Relevant bibliographies by topics / Angiotensin II (AngII)

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  3. Conference papers

Academic literature on the topic 'Angiotensin II (AngII)'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 February 2022

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Journal articles on the topic "Angiotensin II (AngII)"

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Kohler, Konrad, Thomas Wheeler-Schilling, Bernhard Jurklies, Elke Guenther, and Eberhart Zrenner. "Angiotensin II in the rabbit retina." Visual Neuroscience 14, no. 1 (1997): 63–71. http://dx.doi.org/10.1017/s0952523800008762.

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AbstractWe investigated a putative local angiotensin II (AngII) system in the rabbit retina by examining AngII contents in the retina, vitreous humor, and choroid by radioimmunoassays and AngII synthesis in the retina and choroid by detection of angiotensin converting enzyme (ACE) mRNA. An antibody directed against AngII was used to localize possible cellular sources of AngII in the retina. To enhance immunoreactivity and to further examine AngII metabolism, tissues were preincubated in medium containing either protease inhibitors (PI), PI together with the AngII-precursor AngI, or PI and AngI
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Bosnyak, Sanja, Emma S. Jones, Arthur Christopoulos, Marie-Isabel Aguilar, Walter G. Thomas, and Robert E. Widdop. "Relative affinity of angiotensin peptides and novel ligands at AT1 and AT2 receptors." Clinical Science 121, no. 7 (2011): 297–303. http://dx.doi.org/10.1042/cs20110036.

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AT1R (angiotensin type 1 receptor) and AT2R (angiotensin type 2 receptor) are well known to be involved in the complex cardiovascular actions of AngII (angiotensin II). However, shorter peptide fragments of AngII are thought to have biological activity in their own right and elicit effects that oppose those mediated by AngII. In the present study, we have used HEK (human embryonic kidney)-293 cells stably transfected with either AT1R or AT2R to perform a systematic analysis of binding affinities of all the major angiotensin peptides. Additionally, we tested the novel AT2R agonist Compound 21,
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HILL-KAPTURCZAK, NATHALIE, MATTHIAS H. KAPTURCZAK, EDWARD R. BLOCK, et al. "Angiotensin II-Stimulated Nitric Oxide Release from Porcine Pulmonary Endothelium Is Mediated by Angiotensin IV." Journal of the American Society of Nephrology 10, no. 3 (1999): 481–91. http://dx.doi.org/10.1681/asn.v103481.

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Abstract. In this study, a nitric oxide (NO) sensor was used to examine the ability of angiotensin II (AngII), AngIV, and bradykinin (Bk) to stimulate NO release from porcine pulmonary artery (PPAE) and porcine aortic endothelial (PAE) cells and to explore the mechanism of the AngII-stimulated NO release. Physiologic concentrations of AngII, but not Bk, caused release of NO from PPAE cells. In contrast, Bk, but not AngII, stimulated NO release from PAE cells. AngII-stimulated NO release from PPAE cells required extracellular L-arginine and was inhibited by L-nitro-arginine methyl ester. AT1 an
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Yamaguchi, Nobuharu, Daniel Martineau, Stéphane Lamouche, and Richard Briand. "Functional role of local angiotensin-converting enzyme (ACE) in adrenal catecholamine secretion in vivo." Canadian Journal of Physiology and Pharmacology 77, no. 11 (1999): 878–85. http://dx.doi.org/10.1139/y99-094.

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The aim of the present study was to investigate whether exogenous angiotensin I (AngI) is locally converted to angiotensin II (AngII), which in turn results in an increase in the adrenal catecholamine (CA) secretion in the adrenal gland in anesthetized dogs. Plasma CA concentrations in adrenal venous and aortic blood were determined by an HPLC-electrochemical method. Adrenal venous blood flow was measured by gravimetry. Local administration of AngI (0.0062 to 6.2 µg, 0.0096 to 9.6 µM) to the left adrenal gland resulted in significant increases in CA output in a dose-dependent manner. Following
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KOBORI, HIROYUKI, LISA M. HARRISON-BERNARD, and L. GABRIEL NAVAR. "Expression of Angiotensinogen mRNA and Protein in Angiotensin II-Dependent Hypertension." Journal of the American Society of Nephrology 12, no. 3 (2001): 431–39. http://dx.doi.org/10.1681/asn.v123431.

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Abstract. Chronic elevations in circulating angiotensin II (AngII) levels produce sustained hypertension and increased intrarenal AngII contents through multiple mechanisms, which may include sustained or increased local production of AngII. This study was designed to test the hypothesis that chronic AngII infusion increases renal angiotensinogen mRNA and protein levels, thus contributing to the increase in intrarenal AngII levels. AngII (80 ng/min) was infused subcutaneously for 13 d into Sprague-Dawley rats, using osmotic minipumps. Control rats underwent sham operations. By day 12, systolic
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Horiuchi, Masatsugu, Jun Iwanami, and Masaki Mogi. "Regulation of angiotensin II receptors beyond the classical pathway." Clinical Science 123, no. 4 (2012): 193–203. http://dx.doi.org/10.1042/cs20110677.

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The RAS (renin–angiotensin system) plays a role not only in the cardiovascular system, including blood pressure regulation, but also in the central nervous system. AngII (angiotensin II) binds two major receptors: the AT1 receptor (AngII type 1 receptor) and AT2 receptor (AngII type 2 receptor). It has been recognized that AT2 receptor activation not only opposes AT1 receptor actions, but also has unique effects beyond inhibitory cross-talk with AT1 receptor signalling. Novel pathways beyond the classical actions of RAS, the ACE (angiotensin-converting enzyme)/AngII/AT1 receptor axis, have bee
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Zhou, Yi, Xiaoxu Guan, Xiaoyi Chen, et al. "Angiotensin II/Angiotensin II Receptor Blockade Affects Osteoporosis via the AT1/AT2-Mediated cAMP-Dependent PKA Pathway." Cells Tissues Organs 204, no. 1 (2017): 25–37. http://dx.doi.org/10.1159/000464461.

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Animal studies have reported on the benefits of ARB on bone mass. However, the underlying mechanism for angiotensin II (AngII)/AngII receptor blockade (ARB) in regulating bone mass remains elusive. Since high levels of plasma and urine cAMP are observed in osteoporotic and hypertensive patients, we hypothesized that cAMP may be an important molecule for the downstream events of the activation of AT receptors, members of the G-protein-coupled receptor family, in regulating bone turnover. In this study, micro-CT and X-ray analyses indicated that AngII decreased bone mass via biasing bone resorpt
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Laporte, Stéphane A., Antony A. Boucard, Guy Servant, Gaétan Guillemette, Richard Leduc, and Emanuel Escher. "Determination of Peptide Contact Points in the Human Angiotensin II Type I Receptor (AT1) with Photosensitive Analogs of Angiotensin II." Molecular Endocrinology 13, no. 4 (1999): 578–86. http://dx.doi.org/10.1210/mend.13.4.0270.

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Abstract To identify ligand-binding domains of Angiotensin II (AngII) type 1 receptor (AT1), two different radiolabeled photoreactive AngII analogs were prepared by replacing either the first or the last amino acid of the octapeptide by p-benzoyl-l-phenylalanine (Bpa). High yield, specific labeling of the AT1 receptor was obtained with the 125I-[Sar1,Bpa8]AngII analog. Digestion of the covalent 125I-[Sar1,Bpa8]AngII-AT1 complex with V8 protease generated two major fragments of 15.8 kDa and 17.8 kDa, as determined by SDS-PAGE. Treatment of the[ Sar1,Bpa8]AngII-AT1 complex with cyanogen bromide
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Jang, Hee-Seong, Jee In Kim, Jinu Kim, Jeen-Woo Park, and Kwon Moo Park. "Angiotensin II Removes Kidney Resistance Conferred by Ischemic Preconditioning." BioMed Research International 2014 (2014): 1–10. http://dx.doi.org/10.1155/2014/602149.

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Ischemic preconditioning (IPC) by ischemia/reperfusion (I/R) renders resistance to the kidney. Strong IPC triggers kidney fibrosis, which is involved in angiotensin II (AngII) and its type 1 receptor (AT1R) signaling. Here, we investigated the role of AngII/AT1R signal pathway in the resistance of IPC kidneys to subsequent I/R injury. IPC of kidneys was generated by 30 minutes of bilateral renal ischemia and 8 days of reperfusion. Sham-operation was performed to generate control (non-IPC) mice. To examine the roles of AngII and AT1R in IPC kidneys to subsequent I/R, IPC kidneys were subjected
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Binz-Lotter, Julia, Christian Jüngst, Markus M. Rinschen, et al. "Injured Podocytes Are Sensitized to Angiotensin II–Induced Calcium Signaling." Journal of the American Society of Nephrology 31, no. 3 (2020): 532–42. http://dx.doi.org/10.1681/asn.2019020109.

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BackgroundInhibition of angiotensin II (AngII) signaling, a therapeutic mainstay of glomerular kidney diseases, is thought to act primarily through regulating glomerular blood flow and reducing filtration pressure. Although extravascular actions of AngII have been suggested, a direct effect of AngII on podocytes has not been demonstrated in vivo.MethodsTo study the effects of AngII on podocyte calcium levels in vivo, we used intravital microscopy of the kidney in mice expressing the calcium indicator protein GCaMP3.ResultsIn healthy animals, podocytes displayed limited responsiveness to AngII
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Dissertations / Theses on the topic "Angiotensin II (AngII)"

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Parulkar, Madhura. "COPLANAR PCB77 AND ANGII INDUCED VASCULAR DISORDERS." UKnowledge, 2012. http://uknowledge.uky.edu/nutrisci_etds/2.

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Previous studies demonstrated that coplanar PCBs promote inflammation by release of pro-inflammatory cytokines like TNF, MCP-1, and VCAM-1 from endothelial cells as well as adipocytes. Also these PCBs at small doses may contribute to the development of obesity by inducing adipocyte differentiation. Obesity is a known risk factor that promotes cardiovascular disorders like atherosclerosis and AAAs. Evidence shows Ang II, a component of the RAS, leads to the formation of atherosclerosis and AAAs in both normal as well as hyperlipidemic mice. Earlier studies in our laboratory have also shown that
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Kemp, Jacqueline Renee. "Genome-wide Angiotensin II regulated microRNA expression profiling: A smooth muscle-specific microRNA signature." Cleveland State University / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=csu1367845628.

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Mukherjee, Kamalika. "ROLE OF CYCLOOXYGENASE-2 IN ABDOMINAL AORTIC ANEURYSMS IN MICE." UKnowledge, 2012. http://uknowledge.uky.edu/pharmacy_etds/29.

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Abdominal aortic aneurysm (AAA) is a chronic inflammatory disease with no available pharmacological treatment. AAA formation reduces the structural integrity of the vessel and increases the susceptibility to rupture. The inflammatory response within human aneurysmal tissue is characterized by increased expression of cyclooxygenase-2 (COX-2). Similarly, in a mouse model of the disease induced by chronic Angiotensin II (AngII) infusion, we have shown that COX-2 expression in the abdominal aortic smooth muscle layer increases early in the development of the disease. Furthermore, genetic or pharma
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Derrien, Alexandrine. "Étude de la régulation des sous-unités α des protéines Gq et G11 par les hormones ACTH et AngII et de leur couplage aux récepteurs à l'angiotensine II, dans les cellules fasciculoréticulées de la surrénale bovine". Lyon 1, 1997. http://www.theses.fr/1997LYO1T019.

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Flamant, Martin. "Vers de nouveaux acteurs de la fibrose vasculaire et rénale d' origine hypertensive." Paris 6, 2005. http://www.theses.fr/2005PA066298.

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Conference papers on the topic "Angiotensin II (AngII)"

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Consolini, Michelle, Tiziano Passerini, Marina Piccinelli, et al. "Shear Stress and Angiotensin II in the Development and Localization of Abdominal Aortic Aneurysms." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-205071.

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Abdominal aortic aneurysms (AAAs) develop in the infrarenal aorta of humans and in the suprarenal aorta of apoE−/− mice infused with angiotensin II (AngII). Oscillatory wall shear stress in the infrarenal human abdominal aorta is driven by the flow to the gastric arteries, the lumbar curvature and the capacitance of the lower extremities [1]. Two of these factors, the lumbar curvature and the capacitance of the lower extremities, are significantly different in mice than in humans. Therefore, we hypothesized that the differences in localization of AAAs between species is explained by difference
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Haskett, Darren, Marie Fouts, Urs Utzinger, Doug Larson, Mohamad Azhar, and Jonathan Vande Geest. "The Effects of Angiotensin II Infusion on the Mechanical Response and Microstructural Organization of Mouse Aorta." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19635.

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Vascular diseases such as aneurysm and aortic dissection account for almost 16,000 deaths in the United States annually. In both of these diseases vascular inflammation is a common pathogenic factor. Another common pathologic feature of vascular disease includes structural matrix remodeling. It is also increasingly believed that inflammation may play a key role in the formation and progression of atherosclerotic vascular disease. Angiotensin II (AngII), a potent vasopressor, is also a strong inducer of vascular inflammation and aortic remodeling in atherosclerosis-prone mice. Based on this kno
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Haskett, Darren, Urs Utzinger, Mohamad Azhar, and Jonathan Vande Geest. "Progressive Alterations in Biomechanical Response of a Mouse Model of Aneurysm." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80321.

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Abdominal aortic aneurysm (AAA) is a complex disease that leads to a localized dilation of the infrarenal aorta, the rupture of which is associated with significant morbidity and mortality, however the underlying mechanisms by which such changes remains an important unanswered question in the literature. Animal models of AAA can be used to study how changes in the microstructural and biomechanical behavior of aortic tissues develop as disease progresses in these animals. We chose here to investigate changes in mechanical characteristics with time in the established Apolipoprotein E deficient (
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Barr, Kyla N., Craig J. Goergen, Maj Hedehus, et al. "Quantification of Abdominal Aortic Aneurysm Disease Progression Using Small Animal Magnetic Resonance Imaging." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19009.

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Abdominal aortic aneurysm (AAA) disease, defined as a pathological dilation of the vessel wall, is responsible for 15,000 deaths per year in the United States. Human AAA are often asymmetric, typically expanding anteriorly as the posterior region is supported by the vertebral column [1]. Other work has shown that healthy thoracic aortic motion is also asymmetric in pigs and humans [2]. Two commonly used murine models induce AAA growth with either the infusion of angiotensin II (angII) [3] or intra-arterial perfusion of porcine pancreatic elastase (PPE) into the aortic lumen [4]. The purpose of
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