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Glycoconjugates and Related Molecules in Human Vascular Endothelial Cells

DOI: 10.1155/2013/963596

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Vascular endothelial cells (ECs) form the inner lining of blood vessels. They are critically involved in many physiological functions, including control of vasomotor tone, blood cell trafficking, hemostatic balance, permeability, proliferation, survival, and immunity. It is considered that impairment of EC functions leads to the development of vascular diseases. The carbohydrate antigens carried by glycoconjugates (e.g., glycoproteins, glycosphingolipids, and proteoglycans) mainly present on the cell surface serve not only as marker molecules but also as functional molecules. Recent studies have revealed that the carbohydrate composition of the EC surface is critical for these cells to perform their physiological functions. In this paper, we consider the expression and functional roles of endogenous glycoconjugates and related molecules (galectins and glycan-degrading enzymes) in human ECs. 1. Introduction Vascular endothelial cells (ECs) constitute the inner lining (endothelium) of blood vessels that form an interface between the blood and the vessel wall. Blood vessels alter their morphology and function in response to changes in blood flow, and their responses are based on blood flow detection by the vascular endothelium. ECs sense shear stress generated by flowing blood and transmit the signal to the interior of the cell, thereby evoking a cellular response [1]. The EC response to shear stress is closely linked to the regulation of vascular tone, blood coagulation and fibrinolysis, angiogenesis, and vascular remodeling. ECs also control vascular barrier regulation, passive diffusion, and active transport of substances from the blood [2]. Thus, ECs play important roles in vascular homeostatic functions, and excess activation or dysfunction of ECs is considered to lead to the development of vascular-related diseases, such as restenosis, arteriosclerosis, and cancer. Carbohydrate antigens (also called glycans) are expressed on the cell surface as components of glycoproteins, glycosphingolipids, and proteoglycans; these carbohydrate antigens contribute significantly to fundamental biological functions, such as cell differentiation, cell adhesion, cell-cell interaction, pathogen-host recognition, toxin-receptor interactions, cancer metastasis, immune responses, and regulation of signaling pathways [3]. Several studies have revealed that glycoconjugates play key roles in vascular biology. In this paper, we describe the importance of glycoconjugates in human ECs, with respect to their regulated expression and functional roles, particularly under

References

[1]  Y.-S. J. Li, J. H. Haga, and S. J. Chien, “Molecular basis of the effects of shear stress on vascular endothelial cells,” Journal of Biomechanics, vol. 38, no. 10, pp. 1949–1971, 2005.
[2]  W. C. Aird, “Phenotypic heterogeneity of the endothelium: I. Structure, function, and mechanisms,” Circulation Research, vol. 100, no. 2, pp. 158–173, 2007.
[3]  Essentials of Glycobiology, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA, 2nd edition, 2008.
[4]  H. Geyer, R. Geyer, M. Odenthal-Schnittler, and H.-J. Schnittler, “Characterization of human vascular endothelial cadherin glycans,” Glycobiology, vol. 9, no. 9, pp. 915–925, 1999.
[5]  B. K. Chacko, D. W. Scott, R. T. Chandler, and R. P. Patel, “Endothelial surface N-glycans mediate monocyte adhesion and are targets for anti-inflammatory effects of peroxisome proliferator-activated receptor γ ligands,” Journal of Biological Chemistry, vol. 286, no. 44, pp. 38738–38747, 2011.
[6]  J. J. García-Vallejo, W. van Dijk, B. van Het Hof et al., “Activation of human endothelial cells by tumor necrosis factor-α results in profound changes in the expression of glycosylation-related genes,” Journal of Cellular Physiology, vol. 206, no. 1, pp. 203–210, 2006.
[7]  Y. Peng, J. Li, and M. Geng, “The glycan profile of endothelial cells in the present of tumor-conditioned medium and potential roles of β-1,6-GlcNAc branching on HUVEC conformation,” Molecular and Cellular Biochemistry, vol. 340, no. 1-2, pp. 143–152, 2010.
[8]  D. W. Scott, J. Chen, B. K. Chacko, et al., “Role of endothelial N-glycan mannose residues in monocyte recruitment during atherogenesis,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 32, no. 8, pp. e51–e59, 2012.
[9]  C. A. Lingwood, “Glycosphingolipid functions,” Cold Spring Harbor Perspectives in Biology, vol. 3, no. 7, pp. 1–26, 2011.
[10]  B. K. Gillard, M. A. Jones, and D. M. Marcus, “Glycosphingolipids of human umbilical vein endothelial cells and smooth muscle cells,” Archives of Biochemistry and Biophysics, vol. 256, no. 2, pp. 435–445, 1987.
[11]  B. K. Gillard, M. A. Jones, A. A. Turner, D. E. Lewis, and D. M. Marcus, “Interferon-γ alters expression of endothelial cell-surface glycosphingolipids,” Archives of Biochemistry and Biophysics, vol. 279, no. 1, pp. 122–129, 1990.
[12]  N. C. A. J. van de Kar, L. A. H. Monnens, M. A. Karmali, and V. W. M. van Hinsbergh, “Tumor necrosis factor and interleukin-1 induce expression of the verocytotoxin receptor globotriaosylceramide on human endothelial cells: implications for the pathogenesis of the hemolytic uremic syndrome,” Blood, vol. 80, no. 11, pp. 2755–2764, 1992.
[13]  P. B. Eisenhauer, P. Chaturvedi, R. E. Fine et al., “Tumor necrosis factor alpha increases human cerebral endothelial cell Gb3 and sensitivity to Shiga toxin,” Infection and Immunity, vol. 69, no. 3, pp. 1889–1894, 2001.
[14]  C. H. Schweppe, M. Bielaszewska, G. Pohlentz et al., “Glycosphingolipids in vascular endothelial cells: relationship of heterogeneity in Gb3Cer/CD77 receptor expression with differential Shiga toxin 1 cytotoxicity,” Glycoconjugate Journal, vol. 25, no. 4, pp. 291–304, 2008.
[15]  M. Rajesh, A. Kolmakova, and S. Chatterjee, “Novel role of lactosylceramide in vascular endothelial growth factor-mediated angiogenesis in human endothelial cells,” Circulation Research, vol. 97, no. 8, pp. 796–804, 2005.
[16]  A. Kolmakova, M. Rajesh, D. Zang, R. Pili, and S. Chatterjee, “VEGF recruits lactosylceramide to induce endothelial cell adhesion molecule expression and angiogenesis in vitro and in vivo,” Glycoconjugate Journal, vol. 26, no. 5, pp. 547–558, 2009.
[17]  P. Mukherjee, A. C. Faber, L. M. Shelton, R. C. Baek, T. C. Chiles, and T. N. Seyfried, “Thematic review series: sphingolipids. Ganglioside GM3 suppresses the proangiogenic effects of vascular endothelial growth factor and ganglioside GD1a,” Journal of Lipid Research, vol. 49, no. 5, pp. 929–938, 2008.
[18]  S. Dasgupta, M. Yanagisawa, K. Rrishnamurthy, S. S. Liour, and R. K. Yu, “Tumor necrosis factor-α up-regulates glucuronosyltransferase gene expression in human brain endothelial cells and promotes T-cell adhesion,” Journal of Neuroscience Research, vol. 85, no. 5, pp. 1086–1094, 2007.
[19]  S. Dasgupta, J. Silva, G. Wang, and R. K. Yu, “Sulfoglucuronosyl paragloboside is a ligand for T cell adhesion: regulation of sulfoglucuronosyl paragloboside expression via nuclear factor κB signaling,” Journal of Neuroscience Research, vol. 87, no. 16, pp. 3591–3599, 2009.
[20]  S. Dasgupta, G. Wang, and R. K. Yu, “Sulfoglucuronosyl paragloboside promotes endothelial cell apoptosis in inflammation: elucidation of a novel glycosphingolipid-signaling pathway,” Journal of Neurochemistry, vol. 119, no. 4, pp. 749–759, 2011.
[21]  R. V. Iozzo, “Matrix proteoglycans: from molecular design to cellular function,” Annual Review of Biochemistry, vol. 67, pp. 609–652, 1998.
[22]  L. Schaefer and R. M. Schaefer, “Proteoglycans: from structural compounds to signaling molecules,” Cell and Tissue Research, vol. 339, no. 1, pp. 237–246, 2010.
[23]  N. J. Klein, G. I. Shennan, R. S. Heyderman, and M. Levin, “Alteration in glycosaminoglycan metabolism and surface charge on human umbilical vein endothelial cells induced by cytokines, endotoxin and neutrophils,” Journal of Cell Science, vol. 102, part 4, pp. 821–832, 1992.
[24]  S. Devaraj, J.-M. Yun, G. Adamson, J. Galvez, and I. Jialal, “C-reactive protein impairs the endothelial glycocalyx resulting in endothelial dysfunction,” Cardiovascular Research, vol. 84, no. 3, pp. 479–484, 2009.
[25]  T. M. Reine, M. Kusche-Gullberg, A. Feta, T. Jenssen, and S. O. Kolset, “Heparan sulfate expression is affected by inflammatory stimuli in primary human endothelial cells,” Glycoconjugate Journal, vol. 29, no. 1, pp. 67–76, 2012.
[26]  K. Norgard-Sumnicht and A. Varki, “Endothelial heparan sulfate proteoglycans that bind to L-selectin have glucosamine residues with unsubstituted amino groups,” Journal of Biological Chemistry, vol. 270, no. 20, pp. 12012–12024, 1995.
[27]  M. J. Robinson, P. Tessier, R. Poulsom, and N. Hogg, “The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells,” Journal of Biological Chemistry, vol. 277, no. 5, pp. 3658–3665, 2002.
[28]  D. Xu, J. Young, D. Song, and J. D. Esko, “Heparan sulfate is essential for high mobility group protein 1 (HMGB1) signaling by the receptor for advanced glycation end products (RAGE),” Journal of Biological Chemistry, vol. 286, no. 48, pp. 41736–41744, 2011.
[29]  A. M. Vogt, A. Barragan, Q. Chen, F. Kironde, D. Spillmann, and M. Wahlgren, “Heparan sulfate on endothelial cells mediates the binding of Plasmodium falciparum-infected erythrocytes via the DBL1α domain of PfEMP1,” Blood, vol. 101, no. 6, pp. 2405–2411, 2003.
[30]  K. Narita, J. Staub, J. Chien et al., “HSulf-1 inhibits angiogenesis and tumorigenesis in vivo,” Cancer Research, vol. 66, no. 12, pp. 6025–6032, 2006.
[31]  C. Ferreras, G. Rushton, C. L. Cole, et al., “Endothelial heparan sulfate 6-O-sulfation levels regulate angiogenic responses of endothelial cells to fibroblast growth factor 2 and vascular endothelial growth factor,” Journal of Biological Chemistry, vol. 287, no. 43, pp. 36132–36146, 2012.
[32]  T. Wang, Y. Ward, L. Tian et al., “CD97, an adhesion receptor on inflammatory cells, stimulates angiogenesis through binding integrin counterreceptors on endothelial cells,” Blood, vol. 105, no. 7, pp. 2836–2844, 2005.
[33]  P. Estess, A. Nandi, M. Mohamadzadeh, and M. H. Siegelman, “Interleukin 15 induces endothelial hyaluronan expression in vitro and promotes activated T cell extravasation through a CD44-dependent pathway in vivo,” Journal of Experimental Medicine, vol. 190, no. 1, pp. 9–19, 1999.
[34]  D. Vigetti, A. Genasetti, E. Karousou et al., “Proinflammatory cytokines induce hyaluronan synthesis and monocyte adhesion in human endothelial cells through hyaluronan synthase 2 (HAS2) and the nuclear factor-κB (NF-κB) pathway,” Journal of Biological Chemistry, vol. 285, no. 32, pp. 24639–24645, 2010.
[35]  M. Gouverneur, J. A. E. Spaan, H. Pannekoek, R. D. Fontijn, and H. Vink, “Fluid shear stress stimulates incorporation of hyaluronan into endothelial cell glycocalyx,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 290, no. 1, pp. H458–H462, 2006.
[36]  J. Maroski, B. J. Vorderwülbecke, K. Fiedorowicz et al., “Shear stress increases endothelial hyaluronan synthase 2 and hyaluronan synthesis especially in regard to an atheroprotective flow profile,” Experimental Physiology, vol. 96, no. 9, pp. 977–986, 2011.
[37]  J. M. Whitelock, L. D. Graham, J. Melrose, A. D. Murdoch, R. V. Iozzo, and P. Anne Underwood, “Human perlecan immunopurified from different endothelial cell sources has different adhesive properties for vascular cells,” Matrix Biology, vol. 18, no. 2, pp. 163–178, 1999.
[38]  S. Knox, J. Melrose, and J. Whitelock, “Electrophoretic, biosensor, and bioactivity analyses of perlecans of different cellular origins,” Proteomics, vol. 1, no. 12, pp. 1534–1541, 2001.
[39]  S. Knox, C. Merry, S. Stringer, J. Melrose, and J. Whitelock, “Not all perlecans are created equal. Interactions with fibroblast growth factor (FGF) 2 and FGF receptors,” Journal of Biological Chemistry, vol. 277, no. 17, pp. 14657–14665, 2002.
[40]  C. A. Vogl-Willis and I. J. Edwards, “High-glucose-induced structural changes in the heparan sulfate proteoglycan, perlecan, of cultured human aortic endothelial cells,” Biochimica et Biophysica Acta, vol. 1672, no. 1, pp. 36–45, 2004.
[41]  W. Zhang, Y.-J. Chuang, R. Swanson et al., “Antiangiogenic antithrombin down-regulates the expression of the proangiogenic heparan sulfate proteoglycan, perlecan, in endothelial cells,” Blood, vol. 103, no. 4, pp. 1185–1191, 2004.
[42]  W. Zhang, Y.-J. Chuang, T. Jin et al., “Antiangiogenic antithrombin induces global changes in the gene expression profile of endothelial cells,” Cancer Research, vol. 66, no. 10, pp. 5047–5055, 2006.
[43]  K. Sakai, T. Nakamura, K. Matsumoto, and T. Nakamura, “Angioinhibitory action of NK4 involves impaired extracellular assembly of fibronectin mediated by Perlecan-NK4 association,” Journal of Biological Chemistry, vol. 284, no. 33, pp. 22491–22499, 2009.
[44]  D. Béchard, T. Gentina, M. Delehedde et al., “Endocan is a novel chondroitin sulfate/dermatan sulfate proteoglycan that promotes hepatocyte growth factor/scatter factor mitogenic activity,” Journal of Biological Chemistry, vol. 276, no. 51, pp. 48341–48349, 2001.
[45]  M. R. Abid, X. Yi, K. Yano, S.-C. Shih, and W. C. Aird, “Vascular endocan is preferentially expressed in tumor endothelium,” Microvascular Research, vol. 72, no. 3, pp. 136–145, 2006.
[46]  M. Delehedde, L. Devenyns, C. A. Maurage, and R. R. Vivès, “Endocan in cancers: a lesson from a circulating dermatan sulfate proteoglycan,” International Journal of Cell Biology, vol. 2013, Article ID 705027, 11 pages, 2013.
[47]  M. Strazynski, J. A. Eble, H. Kresse, and E. Sch?nherr, “Interleukin (IL)-6 and IL-10 induce decorin mRNA in endothelial cells, but interaction with fibrillar collagen is essential for its translation,” Journal of Biological Chemistry, vol. 279, no. 20, pp. 21266–21270, 2004.
[48]  E. Sch?nherr, C. Sunderk?tter, R. V. Iozzo, and L. Schaefer, “Decorin, a novel player in the insulin-like growth factor system,” Journal of Biological Chemistry, vol. 280, no. 16, pp. 15767–15772, 2005.
[49]  L. R. Fiedler, E. Sch?nherr, R. Waddington et al., “Decorin regulates endothelial cell motility on collagen I through activation of insulin-like growth factor I receptor and modulation of α2β1 integrin activity,” Journal of Biological Chemistry, vol. 283, no. 25, pp. 17406–17415, 2008.
[50]  L. R. Fiedler and J. A. Eble, “Decorin regulates endothelial cell-matrix interactions during angiogenesis,” Cell Adhesion and Migration, vol. 3, no. 1, pp. 3–6, 2009.
[51]  S. Cattaruzza, M. Schiappacassi, ?. Ljungberg-Rose et al., “Distribution of PG-M/versican variants in human tissues and de novo expression of isoform V3 upon endothelial cell activation, migration, and neoangiogenesis in vitro,” Journal of Biological Chemistry, vol. 277, no. 49, pp. 47626–47635, 2002.
[52]  L. Nelimarkka, V. Kainulainen, E. Sch?nherr et al., “Expression of small extracellular chondroitin/dermatan sulfate proteoglycans is differentially regulated in human endothelial cells,” Journal of Biological Chemistry, vol. 272, no. 19, pp. 12730–12737, 1997.
[53]  S. Gengrinovitch, B. Berman, G. David, L. Witte, G. Neufeld, and D. Ron, “Glypican-1 is a VEGF165 binding proteoglycan that acts as an extracellular chaperone for VEGF165,” Journal of Biological Chemistry, vol. 274, no. 16, pp. 10816–10822, 1999.
[54]  D. Qiao, K. Meyer, and A. Friedl, “Glypican-1 stimulates Skp2 autoinduction loop and G1/S transition in endothelial cells,” Journal of Biological Chemistry, vol. 287, no. 8, pp. 5898–5909, 2012.
[55]  S. Gharagozlian, J. Borreb?k, T. Henriksen, T. K. Omsland, H. Shegarfi, and S. O. Kolset, “Effect of hyperglycemic condition on proteoglycan secretion in cultured human endothelial cells,” European Journal of Nutrition, vol. 45, no. 7, pp. 369–375, 2006.
[56]  S. S. Nunes, M. A. F. Outeiro-Bernstein, L. Juliano et al., “Syndecan-4 contributes to endothelial tubulogenesis through interactions with two motifs inside the pro-angiogenic N-terminal domain of thrombospondin-1,” Journal of Cellular Physiology, vol. 214, no. 3, pp. 828–837, 2008.
[57]  O. Noguer, J. Villena, J. Lorita, S. Vilaró, and M. Reina, “Syndecan-2 downregulation impairs angiogenesis in human microvascular endothelial cells,” Experimental Cell Research, vol. 315, no. 5, pp. 795–808, 2009.
[58]  D. M. Beauvais, B. J. Ell, A. R. McWhorter, and A. C. Rapraeger, “Syndecan-1 regulates αvβ3 and αvβ5 integrin activation during angiogenesis and is blocked by synstatin, a novel peptide inhibitor,” Journal of Experimental Medicine, vol. 206, no. 3, pp. 691–705, 2009.
[59]  D. N. W. Cooper, “Galectinomics: finding themes in complexity,” Biochimica et Biophysica Acta, vol. 1572, no. 2-3, pp. 209–231, 2002.
[60]  D. N. W. Cooper and S. H. Barondes, “God must love galectins; he made so many of them,” Glycobiology, vol. 9, no. 10, pp. 979–984, 1999.
[61]  R.-Y. Yang, G. A. Rabinovich, and F.-T. Liu, “Galectins: structure, function and therapeutic potential,” Expert Reviews in Molecular Medicine, vol. 10, p. e17, 2008.
[62]  L. G. Baum, J. J. Seilhamer, M. Pang, W. B. Levine, D. Beynon, and J. A. Berlinger, “Synthesis of an endogeneous lectin, galectin-1, by human endothelial cells is up-regulated by endothelial cell activation,” Glycoconjugate Journal, vol. 12, no. 1, pp. 63–68, 1995.
[63]  A. Ishikawa, T. Imaizumi, H. Yoshida et al., “Double-stranded RNA enhances the expression of galectin-9 in vascular endothelial cells,” Immunology and Cell Biology, vol. 82, no. 4, pp. 410–414, 2004.
[64]  V. L. Thijssen, S. Hulsmans, and A. W. Griffioen, “The galectin profile of the endothelium: altered expression and localization in activated and tumor endothelial cells,” The American Journal of Pathology, vol. 172, no. 2, pp. 545–553, 2008.
[65]  S. Alam, H. Li, A. Margariti et al., “Galectin-9 protein expression in endothelial cells is positively regulated by histone deacetylase 3,” Journal of Biological Chemistry, vol. 286, no. 51, pp. 44211–44217, 2011.
[66]  V. V. Glinsky, G. V. Glinsky, K. Rittenhouse-Olson et al., “The role of Thomsen-Friedenreich antigen in adhesion of human breast and prostate cancer cells to the endothelium,” Cancer Research, vol. 61, no. 12, pp. 4851–4857, 2001.
[67]  G. A. Rabinovich, A. Cumashi, G. A. Bianco et al., “Synthetic lactulose amines: novel class of anticancer agents that induce tumor-cell apoptosis and inhibit galectin-mediated homotypic cell aggregation and endothelial cell morphogenesis,” Glycobiology, vol. 16, no. 3, pp. 210–220, 2006.
[68]  A. I. Markowska, K. C. Jefferies, and N. Panjwani, “Galectin-3 protein modulates cell surface expression and activation of vascular endothelial Growth factor receptor 2 in human endothelial cells,” Journal of Biological Chemistry, vol. 286, no. 34, pp. 29913–29921, 2011.
[69]  C. R. Parish, C. Freeman, and M. D. Hulett, “Heparanase: a key enzyme involved in cell invasion,” Biochimica et Biophysica Acta, vol. 1471, no. 3, pp. M99–M108, 2001.
[70]  I. Vlodavsky and Y. Friedmann, “Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis,” Journal of Clinical Investigation, vol. 108, no. 3, pp. 341–347, 2001.
[71]  K. Godder, I. Vlodavsky, A. Eldor, B. B. Weksler, A. Haimovitz-Freidman, and Z. Fuks, “Heparanase activity in cultured endothelial cells,” Journal of Cellular Physiology, vol. 148, no. 2, pp. 274–280, 1991.
[72]  L. Yuan, J. Hu, Y. Luo, et al., “Upregulation of heparanase in high-glucose-treated endothelial cells promotes endothelial cell migration and proliferation and correlates with Akt and extracellular-signal-regulated kinase phosphorylation,” Molecular Vision, vol. 18, pp. 1684–1695, 2012.
[73]  G. Rao, H. G. Ding, W. Huang et al., “Reactive oxygen species mediate high glucose-induced heparanase-1 production and heparan sulphate proteoglycan degradation in human and rat endothelial cells: a potential role in the pathogenesis of atherosclerosis,” Diabetologia, vol. 54, no. 6, pp. 1527–1538, 2011.
[74]  K. E. Achyuthan and A. M. Achyuthan, “Comparative enzymology, biochemistry and pathophysiology of human exo-α-sialidases (neuraminidases),” Comparative Biochemistry and Physiology B, vol. 129, no. 1, pp. 29–64, 2001.
[75]  E. Monti, A. Preti, B. Venerando, and G. Borsani, “Recent development in mammalian sialidase molecular biology,” Neurochemical Research, vol. 27, no. 7-8, pp. 649–663, 2002.
[76]  A. S. Cross, S. W. Hyun, A. Miranda-Ribera, et al., “NEU1 and NEU3 sialidase activity expressed in human lung microvascular endothelia: NEU1 restrains endothelial cell migration, whereas NEU3 does not,” Journal of Biological Chemistry, vol. 287, no. 19, pp. 15966–15980, 2012.
[77]  K. Tran-Lundmark, P.-K. Tran, G. Paulsson-Berne et al., “Heparan sulfate in perlecan promotes mouse atherosclerosis: roles in lipid permeability, lipid retention, and smooth muscle cell proliferation,” Circulation Research, vol. 103, no. 1, pp. 43–52, 2008.
[78]  F. Huang, J. C. Thompson, P. G. Wilson, H. H. Aung, J. C. Rutledge, and L. R. Tannock, “Angiotensin II increases vascular proteoglycan content preceding and contributing to atherosclerosis development,” Journal of Lipid Research, vol. 49, no. 3, pp. 521–530, 2008.
[79]  J. Folkman, “Angiogenesis in cancer, vascular, rheumatoid and other disease,” Nature Medicine, vol. 1, no. 1, pp. 27–31, 1995.
[80]  M. M. Fuster and L. Wang, “Endothelial heparan sulfate in angiogenesis,” Progress in Molecular Biology and Translational Science, vol. 93, pp. 179–212, 2010.

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