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vegf-vascular-endothelial-growth-factor

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Journal Articles
Journal: Diabetes
Diabetes 2007;56(3):656–665
Published: 01 March 2007
... (n = 60). Normal chow–fed mice (n = 20) had no diabetes. Mice underwent unilateral femoral artery ligation and excision. A plasmid DNA encoded an engineered transcription factor designed to increase vascular endothelial growth factor expression (ZFP-VEGF). On day 10 after the operation...
Meeting Abstracts
Journal: Diabetes
Diabetes 1999;48(11):2229–2239
Published: 01 November 1999
...M E Cooper; D Vranes; S Youssef; S A Stacker; A J Cox; B Rizkalla; D J Casley; L A Bach; D J Kelly; R E Gilbert It has been suggested that the cytokine vascular endothelial growth factor (VEGF) has an important role in the pathogenesis of diabetic retinopathy, but its role in nephropathy has...
Meeting Abstracts
Journal: Diabetes
Diabetes 2021;70(Supplement_1):89-OR
Published: 01 June 2021
...MIIN ROH; HELEN TESFAYE; LLOYD P. AIELLO; SEOYOUNG C. KIM; ELISABETTA PATORNO While intravenous anti-VEGF agents are known to contribute to arterial thromboembolic events, the cardiovascular (CV) safety of intravitreal anti-VEGF inhibitors remain unclear. Using Medicare and 2 U.S. commercial...
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Mechanism-based pharmacological approaches to revert <span class="search-highlight">vascular</span> hyperglycemic...
Published: 17 May 2013
FIG. 2. Mechanism-based pharmacological approaches to revert vascular hyperglycemic memory in subjects with diabetes. ET-1, endothelin-1; H2, histone 2; VEGF, vascular endothelial growth factor. FIG. 2. Mechanism-based pharmacological approaches to revert vascular hyperglycemic memory in subject... More
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Adipose tissue–derived proteins. Adipose tissue secretes a number of protei...
Published: 01 April 2005
FIG. 2. Adipose tissue–derived proteins. Adipose tissue secretes a number of proteins with different functions. Enzymes are involved in steroid (cytocromo P450 aromatase, 17β-hydroxysteroid dehydrogenase [17βHSD], and 11β-hydroxysteroid dehydrogenase [11βHSD]) and lipid (lipoprotein lipase [LPL], cholesterol ester transfer protein [CETP]) metabolism, fibrinolitic system (plasmonigen activator inhibitor-1 [PAI-1]), and blood pressure regulation (ACE). ASP, acylation-stimulating protein; HGF, hepatic growth factor; MCP-1, monocyte chemoattractant protein-1; PGE2, prostaglandin E2; VEGF, vascular endothelial growth factor. FIG. 2. Adipose tissue–derived proteins. Adipose tissue secretes a number of proteins with different functions. Enzymes are involved in steroid (cytocromo P450 aromatase, 17β-hydroxysteroid dehydrogenase [17βHSD], and 11β-hydroxysteroid dehydrogenase [11βHSD]) and lipid (lipoprotein lipase [LPL], cholesterol ester transfer protein [CETP]) metabolism, fibrinolitic system (plasmonigen activator inhibitor-1 [PAI-1]), and blood pressure regulation (ACE). ASP, acylation-stimulating protein; HGF, hepatic growth factor; MCP-1, monocyte chemoattractant protein-1; PGE2, prostaglandin E2; VEGF, vascular endothelial growth factor. More
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Some of the important miRNAs from various studies attempting to identify dy...
Published: 16 December 2015
Figure 1 Some of the important miRNAs from various studies attempting to identify dysregulated miRNAs in DR. The left panel shows miRNAs from in vitro experiments or animal models, and the right panel shows miRNAs reported from clinical studies. Commonly identified miRNAs are represented by inters... More
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Adipocyte and VAT-EC release of inflammatory and angiogenic-related molecul...
Published: 16 January 2014
Figure 3 Adipocyte and VAT-EC release of inflammatory and angiogenic-related molecules. Inflammatory response of adipocytes and VAT-ECs from obese subjects in the 3D cocultures was evaluated by comparing the secretion of inflammatory molecules between adipocytes (AD), cocultured adipocytes/VAT-ECs (AD+ECs), and VAT-ECs (ECs). A: Heat map representation of cytokine and chemokine secretions measured by multiplex assay. Graded shades from green to red represent the secretion levels (pg/mL). Cytokines and chemokines were classified from high to low secretion. ADs were used as a control. B: Significant changes in the secretion of inflammatory molecules in 3D cocultures (AD+ECs) compared with adipocytes, and ECs are represented in the graphs. Results are expressed as the fold variation between AD, AD+ECs, or ECs and to take into account human interindividual variations. Data are presented as means ± SEM of 6 independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001 AD+ECs vs. AD and ECs vs. AD. VEGF, vascular endothelial growth factor. Figure 3. Adipocyte and VAT-EC release of inflammatory and angiogenic-related molecules. Inflammatory response of adipocytes and VAT-ECs from obese subjects in the 3D cocultures was evaluated by comparing the secretion of inflammatory molecules between adipocytes (AD), cocultured adipocytes/VAT-ECs (AD+ECs), and VAT-ECs (ECs). A: Heat map representation of cytokine and chemokine secretions measured by multiplex assay. Graded shades from green to red represent the secretion levels (pg/mL). Cytokines and chemokines were classified from high to low secretion. ADs were used as a control. B: Significant changes in the secretion of inflammatory molecules in 3D cocultures (AD+ECs) compared with adipocytes, and ECs are represented in the graphs. Results are expressed as the fold variation between AD, AD+ECs, or ECs and to take into account human interindividual variations. Data are presented as means ± SEM of 6 independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001 AD+ECs vs. AD and ECs vs. AD. VEGF, vascular endothelial growth factor. More
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Metabolic and secretory functions of human adipocytes cocultured with SAT-E...
Published: 16 January 2014
Figure 5 Metabolic and secretory functions of human adipocytes cocultured with SAT-ECs from lean subjects. A: Adipokine secretions were measured by ELISA. Comparison of leptin and adiponectin secreted from adipocytes cultured alone (AD) (□) or cocultured with lean SAT-ECs (AD+ECs) (■) for 3 days in the 3D setting. Results are represented as the fold variation between AD and AD+ECs to take into account human interindividual variations. B: Lipolytic activity was evaluated by glycerol release from AD or AD+ ECs in the absence (basal) (□) or presence (1 µmol/L) (■) of isoproterenol (Iso). *P < 0.05 basal vs. Iso. n.s., nonsignificant AD vs. AD+ECs in lean cocultures. C: Heat map representation of cytokine and chemokine secretions measured by multiplex assay. Graded shades from green to red represent the secretion levels (pg/mL). Cytokines and chemokines were classified from high to low secretion. Changes in the secretion of inflammatory molecules in 3D cocultures (AD+ECs) compared with adipocytes (AD) and SAT-ECs are represented in the graphs. Results are expressed as the fold variation between AD, AD+ECs, or ECs. AD were used as a control. Data are presented as means ± SEM of 6 independent experiments. **P < 0.01 AD+ECs vs. AD. VEGF, vascular endothelial growth factor. Figure 5. Metabolic and secretory functions of human adipocytes cocultured with SAT-ECs from lean subjects. A: Adipokine secretions were measured by ELISA. Comparison of leptin and adiponectin secreted from adipocytes cultured alone (AD) (□) or cocultured with lean SAT-ECs (AD+ECs) (■) for 3 days in the 3D setting. Results are represented as the fold variation between AD and AD+ECs to take into account human interindividual variations. B: Lipolytic activity was evaluated by glycerol release from AD or AD+ ECs in the absence (basal) (□) or presence (1 µmol/L) (■) of isoproterenol (Iso). *P < 0.05 basal vs. Iso. n.s., nonsignificant AD vs. AD+ECs in lean cocultures. C: Heat map representation of cytokine and chemokine secretions measured by multiplex assay. Graded shades from green to red represent the secretion levels (pg/mL). Cytokines and chemokines were classified from high to low secretion. Changes in the secretion of inflammatory molecules in 3D cocultures (AD+ECs) compared with adipocytes (AD) and SAT-ECs are represented in the graphs. Results are expressed as the fold variation between AD, AD+ECs, or ECs. AD were used as a control. Data are presented as means ± SEM of 6 independent experiments. **P < 0.01 AD+ECs vs. AD. VEGF, vascular endothelial growth factor. More
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Effects of recombinant cytokines IL-6 and IL-1β on cocultured cells from SA...
Published: 16 January 2014
Figure 6 Effects of recombinant cytokines IL-6 and IL-1β on cocultured cells from SAT of lean subjects. A: Leptin secretion evaluated by ELISA in adipocytes (AD) and cocultures (AD+ECs) treated or not with recombinant IL-6 (10 ng/mL) and IL-1β (1 ng/mL) during 3 days in the 3D setting. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05, **P <0.01, AD vs. AD IL-6/IL-1β or AD+ECs AD IL-6/IL-1β. ns, nonsignificant. B: Glycerol release from AD and AD+ECs treated or not with recombinant IL-6 (10 ng/mL) and IL-1β (1 ng/mL) during 3 days in the 3D setting. Glycerol release was measured after isoproterenol (1 µmol/L) stimulation for 4 h. Results are represented as the fold variation of glycerol release between AD and AD+ECs, AD IL-6/IL-1β, or AD+ECs IL-6/IL-1β. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05 AD vs. AD+ECs AD IL-6/IL-1β. C: Multiplex assay of the inflammatory secretome in cocultures treated (AD+ECs IL-6/IL-1β) or not (AD+ECs) with recombinant IL-6 (10 ng/mL) and IL-1β (1 ng/mL) during 3 days in the 3D setting. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05, **P < 0.01, AD+ECs vs. AD+ECs IL-6/IL-1β. VEGF, vascular endothelial growth factor. Figure 6. Effects of recombinant cytokines IL-6 and IL-1β on cocultured cells from SAT of lean subjects. A: Leptin secretion evaluated by ELISA in adipocytes (AD) and cocultures (AD+ECs) treated or not with recombinant IL-6 (10 ng/mL) and IL-1β (1 ng/mL) during 3 days in the 3D setting. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05, **P <0.01, AD vs. AD IL-6/IL-1β or AD+ECs AD IL-6/IL-1β. ns, nonsignificant. B: Glycerol release from AD and AD+ECs treated or not with recombinant IL-6 (10 ng/mL) and IL-1β (1 ng/mL) during 3 days in the 3D setting. Glycerol release was measured after isoproterenol (1 µmol/L) stimulation for 4 h. Results are represented as the fold variation of glycerol release between AD and AD+ECs, AD IL-6/IL-1β, or AD+ECs IL-6/IL-1β. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05 AD vs. AD+ECs AD IL-6/IL-1β. C: Multiplex assay of the inflammatory secretome in cocultures treated (AD+ECs IL-6/IL-1β) or not (AD+ECs) with recombinant IL-6 (10 ng/mL) and IL-1β (1 ng/mL) during 3 days in the 3D setting. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05, **P < 0.01, AD+ECs vs. AD+ECs IL-6/IL-1β. VEGF, vascular endothelial growth factor. More
Images
Pericyte phenotype in WAT from obese subjects. <em>A</em>: Immunofl...
Published: 16 January 2014
Figure 7 Pericyte phenotype in WAT from obese subjects. A: Immunofluorescence analysis by confocal microscopy of VAT from obese subjects using antibodies directed against type IV collagen in adipocytes (a) and blood vessels (bv) (green, Cy2-conjugated anti-mouse IgG) and NG2 in pericytes (arrows) (red, Cy3-conjugated anti-rabbit IgG). A representative photomicrograph is presented. Scale bar = 10 µm. B: Comparison of WAT pericyte-to-EC ratio between lean (SAT lean, n = 22) and obese (SAT obese, n = 12, and VAT obese, n = 26) subjects. **P < 0.05, ***P < 0.001, SAT lean vs. SAT/VAT obese. C: Multiplex assay of the inflammatory secretion profile of pericytes isolated from SAT of lean (SAT-PC lean), SAT of obese (SAT-PC obese), or VAT of obese (VAT-PC obese) subjects. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05, **P < 0.01, SAT-PC lean vs. SAT/VAT-PC obese. D: Multiplex assay of the inflammatory secretion profile in culture associating adipocytes and ECs from VAT of obese subjects (AD+ECs) with addition or not of pericytes from the same VAT depot. Pericytes were pretreated (AD+ECs+PC Dex) or not (AD+ECs+PC) with 100 nmol/L Dex) for 1 h. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05 AD+ECs vs. AD+ECs+PC Dex, #P < 0.05, AD+ECs+PC vs. AD+ECs+PC Dex. VEGF, vascular endothelial growth factor. Figure 7. Pericyte phenotype in WAT from obese subjects. A: Immunofluorescence analysis by confocal microscopy of VAT from obese subjects using antibodies directed against type IV collagen in adipocytes (a) and blood vessels (bv) (green, Cy2-conjugated anti-mouse IgG) and NG2 in pericytes (arrows) (red, Cy3-conjugated anti-rabbit IgG). A representative photomicrograph is presented. Scale bar = 10 µm. B: Comparison of WAT pericyte-to-EC ratio between lean (SAT lean, n = 22) and obese (SAT obese, n = 12, and VAT obese, n = 26) subjects. **P < 0.05, ***P < 0.001, SAT lean vs. SAT/VAT obese. C: Multiplex assay of the inflammatory secretion profile of pericytes isolated from SAT of lean (SAT-PC lean), SAT of obese (SAT-PC obese), or VAT of obese (VAT-PC obese) subjects. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05, **P < 0.01, SAT-PC lean vs. SAT/VAT-PC obese. D: Multiplex assay of the inflammatory secretion profile in culture associating adipocytes and ECs from VAT of obese subjects (AD+ECs) with addition or not of pericytes from the same VAT depot. Pericytes were pretreated (AD+ECs+PC Dex) or not (AD+ECs+PC) with 100 nmol/L Dex) for 1 h. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05 AD+ECs vs. AD+ECs+PC Dex, #P < 0.05, AD+ECs+PC vs. AD+ECs+PC Dex. VEGF, vascular endothelial growth factor. More
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Ang-1 pretreatment of VAT-ECs improves inflammation and adipocyte metabolis...
Published: 16 January 2014
Figure 8 Ang-1 pretreatment of VAT-ECs improves inflammation and adipocyte metabolism. A: Multiplex assay of the inflammatory secretome. Shown is percentage decreased in secretions in Ang-1–treated ECs (Ang-1-ECs) compared with control ECs. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05 Ang-1-ECs vs. ECs. B: Effect on glycerol release from adipocytes cultured alone (AD) or adipocytes cocultured with visceral ECs treated (AD+Ang-1-ECs) or not (AD+ECs) with Ang-1 (100 ng/mL, 24 h) after 3 days in hydrogel. Glycerol release was measured under isoproterenol (1 µmol/L)-stimulated conditions. Results are represented as the fold variation of glycerol release between AD and AD+ECs or AD+Ang-1-ECs cocultures. Data are presented as means ± SEM of 5 independent experiments. ##P < 0.01 AD vs. AD+ECs, *P < 0.05 AD+ECs vs. AD+Ang-1-ECs. C: The insulin response of AD, AD+ECs, and AD+Ang-1-ECs, cultured 3 days in the 3D setting, was evaluated after 10 nmol/L insulin stimulation of pS473 Akt during 15 min. The graph represents quantifications of the immunoblots in insulin-stimulated conditions normalized to total Akt (presented in Supplementary Fig. 13C ). Data are mean ± SEM of 5 independent experiments. ##P < 0.01 AD vs. AD+ECs, *P < 0.05 AD+ECs vs. AD+Ang-1-ECs. D: Multiplex assay of the inflammatory secretion profile in cocultures. Shown is percentage decrease in secretions in AD+Ang-1-EC cocultures compared with control AD+ECs cocultures. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05 AD+Ang-1-ECs vs. AD+ECs. VEGF, vascular endothelial growth factor. Figure 8. Ang-1 pretreatment of VAT-ECs improves inflammation and adipocyte metabolism. A: Multiplex assay of the inflammatory secretome. Shown is percentage decreased in secretions in Ang-1–treated ECs (Ang-1-ECs) compared with control ECs. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05 Ang-1-ECs vs. ECs. B: Effect on glycerol release from adipocytes cultured alone (AD) or adipocytes cocultured with visceral ECs treated (AD+Ang-1-ECs) or not (AD+ECs) with Ang-1 (100 ng/mL, 24 h) after 3 days in hydrogel. Glycerol release was measured under isoproterenol (1 µmol/L)-stimulated conditions. Results are represented as the fold variation of glycerol release between AD and AD+ECs or AD+Ang-1-ECs cocultures. Data are presented as means ± SEM of 5 independent experiments. ##P < 0.01 AD vs. AD+ECs, *P < 0.05 AD+ECs vs. AD+Ang-1-ECs. C: The insulin response of AD, AD+ECs, and AD+Ang-1-ECs, cultured 3 days in the 3D setting, was evaluated after 10 nmol/L insulin stimulation of pS473 Akt during 15 min. The graph represents quantifications of the immunoblots in insulin-stimulated conditions normalized to total Akt (presented in Supplementary Fig. 13C). Data are mean ± SEM of 5 independent experiments. ##P < 0.01 AD vs. AD+ECs, *P < 0.05 AD+ECs vs. AD+Ang-1-ECs. D: Multiplex assay of the inflammatory secretion profile in cocultures. Shown is percentage decrease in secretions in AD+Ang-1-EC cocultures compared with control AD+ECs cocultures. Data are presented as means ± SEM of 5 independent experiments. *P < 0.05 AD+Ang-1-ECs vs. AD+ECs. VEGF, vascular endothelial growth factor. More
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Concept of physiological angiogenesis. <em>1</em>) In tip cells, VE...
Published: 01 January 2011
FIG. 2. Concept of physiological angiogenesis. 1) In tip cells, VEGF stimulates DLL4/NOTCH signaling via VEGF-R2, thereby inhibiting tip cell formation and inducing VEGF-R1 expression in the endothelial cells downstream. Astrocyte-derived SDF-1 acts as an additional chemoattractant, activating CXCR4 in tip cells. 2) In stalk cells, predominance of VEGF-R1 and activation of Tie-2 by Ang-2 secreted from the tip cell lead to proliferation and survival. 3) Platelet-derived growth factor receptor (PDGFR)-β+–pericytes are attracted to the growing sprout by PDGF-B, released from tip cells. Interaction of recruited pericytes with endothelial cell–derived Jagged-1 induces the expression of Notch3 and activation of an autoregulatory loop that further enhances Notch3 activation, thereby promoting pericyte survival, investment, vascular branching, and induction of smooth muscle cell (SMC) genes. 4) Transforming growth factor (TGF)-β produced in endothelial cells further induces SMC differentiation and pericytes-derived Ang-1 binds to and activates the Tie-2 receptor on endothelial cells, thereby stimulating vessel maturation and stabilization. FIG. 2. Concept of physiological angiogenesis. 1) In tip cells, VEGF stimulates DLL4/NOTCH signaling via VEGF-R2, thereby inhibiting tip cell formation and inducing VEGF-R1 expression in the endothelial cells downstream. Astrocyte-derived SDF-1 acts as an additional chemoattractant, activating CXCR4 in tip cells. 2) In stalk cells, predominance of VEGF-R1 and activation of Tie-2 by Ang-2 secreted from the tip cell lead to proliferation and survival. 3) Platelet-derived growth factor receptor (PDGFR)-β+–pericytes are attracted to the growing sprout by PDGF-B, released from tip cells. Interaction of recruited pericytes with endothelial cell–derived Jagged-1 induces the expression of Notch3 and activation of an autoregulatory loop that further enhances Notch3 activation, thereby promoting pericyte survival, investment, vascular branching, and induction of smooth muscle cell (SMC) genes. 4) Transforming growth factor (TGF)-β produced in endothelial cells further induces SMC differentiation and pericytes-derived Ang-1 binds to and activates the Tie-2 receptor on endothelial cells, thereby stimulating vessel maturation and stabilization. More
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Impact of T2D on DNA methylation in human adipose tissue. Global DNA methyl...
Published: 16 August 2014
Figure 2 Impact of T2D on DNA methylation in human adipose tissue. Global DNA methylation in human adipose tissue of nondiabetic and T2D co-twins is shown for the nearest gene regions (A) and CpG island regions (B). Global DNA methylation is calculated as the average DNA methylation based on all CpG sites in each annotated region on the Infinium HumanMethylation450 BeadChip and is shown as the mean ± SD. TSS, proximal promoter, defined as 200 or 1,500 bp upstream of the transcription start site. Shore, flanking region of CpG islands (0–2,000 bp); Shelf, regions flanking island shores (2,000–4,000 bp from the CpG island). N, northern; S, southern. C: Cluster dendogram to visualize the overall relationship between DNA methylation profiles of individuals in the discordant twin cohort. Contr, nondiabetic subject; F, female; M, male. The cluster dendogram was generated using a hierarchical cluster analysis in R ( http://stat.ethz.ch/ R-manual/R-patched/library/stats/html/hclust.html). The absolute differences in DNA methylation of 15,627 individual sites, including 6,754 sites with increased (D) and 8,873 sites with decreased (E) DNA methylation in 28 diabetic subjects compared with 28 nondiabetic unrelated subjects in case-control cohort 2. The degree of DNA methylation in adipose tissue of the 28 nondiabetic subjects is shown for the 6,754 CpG sites with increased DNA methylation (F) and the 8,873 CpG sites with decreased DNA methylation (G) in 28 diabetic compared with 28 nondiabetic unrelated subjects in comparison with the degree of methylation of all analyzed CpG sites using the Infinium HumanMethylation450 BeadChip. Distributions of individual sites that exhibit differential DNA methylation in adipose tissue from 28 diabetic compared with 28 nondiabetic unrelated subjects in relation to nearest gene regions (H) and CpG island regions (I). The distribution of the significant sites compared with the distribution of all analyzed sites on the Infinium HumanMethylation450 BeadChip is significantly different (P values) from what is expected by chance based on χ2 tests (Pchi2). J: Significantly enriched KEGG pathways (FDR-adjusted P values <0.05) of genes that exhibit differential methylation in adipose tissue from 28 diabetic vs. 28 nondiabetic unrelated subjects. ECM, extracellular matrix; MAPK, mitogen-activated protein kinase; VEGF, vascular endothelial growth factor; GnRH, gonadotropin-releasing hormone; RI, receptor 1. K: Differential DNA methylation of IRS1, PPARG, KCNQ1, and TCF7L2 in adipose tissue from 28 diabetic vs. 28 nondiabetic unrelated subjects. The three most significant sites for each gene are presented. Data are shown as the mean ± SD. *q < 0.15 compared with nondiabetic subjects. Figure 2. Impact of T2D on DNA methylation in human adipose tissue. Global DNA methylation in human adipose tissue of nondiabetic and T2D co-twins is shown for the nearest gene regions (A) and CpG island regions (B). Global DNA methylation is calculated as the average DNA methylation based on all CpG sites in each annotated region on the Infinium HumanMethylation450 BeadChip and is shown as the mean ± SD. TSS, proximal promoter, defined as 200 or 1,500 bp upstream of the transcription start site. Shore, flanking region of CpG islands (0–2,000 bp); Shelf, regions flanking island shores (2,000–4,000 bp from the CpG island). N, northern; S, southern. C: Cluster dendogram to visualize the overall relationship between DNA methylation profiles of individuals in the discordant twin cohort. Contr, nondiabetic subject; F, female; M, male. The cluster dendogram was generated using a hierarchical cluster analysis in R (http://stat.ethz.ch/R-manual/R-patched/library/stats/html/hclust.html). The absolute differences in DNA methylation of 15,627 individual sites, including 6,754 sites with increased (D) and 8,873 sites with decreased (E) DNA methylation in 28 diabetic subjects compared with 28 nondiabetic unrelated subjects in case-control cohort 2. The degree of DNA methylation in adipose tissue of the 28 nondiabetic subjects is shown for the 6,754 CpG sites with increased DNA methylation (F) and the 8,873 CpG sites with decreased DNA methylation (G) in 28 diabetic compared with 28 nondiabetic unrelated subjects in comparison with the degree of methylation of all analyzed CpG sites using the Infinium HumanMethylation450 BeadChip. Distributions of individual sites that exhibit differential DNA methylation in adipose tissue from 28 diabetic compared with 28 nondiabetic unrelated subjects in relation to nearest gene regions (H) and CpG island regions (I). The distribution of the significant sites compared with the distribution of all analyzed sites on the Infinium HumanMethylation450 BeadChip is significantly different (P values) from what is expected by chance based on χ2 tests (Pchi2). J: Significantly enriched KEGG pathways (FDR-adjusted P values <0.05) of genes that exhibit differential methylation in adipose tissue from 28 diabetic vs. 28 nondiabetic unrelated subjects. ECM, extracellular matrix; MAPK, mitogen-activated protein kinase; VEGF, vascular endothelial growth factor; GnRH, gonadotropin-releasing hormone; RI, receptor 1. K: Differential DNA methylation of IRS1, PPARG, KCNQ1, and TCF7L2 in adipose tissue from 28 diabetic vs. 28 nondiabetic unrelated subjects. The three most significant sites for each gene are presented. Data are shown as the mean ± SD. *q < 0.15 compared with nondiabetic subjects. More
Journal Articles
Journal: Diabetes
Diabetes 1995;44(1):98–103
Published: 01 January 1995
... ischemic retinal damage. The characterization of vascular endothelial growth factor (VEGF) as an angiogenic molecule whose expression is markedly induced by hypoxia makes it a promising candidate for mediating ischemic retinal neovascularization. Thus, we have characterized the structure, binding...
Journal Articles
Journal: Diabetes
Diabetes 2004;53(3):861–864
Published: 01 March 2004
...David Ray; Manoj Mishra; Shirley Ralph; Ian Read; Robert Davies; Paul Brenchley Diabetic retinopathy and nephropathy cause significant morbidity in patients with diabetes. Vascular endothelial growth factor (VEGF) is a potent angiogenic and vascular permeability factor and is implicated in both...
Journal Articles
Journal: Diabetes
Diabetes 2022;71(5):1149–1165
Published: 22 February 2022
...; Jun Wan; Chandan K. Sen; Kanhaiya Singh Therapeutic vascular endothelial growth factor (VEGF) replenishment has met with limited success for the management of critical limb-threatening ischemia. To improve outcomes of VEGF therapy, we applied single-cell RNA sequencing (scRNA-seq) technology to study...
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Inflammatory profile of cocultured human adipocytes and myocytes: IL-6 and ...
Published: 18 February 2015
Figure 3 Inflammatory profile of cocultured human adipocytes and myocytes: IL-6 and IL-1β as key factors. Muscle cells were differentiated in the 3D hydrogel for 3 days, and then SAT or VAT adipocytes from obese subjects, cultured in the 3D hydrogel, were added for an additional period of 3 days. Media were then collected for the measurement of cytokine and chemokine secretion by a multiplex assay. A: Significant changes in the secretory profile in the 3D cultures of muscle cells and obese VAT adipocytes (AD+MYO) compared with AD as control and MYO are presented in the graph. Data are expressed as fold variations between AD (white bars), AD+MYO (black bars) and MYO (gray bars) to take into account human interindividual variations. Data are presented as the mean ± SEM of seven independent experiments. *P < 0.05, **P < 0.01 AD+MYO vs. AD. B: Significant changes in the secretory profile in the 3D cultures of muscle cells and obese SAT (MYO+SAT AD) or obese VAT adipocytes (MYO+VAT AD) are presented in the graph. Data are expressed as fold variations between MYO (control) and MYO+SAT AD (white bars) or MYO+VAT AD (black bars). Data are presented as the mean ± SEM of eight independent experiments. C: Gene expression of IL-6, IL-8, and IL-1β in muscle cells cultured alone (control, MYO, white bars) or exposed to adipocytes from paired biopsy samples of obese SAT (MYO+SAT AD, gray bars) or VAT adipocytes (MYO+VAT AD, black bars), estimated by real-time PCR. Data (fold over control, MYO) are presented as the mean ± SEM of six independent experiments performed with different adipocyte preparations. *P < 0.05, **P < 0.01 MYO+VAT AD vs. MYO. #P < 0.05, MYO+SAT AD vs. MYO+VAT AD. D: 3D VAT adipocytes were added for an additional period of 3 days and were treated with neutralizing antibodies of IL-6 (2.5 µg/mL) and IL-1β (0.5 µg/mL) (MYO+AD+abIL-6/IL-1β) IgG1 (control MYO+AD IgG) in the 3D setting. Media were then collected for multiplex assay. Black bars represent the percentage decrease in secretions in MYO+AD+abIL-6/IL-1β cocultures compared with control MYO+AD IgG cocultures. Data are presented as the mean ± SEM of five independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001, MYO+AD IgG vs. MYO+AD+abIL-6/IL-1β. E: Multiplex assay of the inflammatory secretome of myocytes treated (MYO IL-6/IL-1β, black bars) or not (MYO, white bars) with recombinant IL-6 (10 ng/mL) and IL-1β (1 ng/mL) over 3 days. Data are presented as the mean ± SEM of five independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001 MYO IL-6/IL-1β vs. MYO. ab, antibodies; FRK, fractalkine; IP-10, interferon-γ–induced protein-10; MIP1α, macrophage inflammatory protein 1α; ns, nonsignificant; VEGF, vascular endothelial growth factor. Figure 3. Inflammatory profile of cocultured human adipocytes and myocytes: IL-6 and IL-1β as key factors. Muscle cells were differentiated in the 3D hydrogel for 3 days, and then SAT or VAT adipocytes from obese subjects, cultured in the 3D hydrogel, were added for an additional period of 3 days. Media were then collected for the measurement of cytokine and chemokine secretion by a multiplex assay. A: Significant changes in the secretory profile in the 3D cultures of muscle cells and obese VAT adipocytes (AD+MYO) compared with AD as control and MYO are presented in the graph. Data are expressed as fold variations between AD (white bars), AD+MYO (black bars) and MYO (gray bars) to take into account human interindividual variations. Data are presented as the mean ± SEM of seven independent experiments. *P < 0.05, **P < 0.01 AD+MYO vs. AD. B: Significant changes in the secretory profile in the 3D cultures of muscle cells and obese SAT (MYO+SAT AD) or obese VAT adipocytes (MYO+VAT AD) are presented in the graph. Data are expressed as fold variations between MYO (control) and MYO+SAT AD (white bars) or MYO+VAT AD (black bars). Data are presented as the mean ± SEM of eight independent experiments. C: Gene expression of IL-6, IL-8, and IL-1β in muscle cells cultured alone (control, MYO, white bars) or exposed to adipocytes from paired biopsy samples of obese SAT (MYO+SAT AD, gray bars) or VAT adipocytes (MYO+VAT AD, black bars), estimated by real-time PCR. Data (fold over control, MYO) are presented as the mean ± SEM of six independent experiments performed with different adipocyte preparations. *P < 0.05, **P < 0.01 MYO+VAT AD vs. MYO. #P < 0.05, MYO+SAT AD vs. MYO+VAT AD. D: 3D VAT adipocytes were added for an additional period of 3 days and were treated with neutralizing antibodies of IL-6 (2.5 µg/mL) and IL-1β (0.5 µg/mL) (MYO+AD+abIL-6/IL-1β) IgG1 (control MYO+AD IgG) in the 3D setting. Media were then collected for multiplex assay. Black bars represent the percentage decrease in secretions in MYO+AD+abIL-6/IL-1β cocultures compared with control MYO+AD IgG cocultures. Data are presented as the mean ± SEM of five independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001, MYO+AD IgG vs. MYO+AD+abIL-6/IL-1β. E: Multiplex assay of the inflammatory secretome of myocytes treated (MYO IL-6/IL-1β, black bars) or not (MYO, white bars) with recombinant IL-6 (10 ng/mL) and IL-1β (1 ng/mL) over 3 days. Data are presented as the mean ± SEM of five independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001 MYO IL-6/IL-1β vs. MYO. ab, antibodies; FRK, fractalkine; IP-10, interferon-γ–induced protein-10; MIP1α, macrophage inflammatory protein 1α; ns, nonsignificant; VEGF, vascular endothelial growth factor. More
Meeting Abstracts
Journal: Diabetes
Diabetes 1999;48(5):1131–1137
Published: 01 May 1999
...T Marumo; V B Schini-Kerth; R Busse Vascular endothelial growth factor (VEGF) has been suggested to play a role in the pathogenesis of diabetic vascular complications. In the present study, we investigated whether expression of monocyte chemoattractant protein-1 (MCP-1), a chemokine that has been...
Journal Articles
Journal: Diabetes
Diabetes 1996;45(8):1016–1023
Published: 01 August 1996
...Hitoshi Takagi; George L King; Lloyd Paul Aiello Vascular endothelial growth factor (VEGF) plays an important role in the hypoxia-stimulated neovascularization of ischemic retinal diseases such as proliferative diabetic retinopathy. VEGF exerts its effect through two known high-affinity tyrosine...
Journal Articles
Journal: Diabetes
Diabetes 2003;52(12):2959–2968
Published: 01 December 2003
...Jun Cai; Shakil Ahmad; Wen G. Jiang; Jianhua Huang; Christopher D. Kontos; Mike Boulton; Asif Ahmed Vascular insufficiency and retinal ischemia precede many proliferative retinopathies and stimulate secretion of various vasoactive growth factors, including vascular endothelial growth factor (VEGF...