Angiotensin II-induced proliferation of aortic myocytes in spontaneously hypertensive rats

Paquet, Jean‐Luc; Baudouin-Legros, Maryvonne; Brunelle, Gilles; Meyer, Philippe

doi:10.1097/00004872-199006000-00010

Cited by 166 publications

(71 citation statements)

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“…[3H]-thymidine incorporation in SHR, but not WKY, cells is consistent with earlier reports of enhanced mitogenicity of the SHR-derived cells (Paquet et al, 1990;Bunkenberg et al, 1990). The observation in our two cell lines that [H]-thymidine responses to insulin show the converse relationship (i.e.…”

Section: Discussionsupporting

confidence: 92%

“…The two cell lines are derived from one strain of Wistar rat, SHR, which spontaneously develops hypertension and another, WKY, which remains normotensive. It has previously been reported that the SHR-derived cells show an enhanced response to All and ET-1 with respect to mitogenesis (Paquet et al, 1990;Bunkenberg et al, 1992) and PLC (Resink et al, 1989;Paquet et al, 1990;Osani & Dunn, 1992) but that there were no differences in receptor numbers and affinities between the two cell types (Bolger et al, 1991;Osani & Dunn, 1992). A recent report has shown that SHR-derived cells have an enhanced PLD response to platelet-derived growth factor, which activates an intrinsic tyrosine kinase receptor (Kondo et al, 1994).…”

Section: Introductionmentioning

confidence: 95%

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Stimulation of two vascular smooth muscle‐derived cell lines by angiotensin II: differential second messenger responses leading to mitogenesis

Morton

Baines

Masood

et al. 1995

British J Pharmacology

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1 We show here that angiotensin II (All) and endothelin-l (ET-1) stimulate [3H]-thymidine incorporation in a smooth muscle cell line derived from aortae of spontaneously hypertensive rats (SHR), but not in cells derived from normotensive controls (WKY). We have used the differential response of the two cell lines to investigate the relationship between second messenger systems and the mitogenic response.2 All produced an increase in accumulation of inositol 1,4,5-triphosphate which was greater in the SHR-derived cell line than in the WKY cells.

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Section: Discussionsupporting

confidence: 92%

Section: Introductionmentioning

confidence: 95%

Stimulation of two vascular smooth muscle‐derived cell lines by angiotensin II: differential second messenger responses leading to mitogenesis

Morton

Baines

Masood

et al. 1995

British J Pharmacology

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“…Other agents, for example, EPA, which attenuate cachexia in the MAC16 model, also have an inhibitory effect on tumour growth (Beck et al, 1991), and this has been shown to be separate from the anticachectic effect and due to starvation of the tumour of essential fatty acids such as linoleic acid (Hudson et al, 1993). However, Ang II is known to stimulate neovascularisation (Fernandez et al, 1985), which in some cases is a requirement for tumour growth, while in vitro it stimulates cell replication in the absence of blood vessels (Paquet et al, 1990). ACE inhibitors retard growth of cancer cells in vitro (Reddy et al, 1995) and inhibit tumour growth in vivo (Hii et al, 1998), possibly through an effect on angiogenesis, while long-term use of ACE inhibitors may protect against the development of cancer (Lever et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Angiotensin II directly induces muscle protein catabolism through the ubiquitin–proteasome proteolytic pathway and may play a role in cancer cachexia

2005

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The ability of angiotensin I (Ang I) and II (Ang II) to induce directly protein degradation in skeletal muscle has been studied in murine myotubes. Angiotensin I stimulated protein degradation with a parabolic dose -response curve and with a maximal effect between 0.05 and 0.1 mM. The effect was attenuated by coincubation with the angiotensin-converting enzyme (ACE) inhibitor imidaprilat, suggesting that angiotensin I stimulated protein degradation through conversion to Ang II. Angiotensin II also stimulated protein breakdown with a similar dose -response curve, and with a maximal effect between 1 and 2.5 mM. Total protein degradation, induced by both Ang I and Ang II, was attenuated by the proteasome inhibitors lactacystin (5 mM) and MG132 (10 mM), suggesting that the effect was mediated through upregulation of the ubiquitin -proteasome proteolytic pathway. Both Ang I and Ang II stimulated an increased proteasome 'chymotrypsin-like' enzyme activity as well as an increase in protein expression of 20S proteasome a-subunits, the 19S subunits MSS1 and p42, at the same concentrations as those inducing protein degradation. The effect of Ang I was attenuated by imidaprilat, confirming that it arose from conversion to Ang II. These results suggest that Ang II stimulates protein degradation in myotubes through induction of the ubiquitin -proteasome pathway. Protein degradation induced by Ang II was inhibited by insulin-like growth factor and by the polyunsaturated fatty acid, eicosapentaenoic acid. These results suggest that Ang II has the potential to cause muscle atrophy through an increase in protein degradation. The highly lipophilic ACE inhibitor imidapril (Vitort) (30 mg kg À1 ) attenuated the development of weight loss in mice bearing the MAC16 tumour, suggesting that Ang II may play a role in the development of cachexia in this model.

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“…[7][8][9] As regards vascular remodeling, several studies have shown that AII promotes proliferation, migration, and growth factor synthesis in several types of vascular cells, including smooth muscle cells and pericytes. [10][11][12][13] Other studies have also investigated the angiogenic effects of exogenous AII in vivo angiogenesis models. [14][15][16][17] Furthermore, recent studies have revealed local expression of several components of the RAS in various cancer cells and tissues.…”

mentioning

confidence: 99%

Roles for host and tumor angiotensin II type 1 receptor in tumor growth and tumor-associated angiogenesis

Imai

Hashimoto

Kihara

et al. 2007

Laboratory Investigation

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Angiotensin II (AII) is a multifunctional bioactive peptide, and host renin-angiotensin system (RAS) is closely associated with tumor growth. Recent reports have described that AII is a proangiogenic growth factor, and that Angiotensin II type 1 (AT1) receptor antagonists reduce tumor growth and tumor-associated angiogenesis. In this paper, we investigated the participation of AT1 receptor-signaling in cancer progression using murine Lewis lung carcinoma (LLC) cells, which express AT1 receptor, and AT1a receptor gene-deficient (AT1aÀ/À) mice. When LLC cells were implanted subcutaneously into wild-type (WT) mice, developed tumors showed intensive angiogenesis with an induction of vascular endothelial growth factor (VEGF) a. Compared with WT mice, tumor growth and tumor-associated angiogenesis was reduced in AT1aÀ/À mice with reduced expression of VEGFa. In AT1aÀ/À mice, administration of the AT1 receptor antagonist, TCV-116, showed further reductions of tumor growth, tumor-associated angiogenesis, and VEGFa expression. In vitro study, the expression of VEGFa mRNA and the production of VEGFa protein in LLC cells were significantly increased by AII, which were cancelled by AT1 receptor antagonist, CV-11974. Although the expression of other angiogenic factors, such as angiopoietin-1, angiopoietin-2, epidermal growth factor, and VEGF receptor 2 mRNA, was also investigated in tumor tissues, the expression of VEGFa was most correlated with tumor size among those other angiogenic factors. VEGFa induction by AT1 receptor-signaling in both host and tumor tissues is one of key regulators of tumor growth and tumor-associated angiogenesis. In conclusion, tumor tissue RAS as well as host tissue RAS were found to have an important role in tumor growth. AT1 receptor-signaling blockade may be a novel and effective target in the treatment of cancer. The renin-angiotensin system (RAS) plays important roles in the regulation of cardiovascular homeostasis and blood pressure. 1 Many pathophysiological activities of angiotensin II (AII) are known to be mediated by the seven transmembrane receptors. Two major subtypes of AII receptors, namely AT1 receptor and AT2 receptor, have been identified, with the former having receptor subtypes, AT1a and AT1b. 2 Most of AII functions in the cardiovascular system are mediated through the AT1 receptor, and in rodents they are mediated through the AT1a receptor. [3][4][5][6] Recently, many reports have suggested that AII is involved in other functions, such as apoptosis, vascular remodeling, and inflammation. 7-9 As regards vascular remodeling, several studies have shown that AII promotes proliferation, migration, and growth factor synthesis in several types of vascular cells, including smooth muscle cells and pericytes. [10][11][12][13] Other studies have also investigated the angiogenic effects of exogenous AII in vivo angiogenesis models. 14-17 Furthermore, recent studies have revealed local expression of several components of the RAS in various cancer cells and tissues. 18 A large-scale clinica...

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Angiotensin II-induced proliferation of aortic myocytes in spontaneously hypertensive rats

Cited by 166 publications

References 0 publications

Stimulation of two vascular smooth muscle‐derived cell lines by angiotensin II: differential second messenger responses leading to mitogenesis

Stimulation of two vascular smooth muscle‐derived cell lines by angiotensin II: differential second messenger responses leading to mitogenesis

Angiotensin II directly induces muscle protein catabolism through the ubiquitin–proteasome proteolytic pathway and may play a role in cancer cachexia

Roles for host and tumor angiotensin II type 1 receptor in tumor growth and tumor-associated angiogenesis

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