51. A case of spheroid‐type localized lactoferrin amyloidosis in the bronchus
- Author
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Nagaaki Katoh, Takeshi Uehara, Satoshi Shiozawa, Tsuneaki Yoshinaga, Fuyuki Kametani, Shojiro Ichimata, Masahide Yazaki, and Daiju Aoyagi
- Subjects
Male ,Proteomics ,0301 basic medicine ,Pathology ,medicine.medical_specialty ,Amyloid ,Biopsy ,Bronchi ,Pathology and Forensic Medicine ,03 medical and health sciences ,0302 clinical medicine ,Seminal vesicle ,Tandem Mass Spectrometry ,Bronchoscopy ,medicine ,Humans ,Bronchus ,medicine.diagnostic_test ,biology ,Lactoferrin ,Chemistry ,Amyloidosis ,Calcinosis ,Bronchial Diseases ,General Medicine ,Middle Aged ,medicine.disease ,Immunohistochemistry ,030104 developmental biology ,medicine.anatomical_structure ,030220 oncology & carcinogenesis ,Right Main Bronchus ,biology.protein ,Tomography, X-Ray Computed ,Chromatography, Liquid ,Calcification - Abstract
We report a case of localized bronchial lactoferrin amyloidosis. A 47-year-old man presented with a complaint of persistent dry cough for two months. Chest computed-tomography revealed a calcification shadow of the right main bronchus; hence, a biopsy was performed, showing layered spheroid-type eosinophilic deposits in the bronchial wall. These deposits were positive for Congo red staining, exhibiting apple-green birefringence under polarized light. In addition, an electron microscopic examination demonstrated that this layered structure was formed by very thin cord-like amyloid deposits. By proteomics analysis using liquid chromatography-tandem mass spectrometry and immunohistochemistry, we confirmed that the deposited amyloid was composed of lactoferrin. While lactoferrin is known to be a precursor protein of localized corneal and seminal vesicle amyloidosis, localized lactoferrin amyloidosis of the bronchus has not been reported in the English literature. Our pathological findings suggested that localized lactoferrin amyloidosis may be caused by long-term tissue damage, and the characteristic spheroid-type appearance is thought to be associated with unique, thin cord-like amyloid deposits.
- Published
- 2019