Sic L. Chan
McGill University
9 Papers
122 Citations
Sic L. Chan is an academic researcher from McGill University. The author has contributed to research in topics: Endosome & Amyloid precursor protein. The author has an hindex of 6, co-authored 9 publications.
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Papers
Fourier transform infrared spectroscopic investigation of temperature- and pressure-induced disaggregation of amyloid A.
TL;DR: The present data indicate that residual amounts of undissociated amyloid in the milieu at physiological and acidic pH may act as nucleating foci rendering dissociatedAmyloid to reaggregate into organized amyloids.
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Selective localization of murine ApoSAA1/SAA2 in endosomes-lysosomes in activated macrophages and their degradation products
TL;DR: The data suggest that following endocytosis of exogenous murine apoSAA/SAA2, the animals undergoing amyloidosis may be processed in the endosomes-lysosomes (EL).
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Colocalization of ubiquitin and serum amyloid A and ubiquitin-bound AA in the endosomes-lysosomes: A double immunogold electron microscopic study
TL;DR: Co-deposition of 6 and 15 nm particles, the latter indicative of AA epitope reactivity, was restricted to dense endosomes-lysosomes (EL), intravesicular “stumpy” and extracellular slender AA fibrils.
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Ubiquitin and Alzheimer's amyloid beta precursor protein colocalize to endosomes-lysosomes in cultured human cells.
TL;DR: It is shown using immunocytochemistry and immunogold electron microscopy that not only AβPP but also ubiquitin co-localize to ELs in CHQ-treated human neuroblastoma (SK-N-SH) and glioblastoma (U-373) and it is hypothesize that Ub may play a role in A βPP processing and/or trafficking toELs, particularly in stress-related conditions.
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Ubiquitin (Ub) interacts non-covalently with Alzheimer amyloid precursor protein (betaPP): isolation of Ub-betaPP conjugates from brain extracts.
TL;DR: It is shown for the first time that Ub interacts avidly but non-covalently with βPP and such complexes, apparently formed in vivo, can be isolated from AD brain extracts by Ub-gel matrix affinity chromatography.
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