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Warren L Lee - One of the best experts on this subject based on the ideXlab platform.
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endothelial hmgb1 is a critical regulator of ldl Transcytosis via an srebp2 sr bi axis
Arteriosclerosis Thrombosis and Vascular Biology, 2021Co-Authors: Siavash Ghaffari, Changsen Wang, Erika Jang, Farnoosh Naderinabi, Rajiv Sanwal, Negar Khosraviani, Benjamin E Steinberg, Neil M Goldenberg, Jiro Ikeda, Warren L LeeAbstract:Objective: LDL (low-density lipoprotein) Transcytosis across the endothelium is performed by the SR-BI (scavenger receptor class B type 1) receptor and contributes to atherosclerosis. HMGB1 (high m...
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bmp 9 and ldl crosstalk regulates alk 1 endocytosis and ldl Transcytosis in endothelial cells
Journal of Biological Chemistry, 2020Co-Authors: Bo Tao, Siavash Ghaffari, Warren L Lee, Jan R Kraehling, Christina M Ramirez, Sungwoon Lee, Joseph W Fowler, Carlos Fernandezhernando, Anne Eichmann, William C SessaAbstract:Bone morphogenetic protein-9 (BMP-9) is a circulating cytokine that is known to play an essential role in the endothelial homeostasis and the binding of BMP-9 to the receptor activin-like kinase 1 (ALK-1) promotes endothelial cell quiescence. Previously, using an unbiased screen, we identified ALK-1 as a high-capacity receptor for low-density lipoprotein (LDL) in endothelial cells that mediates its Transcytosis in a nondegradative manner. Here we examine the crosstalk between BMP-9 and LDL and how it influences their interactions with ALK-1. Treatment of endothelial cells with BMP-9 triggers the extensive endocytosis of ALK-1, and it is mediated by caveolin-1 (CAV-1) and dynamin-2 (DNM2) but not clathrin heavy chain. Knockdown of CAV-1 reduces BMP-9-mediated internalization of ALK-1, BMP-9-dependent signaling and gene expression. Similarly, treatment of endothelial cells with LDL reduces BMP-9-induced SMAD1/5 phosphorylation and gene expression and silencing of CAV-1 and DNM2 diminishes LDL-mediated ALK-1 internalization. Interestingly, BMP-9-mediated ALK-1 internalization strongly re-duces LDL Transcytosis to levels seen with ALK-1 deficiency. Thus, BMP-9 levels can control cell surface levels of ALK-1, via CAV-1, to regulate both BMP-9 signaling and LDL Transcytosis.
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estrogen inhibits ldl low density lipoprotein Transcytosis by human coronary artery endothelial cells via gper g protein coupled estrogen receptor and sr bi scavenger receptor class b type 1
Arteriosclerosis Thrombosis and Vascular Biology, 2018Co-Authors: Siavash Ghaffari, Farnoosh Naderi Nabi, Michael G Sugiyama, Warren L LeeAbstract:Objective- The atheroprotective effects of estrogen are independent of circulating lipid levels. Whether estrogen regulates Transcytosis of LDL (low-density lipoprotein) across the coronary endothelium is unknown. Approach and Results- Using total internal reflection fluorescence microscopy, we quantified Transcytosis of LDL across human coronary artery endothelial cells from multiple donors. LDL Transcytosis was significantly higher in cells from men compared with premenopausal women. Estrogen significantly attenuated LDL Transcytosis by endothelial cells from male but not female donors; Transcytosis of albumin was not affected. Estrogen caused downregulation of endothelial SR-BI (scavenger receptor class B type 1), and overexpression of SR-BI was sufficient to restore LDL Transcytosis. Similarly, depletion of SR-BI by siRNA attenuated endothelial LDL Transcytosis and prevented any further effect of estrogen. In contrast, treatment with estrogen had no effect on SR-BI expression by liver cells. Inhibition of estrogen receptors α and β had no effect on estrogen-mediated attenuation of LDL Transcytosis. However, estrogen's effect on LDL Transcytosis was blocked by depletion of the GPER (G-protein-coupled estrogen receptor). GPER was found to be enriched in endothelial cells compared with hepatocytes and is reported to signal via transactivation of the EGFR (epidermal growth factor receptor); inhibition of EGFR prevented the effect of estrogen on LDL Transcytosis and SR-BI mRNA. Last, SR-BI expression was significantly higher in human coronary artery endothelial cells from male compared with premenopausal female donors. Conclusions- Estrogen significantly inhibits LDL Transcytosis by downregulating endothelial SR-BI; this effect requires GPER.
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estrogen inhibits ldl low density lipoprotein Transcytosis by human coronary artery endothelial cells via gper g protein coupled estrogen receptor and sr bi scavenger receptor class b type 1
Arteriosclerosis Thrombosis and Vascular Biology, 2018Co-Authors: Siavash Ghaffari, Farnoosh Naderi Nabi, Michael G Sugiyama, Warren L LeeAbstract:Objective— The atheroprotective effects of estrogen are independent of circulating lipid levels. Whether estrogen regulates Transcytosis of LDL (low-density lipoprotein) across the coronary endothe...
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sr bi mediated Transcytosis of hdl in brain microvascular endothelial cells is independent of caveolin clathrin and pdzk1
Frontiers in Physiology, 2017Co-Authors: Karen Y Fung, Steffen Nyegaard, Warren L Lee, Changsen Wang, Bryan Heit, Gregory D FairnAbstract:The vascular endothelium supplying the brain exhibits very low paracellular and transcellular permeability and is a major constituent of the blood-brain barrier. High-density lipoprotein (HDL) crosses the blood-brain barrier by Transcytosis, but technical limitations have made it difficult to elucidate its regulation. Using a combination of spinning-disc confocal and total internal reflection fluorescence microscopy, we examined the uptake and Transcytosis of HDL by human primary brain microvascular endothelial cell monolayers. Using these approaches, we report that HDL internalization requires dynamin but not clathrin heavy chain and that its internalization and Transcytosis are saturable. Internalized HDL partially co-localized with the scavenger receptor BI (SR-BI) and knockdown of SR-BI significantly attenuated HDL internalization. However, we observed that the adaptor protein PDZK1-which is critical to HDL-SR-BI signaling in other tissues-is not required for HDL uptake in these cells. Additionally, while these cells express caveolin, the abundance of caveolae in this tissue is negligible and we find that SR-BI and caveolin do not co-fractionate. Furthermore, direct silencing of caveolin-1 had no impact on the uptake of HDL. Finally, inhibition of endothelial nitric oxide synthase increased HDL internalization while increasing nitric oxide levels had no impact. Together, these data indicate that SR-BI-mediated Transcytosis in brain microvascular endothelial cells is distinct from uptake and signaling pathways described for this receptor in other cell types.
Siavash Ghaffari - One of the best experts on this subject based on the ideXlab platform.
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endothelial hmgb1 is a critical regulator of ldl Transcytosis via an srebp2 sr bi axis
Arteriosclerosis Thrombosis and Vascular Biology, 2021Co-Authors: Siavash Ghaffari, Changsen Wang, Erika Jang, Farnoosh Naderinabi, Rajiv Sanwal, Negar Khosraviani, Benjamin E Steinberg, Neil M Goldenberg, Jiro Ikeda, Warren L LeeAbstract:Objective: LDL (low-density lipoprotein) Transcytosis across the endothelium is performed by the SR-BI (scavenger receptor class B type 1) receptor and contributes to atherosclerosis. HMGB1 (high m...
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bmp 9 and ldl crosstalk regulates alk 1 endocytosis and ldl Transcytosis in endothelial cells
Journal of Biological Chemistry, 2020Co-Authors: Bo Tao, Siavash Ghaffari, Warren L Lee, Jan R Kraehling, Christina M Ramirez, Sungwoon Lee, Joseph W Fowler, Carlos Fernandezhernando, Anne Eichmann, William C SessaAbstract:Bone morphogenetic protein-9 (BMP-9) is a circulating cytokine that is known to play an essential role in the endothelial homeostasis and the binding of BMP-9 to the receptor activin-like kinase 1 (ALK-1) promotes endothelial cell quiescence. Previously, using an unbiased screen, we identified ALK-1 as a high-capacity receptor for low-density lipoprotein (LDL) in endothelial cells that mediates its Transcytosis in a nondegradative manner. Here we examine the crosstalk between BMP-9 and LDL and how it influences their interactions with ALK-1. Treatment of endothelial cells with BMP-9 triggers the extensive endocytosis of ALK-1, and it is mediated by caveolin-1 (CAV-1) and dynamin-2 (DNM2) but not clathrin heavy chain. Knockdown of CAV-1 reduces BMP-9-mediated internalization of ALK-1, BMP-9-dependent signaling and gene expression. Similarly, treatment of endothelial cells with LDL reduces BMP-9-induced SMAD1/5 phosphorylation and gene expression and silencing of CAV-1 and DNM2 diminishes LDL-mediated ALK-1 internalization. Interestingly, BMP-9-mediated ALK-1 internalization strongly re-duces LDL Transcytosis to levels seen with ALK-1 deficiency. Thus, BMP-9 levels can control cell surface levels of ALK-1, via CAV-1, to regulate both BMP-9 signaling and LDL Transcytosis.
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estrogen inhibits ldl low density lipoprotein Transcytosis by human coronary artery endothelial cells via gper g protein coupled estrogen receptor and sr bi scavenger receptor class b type 1
Arteriosclerosis Thrombosis and Vascular Biology, 2018Co-Authors: Siavash Ghaffari, Farnoosh Naderi Nabi, Michael G Sugiyama, Warren L LeeAbstract:Objective- The atheroprotective effects of estrogen are independent of circulating lipid levels. Whether estrogen regulates Transcytosis of LDL (low-density lipoprotein) across the coronary endothelium is unknown. Approach and Results- Using total internal reflection fluorescence microscopy, we quantified Transcytosis of LDL across human coronary artery endothelial cells from multiple donors. LDL Transcytosis was significantly higher in cells from men compared with premenopausal women. Estrogen significantly attenuated LDL Transcytosis by endothelial cells from male but not female donors; Transcytosis of albumin was not affected. Estrogen caused downregulation of endothelial SR-BI (scavenger receptor class B type 1), and overexpression of SR-BI was sufficient to restore LDL Transcytosis. Similarly, depletion of SR-BI by siRNA attenuated endothelial LDL Transcytosis and prevented any further effect of estrogen. In contrast, treatment with estrogen had no effect on SR-BI expression by liver cells. Inhibition of estrogen receptors α and β had no effect on estrogen-mediated attenuation of LDL Transcytosis. However, estrogen's effect on LDL Transcytosis was blocked by depletion of the GPER (G-protein-coupled estrogen receptor). GPER was found to be enriched in endothelial cells compared with hepatocytes and is reported to signal via transactivation of the EGFR (epidermal growth factor receptor); inhibition of EGFR prevented the effect of estrogen on LDL Transcytosis and SR-BI mRNA. Last, SR-BI expression was significantly higher in human coronary artery endothelial cells from male compared with premenopausal female donors. Conclusions- Estrogen significantly inhibits LDL Transcytosis by downregulating endothelial SR-BI; this effect requires GPER.
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estrogen inhibits ldl low density lipoprotein Transcytosis by human coronary artery endothelial cells via gper g protein coupled estrogen receptor and sr bi scavenger receptor class b type 1
Arteriosclerosis Thrombosis and Vascular Biology, 2018Co-Authors: Siavash Ghaffari, Farnoosh Naderi Nabi, Michael G Sugiyama, Warren L LeeAbstract:Objective— The atheroprotective effects of estrogen are independent of circulating lipid levels. Whether estrogen regulates Transcytosis of LDL (low-density lipoprotein) across the coronary endothe...
Keith E. Mostov - One of the best experts on this subject based on the ideXlab platform.
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The mammalian retromer regulates Transcytosis of the polymeric immunoglobulin receptor
Nature cell biology, 2004Co-Authors: Marcel Verges, Carol Renfrew Haft, Frédéric Luton, Carmen Gruber, Frank Tiemann, Lorri G. Reinders, Lan Huang, Alma L. Burlingame, Keith E. MostovAbstract:Epithelial cells have separate apical and basolateral plasma membrane domains with distinct compositions. After delivery to one surface, proteins can be endocytosed and then recycled, degraded or transcytosed to the opposite surface. Proper sorting into the transcytotic pathway is essential for maintaining polarity, as most proteins are endocytosed many times during their lifespan. The polymeric immunoglobulin receptor (pIgR) transcytoses polymeric IgA (pIgA) from the basolateral to the apical surface of epithelial cells and hepatocytes. However, the molecular machinery that controls polarized sorting of pIgR-pIgA and other receptors is only partially understood. The retromer is a multimeric protein complex, originally described in yeast, which mediates intracellular sorting of Vps10p, a receptor that transports vacuolar enzymes. The yeast retromer contains two sub-complexes. One includes the Vps5p and Vps17p subunits, which provide mechanical force for vesicle budding. The other is the Vps35p-Vps29p-Vps26p subcomplex, which provides cargo specificity. The mammalian retromer binds to the mannose 6-phosphate receptor, which sorts lysosomal enzymes from the trans-Golgi network to the lysosomal pathway. Here, we show a function for the mammalian Vps35-Vps29-Vps26 retromer subcomplex in promoting pIgR-pIgA Transcytosis.
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Direct Interaction between Rab3b and the Polymeric Immunoglobulin Receptor Controls Ligand-Stimulated Transcytosis in Epithelial Cells
Developmental cell, 2002Co-Authors: Sven C.d. Van Ijzendoorn, Michael J. Tuvim, Thomas Weimbs, Burton F. Dickey, Keith E. MostovAbstract:We have examined the role of rab3b in epithelial cells. In MDCK cells, rab3b localizes to vesicular structures containing the polymeric immunoglobulin receptor (pIgR) and located subjacent to the apical surface. We found that GTP-bound rab3b directly interacts with the cytoplasmic domain of pIgR. Binding of dIgA to pIgR causes a dissociation of the interaction with rab3b, a process that requires dIgA-mediated signaling, Arg657 in the cytoplasmic domain of pIgR, and possibly GTP hydrolysis by rab3b. Binding of dIgA to pIgR at the basolateral surface stimulates subsequent Transcytosis to the apical surface. Overexpression of GTP-locked rab3b inhibits dIgA-stimulated Transcytosis. Together, our data demonstrate that a rab protein can bind directly to a specific cargo protein and thereby control its trafficking.
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the src family protein tyrosine kinase p62 yes controls polymeric iga Transcytosis in vivo
Molecular Cell, 1999Co-Authors: Frédéric Luton, Jean-pierre Vaerman, Marcel Verges, Marius Sudol, Keith E. MostovAbstract:Transcytosis of polymeric immunoglobulin A (pIgA) across epithelial cells is mediated by the polymeric immunoglobulin receptor (pIgR). Binding of pIgA to pIgR stimulates Transcytosis of the pIgA-pIgR complex via a signal transduction pathway that is dependent on a protein tyrosine kinase (PTK) of the SRC family. Here we identify the PTK as p62(yes). We demonstrate the specific physical and functional association of the pIgR with p62(yes) in rodent liver. Analysis of p62(yes) knockout mice revealed a dramatic reduction in the association of tyrosine kinase activity with the pIgR and in Transcytosis of pIgA. We conclude that p62(yes) controls pIgA Transcytosis in vivo.
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dimerization of the polymeric immunoglobulin receptor controls its transcytotic trafficking
Molecular Biology of the Cell, 1998Co-Authors: Karen L Singer, Keith E. MostovAbstract:Binding of dimeric immunoglobulin (Ig)A to the polymeric Ig receptor (pIgR) stimulates Transcytosis of pIgR across epithelial cells. Through the generation of a series of pIgR chimeric constructs, we have tested the ability of ligand to promote receptor dimerization and the subsequent role of receptor dimerization on its intracellular trafficking. Using the cytoplasmic domain of the T cell receptor-ζ chain as a sensitive indicator of receptor oligomerization, we show that a pIgR:ζ chimeric receptor expressed in Jurkat cells initiates a ζ-specific signal transduction cascade when exposed to dimeric or tetrameric IgA, but not when exposed to monomeric IgA. In addition, we replaced the pIgR’s transmembrane domain with that of glycophorin A to force dimerization or with a mutant glycophorin transmembrane domain to prevent dimerization. Forcing dimerization stimulated Transcytosis of the chimera, whereas preventing dimerization abolished ligand-stimulated Transcytosis. We conclude that binding of dimeric IgA to the pIgR induces its dimerization and that this dimerization is necessary and sufficient to stimulate pIgR Transcytosis.
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Signal transduction by the polymeric immunoglobulin receptor suggests a role in regulation of receptor Transcytosis.
The Journal of cell biology, 1996Co-Authors: Michael H. Cardone, Bradley L. Smith, Patricia A. Mennitt, Daria Mochly-rosen, Randi B. Silver, Keith E. MostovAbstract:Many membrane traffic events that were previously thought to be constitutive recently have been found to be regulated by a variety of intracellular signaling pathways. The polymeric immunoglobulin receptor (pIgR) transcytoses dimeric IgA (dIgA) from the basolateral to the apical surface of polarized epithelial cells. Transcytosis is stimulated by binding of dIgA to the pIgR, indicating that the pIgR can transduce a signal to the cytoplasmic machinery responsible for membrane traffic. We report that dIgA binding to the pIgR causes activation of protein kinase C (PKC) and release of inositol 1,4,5-trisphosphate (IP3). The IP3 causes an elevation of intracellular Ca. Artificially activating PKC with phorbol myristate acetate or poisoning the calcium pump with thapsigargin stimulates Transcytosis of pIgR, while the intracellular Ca chelator BAPTA-AM inhibits Transcytosis. Our data suggest that ligand-induced signaling by the pIgR may regulate membrane traffic via well-known second messenger pathways involving PKC, IP3, and Ca. This may be a model of a general means by which membrane traffic is regulated by receptor-ligand interaction and signaling pathways.
Michael G Sugiyama - One of the best experts on this subject based on the ideXlab platform.
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estrogen inhibits ldl low density lipoprotein Transcytosis by human coronary artery endothelial cells via gper g protein coupled estrogen receptor and sr bi scavenger receptor class b type 1
Arteriosclerosis Thrombosis and Vascular Biology, 2018Co-Authors: Siavash Ghaffari, Farnoosh Naderi Nabi, Michael G Sugiyama, Warren L LeeAbstract:Objective- The atheroprotective effects of estrogen are independent of circulating lipid levels. Whether estrogen regulates Transcytosis of LDL (low-density lipoprotein) across the coronary endothelium is unknown. Approach and Results- Using total internal reflection fluorescence microscopy, we quantified Transcytosis of LDL across human coronary artery endothelial cells from multiple donors. LDL Transcytosis was significantly higher in cells from men compared with premenopausal women. Estrogen significantly attenuated LDL Transcytosis by endothelial cells from male but not female donors; Transcytosis of albumin was not affected. Estrogen caused downregulation of endothelial SR-BI (scavenger receptor class B type 1), and overexpression of SR-BI was sufficient to restore LDL Transcytosis. Similarly, depletion of SR-BI by siRNA attenuated endothelial LDL Transcytosis and prevented any further effect of estrogen. In contrast, treatment with estrogen had no effect on SR-BI expression by liver cells. Inhibition of estrogen receptors α and β had no effect on estrogen-mediated attenuation of LDL Transcytosis. However, estrogen's effect on LDL Transcytosis was blocked by depletion of the GPER (G-protein-coupled estrogen receptor). GPER was found to be enriched in endothelial cells compared with hepatocytes and is reported to signal via transactivation of the EGFR (epidermal growth factor receptor); inhibition of EGFR prevented the effect of estrogen on LDL Transcytosis and SR-BI mRNA. Last, SR-BI expression was significantly higher in human coronary artery endothelial cells from male compared with premenopausal female donors. Conclusions- Estrogen significantly inhibits LDL Transcytosis by downregulating endothelial SR-BI; this effect requires GPER.
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estrogen inhibits ldl low density lipoprotein Transcytosis by human coronary artery endothelial cells via gper g protein coupled estrogen receptor and sr bi scavenger receptor class b type 1
Arteriosclerosis Thrombosis and Vascular Biology, 2018Co-Authors: Siavash Ghaffari, Farnoosh Naderi Nabi, Michael G Sugiyama, Warren L LeeAbstract:Objective— The atheroprotective effects of estrogen are independent of circulating lipid levels. Whether estrogen regulates Transcytosis of LDL (low-density lipoprotein) across the coronary endothe...
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a novel assay uncovers an unexpected role for sr bi in ldl Transcytosis
Cardiovascular Research, 2015Co-Authors: Susan Armstrong, Michael G Sugiyama, Karen Y Y Fung, Yizhuo Gao, Changsen Wang, Andrew S Levy, Paymon M Azizi, Mark Roufaiel, Suning Zhu, Dante NeculaiAbstract:Aims Retention of low-density lipoprotein (LDL) cholesterol beneath the arterial endothelium initiates an inflammatory response culminating in atherosclerosis. Since the overlying endothelium is healthy and intact early on, it is likely that LDL passes through endothelial cells by Transcytosis. However, technical challenges have made confirming this notion and elucidating the mechanisms of Transcytosis difficult. We developed a novel assay for measuring LDL Transcytosis in real time across coronary endothelial cell monolayers; we used this approach to identify the receptor involved. Methods and results Murine aortas were perfused ex vivo with LDL and dextran of a smaller molecular radius. LDL (but not dextran) accumulated under the endothelium, indicating that LDL Transcytosis occurs in intact vessels. We then confirmed that LDL Transcytosis occurs in vitro using human coronary artery endothelial cells. An assay was developed to quantify Transcytosis of DiI-LDL in real time using total internal reflection fluorescence microscopy. DiI-LDL Transcytosis was inhibited by excess unlabelled LDL, while degradation of the LDL receptor by PCSK9 had no effect. Instead, LDL colocalized partially with the scavenger receptor SR-BI and overexpression of SR-BI increased LDL Transcytosis; knockdown by siRNA significantly reduced it. Excess HDL, the canonical SR-BI ligand, significantly decreased LDL Transcytosis. Aortas from SR-BI -deficient mice were perfused ex vivo with LDL and accumulated significantly less sub-endothelial LDL compared with wild-type littermates. Conclusion We developed an assay to quantify LDL Transcytosis across endothelial cells and discovered an unexpected role for SR-BI. Elucidating the mechanisms of LDL Transcytosis may identify novel targets for the prevention or therapy of atherosclerosis.
Farnoosh Naderi Nabi - One of the best experts on this subject based on the ideXlab platform.
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estrogen inhibits ldl low density lipoprotein Transcytosis by human coronary artery endothelial cells via gper g protein coupled estrogen receptor and sr bi scavenger receptor class b type 1
Arteriosclerosis Thrombosis and Vascular Biology, 2018Co-Authors: Siavash Ghaffari, Farnoosh Naderi Nabi, Michael G Sugiyama, Warren L LeeAbstract:Objective- The atheroprotective effects of estrogen are independent of circulating lipid levels. Whether estrogen regulates Transcytosis of LDL (low-density lipoprotein) across the coronary endothelium is unknown. Approach and Results- Using total internal reflection fluorescence microscopy, we quantified Transcytosis of LDL across human coronary artery endothelial cells from multiple donors. LDL Transcytosis was significantly higher in cells from men compared with premenopausal women. Estrogen significantly attenuated LDL Transcytosis by endothelial cells from male but not female donors; Transcytosis of albumin was not affected. Estrogen caused downregulation of endothelial SR-BI (scavenger receptor class B type 1), and overexpression of SR-BI was sufficient to restore LDL Transcytosis. Similarly, depletion of SR-BI by siRNA attenuated endothelial LDL Transcytosis and prevented any further effect of estrogen. In contrast, treatment with estrogen had no effect on SR-BI expression by liver cells. Inhibition of estrogen receptors α and β had no effect on estrogen-mediated attenuation of LDL Transcytosis. However, estrogen's effect on LDL Transcytosis was blocked by depletion of the GPER (G-protein-coupled estrogen receptor). GPER was found to be enriched in endothelial cells compared with hepatocytes and is reported to signal via transactivation of the EGFR (epidermal growth factor receptor); inhibition of EGFR prevented the effect of estrogen on LDL Transcytosis and SR-BI mRNA. Last, SR-BI expression was significantly higher in human coronary artery endothelial cells from male compared with premenopausal female donors. Conclusions- Estrogen significantly inhibits LDL Transcytosis by downregulating endothelial SR-BI; this effect requires GPER.
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estrogen inhibits ldl low density lipoprotein Transcytosis by human coronary artery endothelial cells via gper g protein coupled estrogen receptor and sr bi scavenger receptor class b type 1
Arteriosclerosis Thrombosis and Vascular Biology, 2018Co-Authors: Siavash Ghaffari, Farnoosh Naderi Nabi, Michael G Sugiyama, Warren L LeeAbstract:Objective— The atheroprotective effects of estrogen are independent of circulating lipid levels. Whether estrogen regulates Transcytosis of LDL (low-density lipoprotein) across the coronary endothe...
