The pivotal role of scavenger receptor CD36 and phagocyte-derived oxidants in oxidized low density lipoprotein-induced adhesion to endothelial cells

Kopprasch, Steffi; Pietzsch, Jens; Westendorf, T.; Kruse, Hans-Joachim; Gräßler, J

doi:10.1016/j.biocel.2003.08.001

Cited by 31 publications

(13 citation statements)

References 39 publications

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“…This differential activity was ascribed to selective expression of CD36 on microvascular endothelial cells (29). However, others have reported (39,40) and we have confirmed low-level expression of CD36 in HUVECs. Because we see potent inhibition of NO-induced adhesion, proliferation, and cGMP accumulation in HUVECs by both TSRs and a CD36 agonist antibody, CD36 presumably mediates the corresponding responses to TSP1.…”

Section: Discussionsupporting

confidence: 43%

Thrombospondin-1 inhibits endothelial cell responses to nitric oxide in a cGMP-dependent manner

Isenberg

Ridnour

Perruccio

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

245

261

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Redox signaling plays an important role in the positive regulation of angiogenesis by vascular endothelial growth factor, but its role in signal transduction by angiogenesis inhibitors is less clear. Using muscle explants in 3D culture, we found that explants from mice lacking the angiogenesis inhibitor thrombospondin-1 (TSP1) exhibit exaggerated angiogenic responses to an exogenous NO donor, which could be reversed by providing exogenous TSP1. To define the basis for inhibition by TSP1, we examined the effects of TSP1 on several proangiogenic responses of endothelial cells to NO. NO has a biphasic effect on endothelial cell proliferation. The positive effect at low doses of NO is sensitive to inhibition of cGMP signaling and picomolar concentrations of TSP1. NO stimulates both directed (chemotactic) and random (chemokinetic) motility of endothelial cells in a cGMP-dependent manner. TSP1 potently inhibits chemotaxis stimulated by NO. Low doses of NO also stimulate adhesion of endothelial cells on type I collagen in a cGMP-dependent manner. TSP1 potently inhibits this response both upstream and downstream of cGMP. NO-stimulated endothelial cell responses are inhibited by recombinant type 1 repeats of TSP1 and a CD36 agonist antibody but not by the N-terminal portion of TSP1, suggesting that CD36 or a related receptor mediates these effects. These results demonstrate a potent antagonism between TSP1 and proangiogenic signaling downstream of NO. Further elucidation of this inhibitory signaling pathway may identify new molecular targets to regulate pathological angiogenesis.angiogenesis ͉ cell adhesion ͉ chemotaxis ͉ proliferation ͉ CD36 R edox signaling plays a central role in both developmental and pathological angiogenesis (1). Low to moderate concentrations of NO act on endothelial cells to stimulate angiogenesis by activating soluble guanylyl cyclase (sGC), thereby increasing cGMP, which activates cGMP-dependent protein kinases (2) and other cGMP-dependent pathways (3, 4). These responses lead to downstream activation of the Ras-Raf-extracellular-regulated kinase (ERK) (5), vasodilator-stimulated phosphoprotein (6), and phosphatidylinositol 3-kinase-Akt pathways (7). At specific doses, NO donors induce endothelial cell chemotaxis (7,8), permeability (9), and proliferation in vitro (10, 11) and angiogenesis in vivo (12).Consistent with these observations, endogenous NO synthesis in endothelial cells is induced by some angiogenic factors, including vascular endothelial growth factor (VEGF) (13). VEGF receptor signaling activates Akt in a phosphatidylinositol 3-kinase-and PKC-dependent manner, which phosphorylates endothelial NO synthase (eNOS) on Ser-1177 (14, 15). This modification increases eNOS activity and NO synthesis. eNOS activation plays a crucial role in VEGF-induced angiogenesis and vascular permeability (16,17). Conversely, NO induces VEGF transcription by inducing synthesis and stabilization of . These data suggest a positive feedback loop between NO and VEGF signaling. However, inhibitory effects of ...

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Section: Discussionsupporting

confidence: 43%

Thrombospondin-1 inhibits endothelial cell responses to nitric oxide in a cGMP-dependent manner

Isenberg

Ridnour

Perruccio

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

245

261

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“…This is attributed primar- 84 ily to interaction with the class B scavenger receptors CD36 and 85 SR-B1 [14]. HOCl-LDL may also promote the development of ather-86 osclerosis by stimulating macrophage adhesion to endothelial cells 87 [15] and the induction of macrophage apoptosis (e.g. [16]), a factor 88 known to destabilise atherosclerotic lesions [17].…”

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confidence: 98%

Comparative reactivity of the myeloperoxidase-derived oxidants HOCl and HOSCN with low-density lipoprotein (LDL): Implications for foam cell formation in atherosclerosis

Ismael

Proudfoot

Brown

et al. 2015

Archives of Biochemistry and Biophysics

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Atherosclerosis is characterised by the accumulation of lipids within macrophages in the artery wall. Low-density lipoprotein (LDL) is the source of this lipid, owing to the uptake of oxidised LDL by scavenger receptors. Myeloperoxidase (MPO) released by leukocytes during inflammation produces oxidants that are implicated in atherosclerosis. Modification of LDL by the MPO oxidant hypochlorous acid (HOCl), results in extensive lipid accumulation by macrophages. However, the reactivity of the other major MPO oxidant, hypothiocyanous acid (HOSCN) with LDL is poorly characterised, which is significant given that thiocyanate is the favoured substrate for MPO. In this study, we comprehensively compare the reactivity of HOCl and HOSCN with LDL, and show key differences in the profile of oxidative damage observed. HOSCN selectively modifies Cys residues on apolipoprotein B100, and oxidises cholesteryl esters resulting in formation of lipid hydroperoxides, 9-hydroxy-10,12-octadecadienoic acid (9-HODE) and F2-isoprostanes. The modification of LDL by HOSCN results macrophage lipid accumulation, though generally to a lesser extent than HOCl-modified LDL. This suggests that a change in the ratio of HOSCN:HOCl formation by MPO from variations in plasma thiocyanate levels, will influence the nature of LDL oxidation in vivo, and has implications for the progression of atherosclerosis.

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“…It has to be considered that RAGE and certain scavenger receptors share a common ligand recognition principle based on electrostatic interactions between the positively charged receptor surface domains and negatively charged ligands (Adachi and Tsujimoto 2006; Jimenez-Dalmaroni et al 2009; Gao et al 2010; Fritz 2011). In this regard, there is an experimental evidence that well-characterized RAGE-ligands, such as advanced glycation endproducts, hypochlorite-modified proteins/apolipoproteins, and amyloid-β, also bind to CD36 (Ohgami et al 2001; Kopprasch et al 2004; Marsche et al 2007; Jones et al 2013). Another important property RAGE and CD36 have in common is the activation of signaling cascades (Goyette et al 2009; Park 2014).…”

Section: Introductionmentioning

confidence: 99%

Insights into binding of S100 proteins to scavenger receptors: class B scavenger receptor CD36 binds S100A12 with high affinity

2016

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The EF-hand type calcium-binding protein S100A12 exerts numerous intra- and extracellular functions of (patho)physiological relevance. Therefore, receptors of S100A12 are of high interest for research and clinical applications. Beside the extensively studied receptor for advanced glycation endproducts (RAGE), G-protein coupled receptors and more recently, scavenger receptors are suggested to be putative S100A12 receptors. Own findings and further information from the literature predestined CD36, a class B scavenger receptor, as promising candidate. To substantiate or prove against this hypothesis, this study aimed at investigation of interaction of S100A12 and CD36 on molecular and cellular level by the use of surface plasmon resonance (SPR), radio- and fluorescence-tracer-based cell binding, and cell activation experiments. S100A12 revealed binding affinity to CD36 in the low nanomolar range, essentially, at the CD36 thrombospondin-1 binding site. Additionally, S100A12-mediated translocation of CD36 to the membrane and elevation of both CD36 and peroxisome proliferator-activated receptor γ (PPARγ) expression was observed, which suggest a potential regulatory function of S100A12–CD36 interaction.Electronic supplementary materialThe online version of this article (doi:10.1007/s00726-016-2349-2) contains supplementary material, which is available to authorized users.

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The pivotal role of scavenger receptor CD36 and phagocyte-derived oxidants in oxidized low density lipoprotein-induced adhesion to endothelial cells

Cited by 31 publications

References 39 publications

Thrombospondin-1 inhibits endothelial cell responses to nitric oxide in a cGMP-dependent manner

Thrombospondin-1 inhibits endothelial cell responses to nitric oxide in a cGMP-dependent manner

Comparative reactivity of the myeloperoxidase-derived oxidants HOCl and HOSCN with low-density lipoprotein (LDL): Implications for foam cell formation in atherosclerosis

Insights into binding of S100 proteins to scavenger receptors: class B scavenger receptor CD36 binds S100A12 with high affinity

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