Ultrastructural analysis of amyloidoma.
Amyloidomas are localized mass-forming deposits of amyloid that occur with or without association with systemic amyloidosis. The ultrastructural findings in 3 amyloidomas from 2 autopsy patients with primary systemic AL amyloidosis are described. By transmission electron microscopy, there were randomly oriented nonbranching fibrils showing some unusual curvilinear forms and considerable variability in fibril diameter (two subsets of fibrils, one 12-14 nm and another 28-30 nm in diameter). The larger fibrils showed features of microtubule formation. Scanning electron microscopy demonstrated complex 3-dimensional tangles of fibrils. These findings add to the current ultrastructural and morphologic spectrum of paraprotein deposition disease.
Garcia
Christopher A
CA
University of Illinois-Peoria Medical School, Peoria, Illinois, USA.
Abell-Aleff
Patrice C
PC
Gamb
Scott I
SI
Miller
Dylan V
DV
D000368:Aged; D000682:Amyloid / Q000378:metabolism / Q000648:ultrastructure*; D000686:Amyloidosis / Q000150:complications / Q000378:metabolism / Q000473:pathology* / Q000601:surgery; D017809:Fatal Outcome; D005260:Female; D006331:Heart Diseases / Q000150:complications / Q000378:metabolism / Q000473:pathology*; D006801:Humans; D007668:Kidney / Q000378:metabolism / Q000473:pathology; D007674:Kidney Diseases / Q000150:complications / Q000378:metabolism / Q000473:pathology*; D008297:Male; D008855:Microscopy, Electron, Scanning; D046529:Microscopy, Electron, Transmission; D008875:Middle Aged; D009206:Myocardium / Q000378:metabolism / Q000473:pathology; D033581:Stem Cell Transplantation
D000682:Amyloid