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Molecule Glycomimetics Inhibit Vascular Calcification via c-Met/Notch3/HES1 Signalling.\nBACKGROUND/AIMS: Vascular calcification represents a huge clinical problem contributing to adverse cardiovascular events, with no effective treatment currently available. Upregulation of hepatocyte growth factor has been linked with vascular calcification, and thus, represent a potential target in the development of a novel therapeutic strategy. Glycomimetics have been shown to interrupt HGF-receptor signalling, therefore this study investigated the effect of novel glycomimetics on osteogenic signalling and vascular calcification in vitro.\nMETHODS: Primary human vascular smooth muscle cells (HVSMCs) were induced by β-glycerophosphate (β-GP) and treated with 4 glycomimetic compounds (C1-C4). The effect of β-GP and C1-C4 on alkaline phosphatase (ALP), osteogenic markers and c-Met/Notch3/HES1 signalling was determined using colorimetric assays, qRT-PCR and western blotting respectively.\nRESULTS: C1-C4 significantly attenuated β-GP-induced calcification, as shown by Alizarin Red S staining and calcium content by day 14. In addition, C1-C4 reduced ALP activity and prevented upregulation of the osteogenic markers, BMP-2, Runx2, Msx2 and OPN. Furthermore, β-GP increased c-Met phosphorylation at day 21, an effect ameliorated by C2 and C4 and the c-Met inhibitor, crizotinib. We next interrogated the effects of the Notch inhibitor DAPT and confirmed an inhibition of β-GP up-regulated Notch3 protein by C2, DAPT and crizotinib compared to controls. Hes-1 protein upregulation by β-GP, was also significantly downregulated by C2 and DAPT. GOLD docking analysis identified a potential binding interaction of C1-C4 to HGF which will be investigated further.\nCONCLUSION: These findings demonstrate that glycomimetics have potent anti-calcification properties acting via HGF/c-Met and Notch signalling."}

{"project":"PubMed_Structured_Abstracts","denotations":[{"id":"T1","span":{"begin":111,"end":639},"obj":"OBJECTIVE"},{"id":"T2","span":{"begin":649,"end":990},"obj":"METHODS"},{"id":"T3","span":{"begin":1000,"end":1760},"obj":"RESULTS"},{"id":"T4","span":{"begin":1773,"end":1903},"obj":"CONCLUSIONS"}],"text":"Small Molecule Glycomimetics Inhibit Vascular Calcification via c-Met/Notch3/HES1 Signalling.\nBACKGROUND/AIMS: Vascular calcification represents a huge clinical problem contributing to adverse cardiovascular events, with no effective treatment currently available. Upregulation of hepatocyte growth factor has been linked with vascular calcification, and thus, represent a potential target in the development of a novel therapeutic strategy. Glycomimetics have been shown to interrupt HGF-receptor signalling, therefore this study investigated the effect of novel glycomimetics on osteogenic signalling and vascular calcification in vitro.\nMETHODS: Primary human vascular smooth muscle cells (HVSMCs) were induced by β-glycerophosphate (β-GP) and treated with 4 glycomimetic compounds (C1-C4). The effect of β-GP and C1-C4 on alkaline phosphatase (ALP), osteogenic markers and c-Met/Notch3/HES1 signalling was determined using colorimetric assays, qRT-PCR and western blotting respectively.\nRESULTS: C1-C4 significantly attenuated β-GP-induced calcification, as shown by Alizarin Red S staining and calcium content by day 14. In addition, C1-C4 reduced ALP activity and prevented upregulation of the osteogenic markers, BMP-2, Runx2, Msx2 and OPN. Furthermore, β-GP increased c-Met phosphorylation at day 21, an effect ameliorated by C2 and C4 and the c-Met inhibitor, crizotinib. We next interrogated the effects of the Notch inhibitor DAPT and confirmed an inhibition of β-GP up-regulated Notch3 protein by C2, DAPT and crizotinib compared to controls. Hes-1 protein upregulation by β-GP, was also significantly downregulated by C2 and DAPT. GOLD docking analysis identified a potential binding interaction of C1-C4 to HGF which will be investigated further.\nCONCLUSION: These findings demonstrate that glycomimetics have potent anti-calcification properties acting via HGF/c-Met and Notch signalling."}

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musculus"},{"id":"T55","span":{"begin":1263,"end":1265},"obj":"CVCL_S009|Spontaneously_immortalized_cell_line|Epinephelus tauvina"},{"id":"T56","span":{"begin":1276,"end":1277},"obj":"CVCL_S361|Finite_cell_line|Mus musculus"},{"id":"T57","span":{"begin":1309,"end":1311},"obj":"CVCL_8754|Cancer_cell_line|Homo sapiens"},{"id":"T58","span":{"begin":1309,"end":1311},"obj":"CVCL_H241|Cancer_cell_line|Homo sapiens"},{"id":"T59","span":{"begin":1334,"end":1336},"obj":"CVCL_1G31|Induced_pluripotent_stem_cell|Pan troglodytes"},{"id":"T60","span":{"begin":1334,"end":1336},"obj":"CVCL_4722|Cancer_cell_line|Rattus norvegicus"},{"id":"T61","span":{"begin":1334,"end":1336},"obj":"CVCL_7426|Finite_cell_line|Homo sapiens"},{"id":"T62","span":{"begin":1334,"end":1336},"obj":"CVCL_L327|Cancer_cell_line|Canis lupus familiaris"},{"id":"T63","span":{"begin":1341,"end":1343},"obj":"CVCL_1G33|Induced_pluripotent_stem_cell|Pan troglodytes"},{"id":"T64","span":{"begin":1341,"end":1343},"obj":"CVCL_4783|Cancer_cell_line|Homo sapiens"},{"id":"T65","span":{"begin":1341,"end":1343},"obj":"CVCL_5111|Cancer_cell_line|Homo sapiens"},{"id":"T66","span":{"begin":1341,"end":1343},"obj":"CVCL_7311|Finite_cell_line|Homo sapiens"},{"id":"T67","span":{"begin":1341,"end":1343},"obj":"CVCL_H536|Cancer_cell_line|Rattus norvegicus"},{"id":"T68","span":{"begin":1341,"end":1343},"obj":"CVCL_W593|Induced_pluripotent_stem_cell|Homo sapiens"},{"id":"T69","span":{"begin":1352,"end":1353},"obj":"CVCL_S361|Finite_cell_line|Mus musculus"},{"id":"T70","span":{"begin":1381,"end":1383},"obj":"CVCL_5M23|Cancer_cell_line|Mesocricetus auratus"},{"id":"T71","span":{"begin":1437,"end":1441},"obj":"CVCL_D279|Cancer_cell_line|Homo sapiens"},{"id":"T72","span":{"begin":1456,"end":1458},"obj":"CVCL_8754|Cancer_cell_line|Homo sapiens"},{"id":"T73","span":{"begin":1456,"end":1458},"obj":"CVCL_H241|Cancer_cell_line|Homo sapiens"},{"id":"T74","span":{"begin":1475,"end":1477},"obj":"CVCL_S009|Spontaneously_immortalized_cell_line|Epinephelus tauvina"},{"id":"T75","span":{"begin":1509,"end":1511},"obj":"CVCL_1G31|Induced_pluripotent_stem_cell|Pan troglodytes"},{"id":"T76","span":{"begin":1509,"end":1511},"obj":"CVCL_4722|Cancer_cell_line|Rattus norvegicus"},{"id":"T77","span":{"begin":1509,"end":1511},"obj":"CVCL_7426|Finite_cell_line|Homo sapiens"},{"id":"T78","span":{"begin":1509,"end":1511},"obj":"CVCL_L327|Cancer_cell_line|Canis lupus familiaris"},{"id":"T79","span":{"begin":1513,"end":1517},"obj":"CVCL_D279|Cancer_cell_line|Homo sapiens"},{"id":"T80","span":{"begin":1555,"end":1560},"obj":"CVCL_D092|Embryonic_stem_cell|Homo sapiens"},{"id":"T81","span":{"begin":1587,"end":1589},"obj":"CVCL_S009|Spontaneously_immortalized_cell_line|Epinephelus tauvina"},{"id":"T82","span":{"begin":1631,"end":1633},"obj":"CVCL_1G31|Induced_pluripotent_stem_cell|Pan troglodytes"},{"id":"T83","span":{"begin":1631,"end":1633},"obj":"CVCL_4722|Cancer_cell_line|Rattus norvegicus"},{"id":"T84","span":{"begin":1631,"end":1633},"obj":"CVCL_7426|Finite_cell_line|Homo sapiens"},{"id":"T85","span":{"begin":1631,"end":1633},"obj":"CVCL_L327|Cancer_cell_line|Canis lupus familiaris"},{"id":"T86","span":{"begin":1638,"end":1642},"obj":"CVCL_D279|Cancer_cell_line|Homo sapiens"},{"id":"T87","span":{"begin":1677,"end":1678},"obj":"CVCL_6479|Finite_cell_line|Mus musculus"},{"id":"T88","span":{"begin":1712,"end":1714},"obj":"CVCL_1G30|Induced_pluripotent_stem_cell|Pan troglodytes"},{"id":"T89","span":{"begin":1712,"end":1714},"obj":"CVCL_L326|Cancer_cell_line|Canis lupus familiaris"},{"id":"T90","span":{"begin":1712,"end":1714},"obj":"CVCL_RG57|Induced_pluripotent_stem_cell|Homo sapiens"},{"id":"T91","span":{"begin":1712,"end":1714},"obj":"CVCL_WT75|Induced_pluripotent_stem_cell|Homo sapiens"},{"id":"T92","span":{"begin":1715,"end":1717},"obj":"CVCL_1G33|Induced_pluripotent_stem_cell|Pan troglodytes"},{"id":"T93","span":{"begin":1715,"end":1717},"obj":"CVCL_4783|Cancer_cell_line|Homo sapiens"},{"id":"T94","span":{"begin":1715,"end":1717},"obj":"CVCL_5111|Cancer_cell_line|Homo sapiens"},{"id":"T95","span":{"begin":1715,"end":1717},"obj":"CVCL_7311|Finite_cell_line|Homo sapiens"},{"id":"T96","span":{"begin":1715,"end":1717},"obj":"CVCL_H536|Cancer_cell_line|Rattus norvegicus"},{"id":"T97","span":{"begin":1715,"end":1717},"obj":"CVCL_W593|Induced_pluripotent_stem_cell|Homo sapiens"},{"id":"T98","span":{"begin":1876,"end":1877},"obj":"CVCL_S361|Finite_cell_line|Mus musculus"}],"text":"Small Molecule Glycomimetics Inhibit Vascular Calcification via c-Met/Notch3/HES1 Signalling.\nBACKGROUND/AIMS: Vascular calcification represents a huge clinical problem contributing to adverse cardiovascular events, with no effective treatment currently available. Upregulation of hepatocyte growth factor has been linked with vascular calcification, and thus, represent a potential target in the development of a novel therapeutic strategy. Glycomimetics have been shown to interrupt HGF-receptor signalling, therefore this study investigated the effect of novel glycomimetics on osteogenic signalling and vascular calcification in vitro.\nMETHODS: Primary human vascular smooth muscle cells (HVSMCs) were induced by β-glycerophosphate (β-GP) and treated with 4 glycomimetic compounds (C1-C4). The effect of β-GP and C1-C4 on alkaline phosphatase (ALP), osteogenic markers and c-Met/Notch3/HES1 signalling was determined using colorimetric assays, qRT-PCR and western blotting respectively.\nRESULTS: C1-C4 significantly attenuated β-GP-induced calcification, as shown by Alizarin Red S staining and calcium content by day 14. In addition, C1-C4 reduced ALP activity and prevented upregulation of the osteogenic markers, BMP-2, Runx2, Msx2 and OPN. Furthermore, β-GP increased c-Met phosphorylation at day 21, an effect ameliorated by C2 and C4 and the c-Met inhibitor, crizotinib. We next interrogated the effects of the Notch inhibitor DAPT and confirmed an inhibition of β-GP up-regulated Notch3 protein by C2, DAPT and crizotinib compared to controls. Hes-1 protein upregulation by β-GP, was also significantly downregulated by C2 and DAPT. GOLD docking analysis identified a potential binding interaction of C1-C4 to HGF which will be investigated further.\nCONCLUSION: These findings demonstrate that glycomimetics have potent anti-calcification properties acting via HGF/c-Met and Notch signalling."}