Biochemical isolation of a membrane microdomain from resting platelets highly enriched in the plasma membrane glycoprotein CD36

Dorahy, Douglas J.; Lincz, Lisa F.; Meldrum, Cliff; Burns, Gordon F.

doi:10.1042/bj3190067

Cited by 124 publications

(118 citation statements)

References 33 publications

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“…In some cell types, expression of caveolin-1 has been shown to be necessary for plasma membrane targeting of CD36, and disruption of caveolae may effect some CD36 dependent functions (Ring, Le Lay, Pohl, Verkade, & Stremmel 2006,Vistisen, Roepstorff, Roepstorff, Bonen, van Deurs, & Kiens, 2004,Frank, Lee, Park, Tandon, Scherer, & Lisanti,. 2004,Pohl, Ring, Korkmaz, Ehehalt, & Stremmel, 2005,Kincer, et al, 2002, Dorahy, Lincz, Meldrum, & Burns, 1996. The partitioning of CD36 to specific plasma membrane domains may facilitate interaction with signaling partners that are essential to CD36 dependent responses.…”

Section: Cd36 Structure and Expressionmentioning

confidence: 99%

CD36: Implications in cardiovascular disease

Febbraio

Silverstein

2007

The International Journal of Biochemistry & Cell Biology

215

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CD36 is a broadly expressed membrane glycoprotein that acts as a facilitator of fatty acid uptake, a signaling molecule, and a receptor for a wide range of ligands, including apoptotic cells, modified forms of low density lipoprotein, thrombospondins, fibrillar beta-amyloid, components of gram positive bacterial walls and malaria infected erythrocytes. CD36 expression on macrophages, dendritic and endothelial cells, and in tissues including muscle, heart, and fat, suggest diverse roles, and indeed, this is truly a multifunctional receptor involved in both homeostatic and pathologic conditions. Despite an impressive increase in our knowledge of CD36 functions, in depth understanding of the mechanistic aspects of this protein remains elusive. This review focuses on CD36 in cardiovascular disease-what we know, and what we have yet to learn.

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Section: Cd36 Structure and Expressionmentioning

confidence: 99%

CD36: Implications in cardiovascular disease

Febbraio

Silverstein

2007

The International Journal of Biochemistry & Cell Biology

215

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“…In addition, another class B scavenger receptor, CD36, has also been localized to caveolae (39,40). Both SR-BI (19) and CD36 (41) 3 H]CE in the reversible pool (q) was quantified by incubating cells in the presence of unlabeled HDL (100 g/ml) for 120 min and counting radiolabeled CE in the medium.…”

Section: Discussionmentioning

confidence: 99%

The Class B, Type I Scavenger Receptor Promotes the Selective Uptake of High Density Lipoprotein Cholesterol Ethers into Caveolae

Graf¹,

Connell²,

Westhuyzen³

et al. 1999

Journal of Biological Chemistry

163

105

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The uptake of cholesterol esters from high density lipoproteins (HDLs) is characterized by the initial movement of cholesterol esters into a reversible plasma membrane pool. Cholesterol esters are subsequently internalized to a nonreversible pool. Unlike the uptake of cholesterol from low density lipoproteins, cholesterol ester uptake from HDL does not involve the internalization and degradation of the particle and is therefore termed selective. The class B, type I scavenger receptor (SR-BI) has been identified as an HDL receptor and shown to mediate selective cholesterol ester uptake. SR-BI is localized to cholesterol-and sphingomyelinrich microdomains called caveolae. Caveolae are directly involved in cholesterol trafficking. Therefore, we tested the hypothesis that caveolae are acceptors for HDL-derived cholesterol ether (CE). Our studies demonstrate that in Chinese hamster ovary cells expressing SR-BI, >80% of the plasma membrane associated CE is present in caveolae after 7.5 min of selective cholesterol ether uptake. We also show that excess, unlabeled HDL can extract the radiolabeled CE from caveolae, demonstrating that caveolae constitute a reversible plasma membrane pool of CE. Furthermore, 50% of the caveolaeassociated CE can be chased into a nonreversible pool. We conclude that caveolae are acceptors for HDL-derived cholesterol ethers, and that caveolae constitute a reversible, plasma membrane pool of cholesterol ethers.Plasma levels of high density lipoprotein (HDL) 1 cholesterol are negatively correlated with the risk of developing atherosclerosis, the leading cause of death in western, industrialized countries (1, 2). The role of HDL in cholesterol metabolism includes the delivery of cholesterol esters to steroidogenic tissues (3, 4) and the transfer of cholesterol from peripheral tissues to the liver in a process termed reverse cholesterol transport (5, 6). Reverse cholesterol transport requires the extraction of cholesterol from extrahepatic cells by HDL and the subsequent delivery of cholesterol esters to hepatocytes.The mechanism for the delivery of cholesterol esters from HDL to cells is described as selective uptake, because the uptake of cholesterol ester is independent of HDL internalization (7,8). Selective uptake of cholesterol ester from HDL is characterized by the initial movement of cholesterol ester into a reversible, plasma membrane pool and the subsequent internalization to a nonreversible, intracellular pool (9, 10).The mechanisms of cholesterol and cholesterol ester exchange between the cell surface and HDL are not well understood. Receptor-independent and receptor-dependent hypotheses have been proposed to explain the transfer of cholesterol and cholesterol ester between the cell surface and HDL (6). In the receptor-independent model, diffusion is thought to account for both the uptake of cholesterol esters and the efflux of free cholesterol. In contrast, HDL-binding proteins, such as class B, type I scavenger receptor (SR-BI) and class B, type II scavenger receptor, can mediate t...

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“…These cholesterol-and sphingolipid-enriched structures may serve to concentrate signaling molecules and facilitate the integration of signaling cascades. For example, in platelets, in addition to CD36, src, and the src-related kinase lyn, also colocalize in these domains (12). Multiple lines of evidence indicate that caveolae serve an integral role in the trafficking of cholesterol in cells.…”

Section: Distribution and Function Of Cd36mentioning

confidence: 99%