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Bernardo L. Trigatti

Researcher at McMaster University

Publications -  95
Citations -  6459

Bernardo L. Trigatti is an academic researcher from McMaster University. The author has contributed to research in topics: Cholesterol & Scavenger receptor. The author has an hindex of 33, co-authored 93 publications receiving 6044 citations. Previous affiliations of Bernardo L. Trigatti include Hamilton Health Sciences & Massachusetts Institute of Technology.

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A targeted mutation in the murine gene encoding the high density lipoprotein (HDL) receptor scavenger receptor class B type I reveals its key role in HDL metabolism.

TL;DR: Results provide strong support for the proposal that in mice the gene encoding SR-BI plays a key role in determining the levels of plasma lipoprotein cholesterol (primarily HDL) and the accumulation of cholesterol stores in the adrenal gland.
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Influence of the high density lipoprotein receptor SR-BI on reproductive and cardiovascular pathophysiology

TL;DR: It is shown that SR-BI is required for maintaining normal biliary cholesterol levels, oocyte development, and female fertility, and thatSR-BI can protect against early-onset atherosclerosis.
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Loss of SR-BI expression leads to the early onset of occlusive atherosclerotic coronary artery disease, spontaneous myocardial infarctions, severe cardiac dysfunction, and premature death in apolipoprotein E-deficient mice.

TL;DR: SR-BI/apoE dKO mice provide a new murine model for CHD and may help better define the role of lipoprotein metabolism and atherosclerosis in the pathogenesis of myocardial infarction and cardiac dysfunction.
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Murine SR-BI, a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolae.

TL;DR: The structure and subcellular localization of murine SR-BI (mSR-BI) expressed either in transfected Chinese hamster ovary cells or in murine adrenocortical Y1-BS1 cells are studied, raising the possibility that the unique properties of these specialized cell surface domains may play a critical role in SR- BI-mediated transfer of lipids between lipoproteins and cells.