NIH VideoCast - Proteoglycans: Arbiters of Lipoprotein Metabolism

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Proteoglycans: Arbiters of Lipoprotein Metabolism

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Air date:	Wednesday, September 11, 2013, 3:00:00 PM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 260 (55 Live, 205 On-demand)
Category:	WALS - Wednesday Afternoon Lectures
Runtime:	01:05:35
Closed captioning:	Check box to display CC outside of the video Note: You can drag the captioning window around and resize it
Description:	Wednesday Afternoon Lecture Series Recently, genetic experiments in mice identified the heparan sulfate proteoglycan syndecan-1 as an important receptor for triglyceride-rich lipoprotein (TRL) clearance in the liver. This receptor consists of a protein core and one or more heparan sulfate chains, which make up the binding site for the TRLs. Binding depends on the heparan sulfate chains based on the accumulation of plasma TRLs in mice bearing mutations in heparan sulfate biosynthesis. To identify the major apolipoproteins that mediate binding to the heparan sulfate chains, we developed a series of in vitro and in vivo assays, which led to the identification of apolipoprotein E and apolipoprotein A5 as the relevant ligands on TRLs. Clearance of TRLs through syndecan-1 is atheroprotective based on the increase in atherosclerosis in knock-out mice fed a high-fat diet. Proteoglycans in macrophages also play an atheroprotective role, but not through a clearance mechanism. Instead, one or more proteoglycans on the macrophage keep the cells in a tonic state in response to interferon beta stimulation. For more information go to http://wals.od.nih.gov

NLM Title:	Proteoglycans : arbiters of lipoprotein metabolism / Jeffrey Esko.
Author:	Esko, Jeffrey David. National Institutes of Health (U.S.),
Publisher:
Abstract:	(CIT): Recently, genetic experiments in mice identified the heparan sulfate proteoglycan syndecan-1 as an important receptor for triglyceride-rich lipoprotein (TRL) clearance in the liver. This receptor consists of a protein core and one or more heparan sulfate chains, which make up the binding site for the TRLs. Binding depends on the heparan sulfate chains based on the accumulation of plasma TRLs in mice bearing mutations in heparan sulfate biosynthesis. To identify the major apolipoproteins that mediate binding to the heparan sulfate chains, we developed a series of in vitro and in vivo assays, which led to the identification of apolipoprotein E and apolipoprotein A5 as the relevant ligands on TRLs. Clearance of TRLs through syndecan-1 is atheroprotective based on the increase in atherosclerosis in knock-out mice fed a high-fat diet. Proteoglycans in macrophages also play an atheroprotective role, but not through a clearance mechanism. Instead, one or more proteoglycans on the macrophage keep the cells in a tonic state in response to interferon beta stimulation.
Subjects:	Hypertriglyceridemia--metabolism Lipoproteins--metabolism Proteoglycans--metabolism Syndecan-1--metabolism
Publication Types:	Lecture Webcast

NLM Classification:	QU 55.5
NLM ID:	101618065
CIT Live ID:	13155
Permanent link:	https://videocast.nih.gov/watch=13155

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