Year: 2016
Type: dissertation
Abstract: Apolipoprotein B-100 (apoB100) is the main structural protein of atherogenic lipoproteins and is a key risk factor for development of coronary heart disease. The molecular mechanisms that regulate apoB100 degradation or secretion are not clearly understood but evidence supports intracellular lipid supply as a major decisive factor. Ancient Ubiquitous Protein 1 (AUP1) has been found to be present on the surface of Lipid Droplets (LDs), and has been implicated in ER-Associated Degradation. AUP1 knockdown dramatically increased levels of cellular apoB100 and facilitated secretion of apoB100 containing VLDL-sized particles from HepG2 cells. Knocking down AUP1 also increased Triglyceride (TG) levels in apoB100 containing VLDL particles. AUP1 was found to interact with apoB100 intracellularly based on co-immunoprecipitation experiments as well as in situ proximity ligation assay. Finally, modulating AUP-1 altered LD size in HepG2 cells and its knockdown increased the average size of LDs.
Source: TSpace (University of Toronto)
Author: Mostafa Zamani
Language: English
Subfield: Cardiology and Cardiovascular Medicine
Field: Medicine
Domain: Health Sciences
Open Access status: green
OpenAlex ID: W2946194317