The Experts below are selected from a list of 262788 Experts worldwide ranked by ideXlab platform
Ke-ke Yang - One of the best experts on this subject based on the ideXlab platform.
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Interaction of renin–angiotensin system and adenosine monophosphate–activated protein Kinase Signaling pathway in renal carcinogenesis of uninephrectomized rats:
Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine, 2017Co-Authors: Ke-ke Yang, Yi Sui, Hui-rong Zhou, Hai-lu ZhaoAbstract:Renin-angiotensin system and adenosine monophosphate-activated protein Kinase Signaling pathway both play important roles in carcinogenesis, but the interplay of renin-angiotensin system and adenosine monophosphate-activated protein Kinase in carcinogenesis is not clear. In this study, we researched the interaction of renin-angiotensin system and adenosine monophosphate-activated protein Kinase in renal carcinogenesis of uninephrectomized rats. A total of 96 rats were stratified into four groups: sham, uninephrectomized, and uninephrectomized treated with angiotensin-converting enzyme inhibitor or angiotensin receptor blocker. Renal adenosine monophosphate-activated protein Kinase and its downstream molecule acetyl coenzyme A carboxylase were detected by immunohistochemistry and western blot at 10 months after uninephrectomy. Meanwhile, we examined renal carcinogenesis by histological transformation and expressions of Ki67 and mutant p53. During the study, fasting lipid profiles were detected dynamically at 3, 6, 8, and 10 months. The results indicated that adenosine monophosphate-activated protein Kinase expression in uninephrectomized rats showed 36.8% reduction by immunohistochemistry and 89.73% reduction by western blot. Inversely, acetyl coenzyme A carboxylase expression increased 83.3% and 19.07% in parallel to hyperlipidemia at 6, 8, and 10 months. The histopathology of carcinogenesis in remnant kidneys was manifested by atypical proliferation and carcinoma in situ, as well as increased expressions of Ki67 and mutant p53. Intervention with angiotensin-converting enzyme inhibitor or angiotensin receptor blocker significantly prevented the inhibition of adenosine monophosphate-activated protein Kinase Signaling pathway and renal carcinogenesis in uninephrectomized rats. In conclusion, the novel findings suggest that uninephrectomy-induced disturbance in adenosine monophosphate-activated protein Kinase Signaling pathway resulted in hyperlipidemia and carcinogenesis in tubular epithelial cells, which may be largely attenuated by renin-angiotensin system blockade, implying the interaction of renin-angiotensin system and adenosine monophosphate-activated protein Kinase Signaling pathway in renal carcinogenesis of uninephrectomized rats.
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interaction of renin angiotensin system and adenosine monophosphate activated protein Kinase Signaling pathway in renal carcinogenesis of uninephrectomized rats
Tumor Biology, 2017Co-Authors: Ke-ke Yang, Yi Sui, Hui-rong Zhou, Hai-lu ZhaoAbstract:Renin–angiotensin system and adenosine monophosphate–activated protein Kinase Signaling pathway both play important roles in carcinogenesis, but the interplay of renin–angiotensin system and adenos...
R. Clinton Webb - One of the best experts on this subject based on the ideXlab platform.
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Comparative pharmacological analysis of Rho-Kinase inhibitors and identification of molecular components of Ca2+ sensitization in the rat lower urinary tract.
Biochemical pharmacology, 2007Co-Authors: Cleber E. Teixeira, Liming Jin, Fernanda Priviero, Zhekang Ying, R. Clinton WebbAbstract:We aimed to compare the expression and function of molecular components of the RhoA/Rho-Kinase Signaling pathway in the contractile responses of detrusor, trigonal and urethral smooth muscle, using selective Rho-Kinase inhibitors. Contractility studies and molecular approaches were employed to demonstrate the expression patterns and functional activity of the RhoA/Rho-Kinase Signaling pathway in the lower urinary tract. Frequency-response curves (1-32 Hz) and concentration-response curves (CRC) to carbachol (CCh, 0.01-30 microM), phenylephrine (PE, 0.01-300 microM) and endothelin-1 (ET-1, 0.01-100 nM) were significantly attenuated (p
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Targeting the vascular RhoA–Rho-Kinase Signaling pathway in hypertension
Drug Discovery Today: Therapeutic Strategies, 2005Co-Authors: Cleber E. Teixeira, R. Clinton WebbAbstract:Considerable evidence demonstrates that RhoA–Rho-Kinase Signaling plays an important role in various cellular functions including vascular smooth muscle contraction. Animal experiments have demonstrated a prominent role for this Signaling cascade in different models of hypertension. This review describes the physiological and pathophysiological roles of the RhoA–Rho-Kinase pathway, that can be considered as novel therapeutic targets in the treatment of cardiovascular diseases, such as hypertension.
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Hypertension and RhoA/Rho-Kinase Signaling in the Vasculature. Highlights From the Recent Literature
Hypertension (Dallas Tex. : 1979), 2004Co-Authors: Dexter L. Lee, R. Clinton Webb, Liming JinAbstract:Under normal conditions, contractile activity in vascular smooth muscle is initiated by either receptor activation (norepinephrine, angiotensin II, etc.) or by a stretch-activated mechanism. After this activation, several Signaling pathways can initiate a Ca2+-calmodulin interaction to stimulate phosphorylation of the light chain of myosin. Ca2+ sensitization of the contractile proteins is signaled by the RhoA/Rho-Kinase pathway to inhibit the dephosphorylation of the light chain by myosin phosphatase thereby maintaining force generation. In opposition to force generation, NO is released from endothelial cells and causes vasodilation through inhibition of the RhoA/Rho-Kinase Signaling pathway. This brief review will highlight recent studies demonstrating a role for the RhoA/Rho-Kinase Signaling pathway in the increased vasoconstriction characteristic of hypertension.
Hai-lu Zhao - One of the best experts on this subject based on the ideXlab platform.
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Interaction of renin–angiotensin system and adenosine monophosphate–activated protein Kinase Signaling pathway in renal carcinogenesis of uninephrectomized rats:
Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine, 2017Co-Authors: Ke-ke Yang, Yi Sui, Hui-rong Zhou, Hai-lu ZhaoAbstract:Renin-angiotensin system and adenosine monophosphate-activated protein Kinase Signaling pathway both play important roles in carcinogenesis, but the interplay of renin-angiotensin system and adenosine monophosphate-activated protein Kinase in carcinogenesis is not clear. In this study, we researched the interaction of renin-angiotensin system and adenosine monophosphate-activated protein Kinase in renal carcinogenesis of uninephrectomized rats. A total of 96 rats were stratified into four groups: sham, uninephrectomized, and uninephrectomized treated with angiotensin-converting enzyme inhibitor or angiotensin receptor blocker. Renal adenosine monophosphate-activated protein Kinase and its downstream molecule acetyl coenzyme A carboxylase were detected by immunohistochemistry and western blot at 10 months after uninephrectomy. Meanwhile, we examined renal carcinogenesis by histological transformation and expressions of Ki67 and mutant p53. During the study, fasting lipid profiles were detected dynamically at 3, 6, 8, and 10 months. The results indicated that adenosine monophosphate-activated protein Kinase expression in uninephrectomized rats showed 36.8% reduction by immunohistochemistry and 89.73% reduction by western blot. Inversely, acetyl coenzyme A carboxylase expression increased 83.3% and 19.07% in parallel to hyperlipidemia at 6, 8, and 10 months. The histopathology of carcinogenesis in remnant kidneys was manifested by atypical proliferation and carcinoma in situ, as well as increased expressions of Ki67 and mutant p53. Intervention with angiotensin-converting enzyme inhibitor or angiotensin receptor blocker significantly prevented the inhibition of adenosine monophosphate-activated protein Kinase Signaling pathway and renal carcinogenesis in uninephrectomized rats. In conclusion, the novel findings suggest that uninephrectomy-induced disturbance in adenosine monophosphate-activated protein Kinase Signaling pathway resulted in hyperlipidemia and carcinogenesis in tubular epithelial cells, which may be largely attenuated by renin-angiotensin system blockade, implying the interaction of renin-angiotensin system and adenosine monophosphate-activated protein Kinase Signaling pathway in renal carcinogenesis of uninephrectomized rats.
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interaction of renin angiotensin system and adenosine monophosphate activated protein Kinase Signaling pathway in renal carcinogenesis of uninephrectomized rats
Tumor Biology, 2017Co-Authors: Ke-ke Yang, Yi Sui, Hui-rong Zhou, Hai-lu ZhaoAbstract:Renin–angiotensin system and adenosine monophosphate–activated protein Kinase Signaling pathway both play important roles in carcinogenesis, but the interplay of renin–angiotensin system and adenos...
Scott P. Levick - One of the best experts on this subject based on the ideXlab platform.
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tryptase protease activated receptor 2 interactions induce selective mitogen activated protein Kinase Signaling and collagen synthesis by cardiac fibroblasts
Hypertension, 2011Co-Authors: Jennifer L. Mclarty, Giselle C. Meléndez, Gregory L. Brower, Joseph S. Janicki, Scott P. LevickAbstract:The mast cell product, tryptase, has recently been implicated to mediate fibrosis in the hypertensive heart. Tryptase has been shown to mediate noncardiac fibroblast function via activation of protease-activated receptor 2 and subsequent activation of the mitogen-activated protein Kinase pathway, including extracellular signal–regulated Kinase 1/2. Therefore, we hypothesized that this pathway may be a mechanism leading to fibrosis in the hypertensive heart. Isolated adult cardiac fibroblasts were treated with tryptase, which induced activation of extracellular signal–regulated Kinase 1/2 via protease-activated receptor 2. Blockade of protease activated receptor 2 with FSLLRY (10 μmol/L) and inhibition of the extracellular signal–regulated Kinase pathway with PD98059 (10 μmol/L) prevented collagen synthesis in isolated cardiac fibroblasts stimulated with tryptase. In contrast, p38 mitogen-activated protein Kinase and stress-activated protein/c-Jun N-terminal Kinase were not activated by tryptase. Cardiac fibroblasts isolated from spontaneously hypertensive rats showed this same pattern of activation. Treatment of spontaneously hypertensive rats with FSLLRY prevented fibrosis in these animals, indicating the in vivo applicability of the cultured fibroblast findings. Also, tryptase induced a myofibroblastic phenotype indicated by elevations in α-smooth muscle actin and extra type III domain A (ED-A) fibronectin. Thus, the results from this study demonstrate the importance of tryptase for inducing a cardiac myofibroblastic phenotype, ultimately leading to the development of cardiac fibrosis. Specifically, tryptase causes cardiac fibroblasts to increase collagen synthesis via a mechanism involving activation of protease-activated receptor 2 and subsequent induction of extracellular signal–regulated Kinase Signaling.
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Tryptase/Protease-Activated Receptor 2 Interactions Induce Selective Mitogen-Activated Protein Kinase Signaling and Collagen Synthesis by Cardiac Fibroblasts
Hypertension, 2011Co-Authors: Jennifer L. Mclarty, Giselle C. Meléndez, Gregory L. Brower, Joseph S. Janicki, Scott P. LevickAbstract:The mast cell product, tryptase, has recently been implicated to mediate fibrosis in the hypertensive heart. Tryptase has been shown to mediate noncardiac fibroblast function via activation of protease-activated receptor 2 and subsequent activation of the mitogen-activated protein Kinase pathway, including extracellular signal–regulated Kinase 1/2. Therefore, we hypothesized that this pathway may be a mechanism leading to fibrosis in the hypertensive heart. Isolated adult cardiac fibroblasts were treated with tryptase, which induced activation of extracellular signal–regulated Kinase 1/2 via protease-activated receptor 2. Blockade of protease activated receptor 2 with FSLLRY (10 μmol/L) and inhibition of the extracellular signal–regulated Kinase pathway with PD98059 (10 μmol/L) prevented collagen synthesis in isolated cardiac fibroblasts stimulated with tryptase. In contrast, p38 mitogen-activated protein Kinase and stress-activated protein/c-Jun N-terminal Kinase were not activated by tryptase. Cardiac fibroblasts isolated from spontaneously hypertensive rats showed this same pattern of activation. Treatment of spontaneously hypertensive rats with FSLLRY prevented fibrosis in these animals, indicating the in vivo applicability of the cultured fibroblast findings. Also, tryptase induced a myofibroblastic phenotype indicated by elevations in α-smooth muscle actin and extra type III domain A (ED-A) fibronectin. Thus, the results from this study demonstrate the importance of tryptase for inducing a cardiac myofibroblastic phenotype, ultimately leading to the development of cardiac fibrosis. Specifically, tryptase causes cardiac fibroblasts to increase collagen synthesis via a mechanism involving activation of protease-activated receptor 2 and subsequent induction of extracellular signal–regulated Kinase Signaling.
Cleber E. Teixeira - One of the best experts on this subject based on the ideXlab platform.
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Comparative pharmacological analysis of Rho-Kinase inhibitors and identification of molecular components of Ca2+ sensitization in the rat lower urinary tract.
Biochemical pharmacology, 2007Co-Authors: Cleber E. Teixeira, Liming Jin, Fernanda Priviero, Zhekang Ying, R. Clinton WebbAbstract:We aimed to compare the expression and function of molecular components of the RhoA/Rho-Kinase Signaling pathway in the contractile responses of detrusor, trigonal and urethral smooth muscle, using selective Rho-Kinase inhibitors. Contractility studies and molecular approaches were employed to demonstrate the expression patterns and functional activity of the RhoA/Rho-Kinase Signaling pathway in the lower urinary tract. Frequency-response curves (1-32 Hz) and concentration-response curves (CRC) to carbachol (CCh, 0.01-30 microM), phenylephrine (PE, 0.01-300 microM) and endothelin-1 (ET-1, 0.01-100 nM) were significantly attenuated (p
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Targeting the vascular RhoA–Rho-Kinase Signaling pathway in hypertension
Drug Discovery Today: Therapeutic Strategies, 2005Co-Authors: Cleber E. Teixeira, R. Clinton WebbAbstract:Considerable evidence demonstrates that RhoA–Rho-Kinase Signaling plays an important role in various cellular functions including vascular smooth muscle contraction. Animal experiments have demonstrated a prominent role for this Signaling cascade in different models of hypertension. This review describes the physiological and pathophysiological roles of the RhoA–Rho-Kinase pathway, that can be considered as novel therapeutic targets in the treatment of cardiovascular diseases, such as hypertension.
