Angiotensin II via Activation of Type 1 Receptor Upregulates Expression of Endoglin in Human Coronary Artery Endothelial Cells

Li, Dayuan; Chen, Hongjiang; Mehta, Jawahar L.

doi:10.1161/hy1101.092971

Cited by 33 publications

(24 citation statements)

References 45 publications

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“…Recently, it has been reported that angiotensin II induces endoglin overexpression in cultured endothelial cells. 35 Previous studies have demonstrated that angiotensin II increases TGF-␤1 synthesis in fibroblasts, smooth muscle cells, and renal mesangial cells. 36,37 Angiotensin II also induced the expression of TGF-␤ type I and type II receptors.…”

Section: Discussionmentioning

confidence: 99%

Endoglin Upregulation During Experimental Renal Interstitial Fibrosis in Mice

et al. 2002

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Abstract-The goal of the present study was to evaluate the role of endoglin, a transforming growth factor-␤1 (TGF-␤1) accessory receptor, in the pathogenesis of renal fibrosis. This was achieved by testing a model of tubulo-interstitial fibrosis induced by unilateral ureteral obstruction in endoglin heterozygous (Eng ϩ/-) mice. Northern and Western blot analysis revealed that endoglin expression in kidneys of these mice was significantly reduced compared with Eng ϩ/ϩ littermates. Pronounced interstitial fibrosis induced by ureteral obstruction was confirmed histologically by Masson's trichromic staining and by increased immunostaining for fibronectin and laminin without significant differences between Eng ϩ/-and Eng ϩ/ϩ mice. Ureteral obstruction induced significant increases in ␣2(I) and ␣1(IV) collagen, fibronectin, and TGF-␤1 mRNA levels, as well as in total kidney collagen but changes were similar in Eng ϩ/-and Eng ϩ/ϩ mouse kidneys. Ureteral obstruction also induced a 2-fold increase in endoglin mRNA levels in both Eng ϩ/ϩ mice and Eng ϩ/-mice, which was confirmed by Western blot analysis. Thus, the present study provides clear evidence that endoglin is upregulated in the kidneys of mice with interstitial fibrosis induced by unilateral ureteral ligation. However, Eng ϩ/-mice do not show any changes in the severity of renal disease induced in this model when compared with normal mice, suggesting that the absolute level of endoglin is not critical for the effects of TGF-␤1 in the renal fibrosis process.

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Section: Discussionmentioning

confidence: 99%

Endoglin Upregulation During Experimental Renal Interstitial Fibrosis in Mice

et al. 2002

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“…38,39 Ox-LDL has also been shown to upregulate angiotensin II type 1 receptors in atherosclerosis. 4 Angiotensin II type 1 receptor expression, like ox-LDL, decreases TGF-␤ 1 synthesis and increases the expression of its receptors, 40 and may contribute to alterations in TGF-␤ 1 and its receptors.…”

Section: Discussionmentioning

confidence: 99%

Transforming Growth Factor-β ₁ Modulates Oxidatively Modified LDL–Induced Expression of Adhesion Molecules

Chen

Saldeen

et al. 2001

Circulation Research

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Abstract-Oxidatively modified LDL (ox-LDL) activates a lectin-like receptor, LOX-1, which results in the expression of adhesion molecules on endothelial surface. We investigated the regulation of the expression of transforming growth factor-␤ 1 (TGF-␤ 1 ) and its receptors by ox-LDL and the functional significance of this interaction with regard to adhesion molecule expression in human coronary artery endothelial cells (HCAECs

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“…Primer sequences as well as length of mRNA products for endoglin were taken from Li et al, 21 for ␤-3 integrin from GenBank (GenBank accession nos. G26607, M25108), and for ␤-globin from Smith et al 22 All primer pairs were synthesized by Invitrogen (Carlsbad, CA).…”

Section: Determination Of Enos Mrnamentioning

confidence: 99%

Red blood cells express a functional endothelial nitric oxide synthase

Kleinbongard¹

2006

Blood

485

418

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The synthesis of nitric oxide (NO) in the circulation has been attributed exclusively to the vascular endothelium. Red blood cells (RBCs) have been demonstrated to carry a nonfunctional NO synthase (NOS) and, due to their huge hemoglobin content, have been assumed to metabolize large quantities of NO. More recently, however, RBCs have been identified to reversibly bind, transport, and release NO within the cardiovascular system. We now provide evidence that RBCs from humans express an active and functional endothelial-type NOS (eNOS), which is localized in the plasma membrane and the cytoplasm of RBCs. This NOS is regulated by its substrate L-arginine, by calcium, and by phosphorylation via PI3 kinase. RBC-NOS activity regulates deformability of RBC membrane and inhibits activation of platelets. The NOS-dependent conversion of L-arginine IntroductionNitric oxide (NO) is a signaling molecule of major importance present in various cell types. 1,2 It modulates not only the function of the vascular wall but also that of blood cells, such as platelets and leukocytes. NO is synthesized by a family of NO synthases (NOSs) through the conversion of L-arginine to L-citrulline, using molecular oxygen. Until recently, the expression pattern of NOS isoforms appeared to be cell specific. Constitutively expressed neuronal and endothelial NOS (referred as NOS1 and NOS3) were identified in and cloned from neuronal and endothelial cells at first. Inducible NOS (NOS2) was originally isolated from activated macrophages. 3,4 In the vascular system under resting conditions, NO synthesis has been attributed exclusively to the vascular endothelium expressing a NOS3 (eNOS) isoform. Initially thought to be a simple calmodulin-regulated enzyme, it is clear that eNOS has evolved to be tightly controlled by cofactors and posttranslational modifications, phosphorylation on multiple residues, and regulated protein-protein interactions. 5,6 To date, human blood and, in particular, hemoglobin-carrying red blood cells (RBCs) have been considered as a major sink of NO. 7,8 Although early reports postulated a NOS resident in RBCs, 9 subsequent studies were unable to confirm an active NOS within RBCs. 10 Current information on the NOS isoform, its localization, and functional activity within RBCs is still inconsistent and subject to considerable debate. Most importantly, a NOS-dependent formation and release of NO-related species from RBCs has not been shown so far. In fact, the diffusion-limited chemical inactivation of NO by intra-erythrocytic hemoglobin would suggest that even if RBCs contain NOS, NO production from such would represent a futile vestigial function derived from an earlier stem-cell precursor (prior to RBC hemoglobinization).Indeed, the characterization and proof of a functional NOS in RBCs has been hampered by the high content of hemoglobin. First, the complex and oxygen-sensitive biochemistry of NO with intracellular and extracellular proteins 8 demands a composite analysis of the various constituents of the circulating NO p...

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Angiotensin II via Activation of Type 1 Receptor Upregulates Expression of Endoglin in Human Coronary Artery Endothelial Cells

Cited by 33 publications

References 45 publications

Endoglin Upregulation During Experimental Renal Interstitial Fibrosis in Mice

Endoglin Upregulation During Experimental Renal Interstitial Fibrosis in Mice

Transforming Growth Factor-β ₁ Modulates Oxidatively Modified LDL–Induced Expression of Adhesion Molecules

Red blood cells express a functional endothelial nitric oxide synthase

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Angiotensin II via Activation of Type 1 Receptor Upregulates Expression of Endoglin in Human Coronary Artery Endothelial Cells

Cited by 33 publications

References 45 publications

Endoglin Upregulation During Experimental Renal Interstitial Fibrosis in Mice

Endoglin Upregulation During Experimental Renal Interstitial Fibrosis in Mice

Transforming Growth Factor-β 1 Modulates Oxidatively Modified LDL–Induced Expression of Adhesion Molecules

Red blood cells express a functional endothelial nitric oxide synthase

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Transforming Growth Factor-β ₁ Modulates Oxidatively Modified LDL–Induced Expression of Adhesion Molecules