SUMMARY:We report a novel localized amyloidosis associated with lactoferrin. To elucidate the precursor protein of corneal amyloidosis associated with trichiasis, we analyzed amyloid deposits from three patients by histopathology and biochemistry. Amyloid deposits showed immunoreactivity, confirmed by electron microscopy, for only anti-human lactoferrin antibody. Electrophoresis of amyloid fibrils revealed lactoferrin with and without sugar chains; N-terminal sequence analysis revealed full-length lactoferrin and a truncated tripeptide of N-terminal amino acids, Gly-Arg-Arg. Carboxymethylated wild-type lactoferrin formed amyloid fibrils in vitro. Lactoferrin gene analysis in the three patients revealed a Glu561Asp mutation in all of the patients and a compound heterozygote of Ala11Thr and Glu561Asp mutations in one patient. A heterozygotic Glu561Asp mutation appeared in 44.8% of healthy Japanese volunteers, suggesting that the mutation may not be an essential mutation for amyloid formation (p ϭ 0.104). Results thus suggest that lactoferrin is this precursor protein. (Lab Invest 2002, 82:757-765).

The poor accuracy of SUV(max) in 18F-FDG-PET/CT in distinguishing malignant from benign bone tumors was confirmed; some benign bone tumors showed high FDG uptake. Giant cell tumor of bone was a major false-positive histopathological subtype of bone tumors, showing high FDG accumulation. HK-2 contributed significantly to FDG uptake, whereas GLUT-1 appeared to play no role in FDG uptake in giant cell tumor of bone.

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Therapeutic study, Level III.

The sequentially annealed HXLPE reduced the in vivo polyethylene wear particles by 58% compared with conventional polyethylene without the significant change of particle size and shape.