapy selection.
Area of Science:
- Biochemistry
- Pathology
- Proteomics
Background:
- Amyloidosis results from extracellular protein deposition, with 36 known amyloidogenic proteins in humans.
- Accurate identification of the specific amyloid protein is vital for effective patient therapy.
- Apolipoprotein A-IV is recognized as amyloid-associated, yet apolipoprotein A-IV amyloidosis is infrequently reported.
Observation:
- This study presents a case of systemic apolipoprotein A-IV-associated amyloidosis.
- The diagnosis was confirmed through proteome analysis of formalin-fixed paraffin-embedded tissue.
- Immunohistochemical techniques further supported the identification of apolipoprotein A-IV as the causative protein.
Findings:
- Proteome analysis successfully identified apolipoprotein A-IV in amyloid deposits.
- Formalin-fixed paraffin-embedded tissue was effectively utilized for proteomic and immunohistochemical analysis.
- This case expands the understanding of apolipoprotein A-IV amyloidosis.
Implications:
- The findings highlight the utility of proteome analysis in diagnosing rare amyloidosis subtypes.
- This diagnostic approach can guide therapeutic strategies for patients with specific amyloid protein types.
- Further research into apolipoprotein A-IV amyloidosis is warranted to understand its pathogenesis and clinical course.
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