Enhancement of phosphatidylcholine biosynthesis by angiotensin-(1–7) in the rat renal cortex

Gironacci, Mariela M.; Fernández-Tomé, Marı́a del Carmen; Speziale, E.; Sterín-Speziale, Norma; Peña, Clara

doi:10.1016/s0006-2952(01)00920-0

Cited by 15 publications

(11 citation statements)

References 29 publications

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“…These studies followed the report that the ANG-(1-7) increase in glomerular filtration rate was associated with a substantial natriuretic and diuretic response in isolated rat kidneys (30). The inhibitory effects of ANG-(1-7) on transcellular sodium transport is associated with activation of phospholipase A 2 (4), increased phosphatidylcholine (53), and release of cyclooxygenase products (27) ( Table 1). Inhibition of Na ϩ -K ϩ -ATPase activity by ANG-(1-7) may be under dual regulation of both AT 1 and AT 2 receptors (29), although in the rat low ANG-(1-7) (10 Ϫ12 M) concentrations increase fluid reabsorption while the opposite is true at higher concentrations (10 Ϫ8 M) (51).…”

mentioning

confidence: 63%

“…Effects are blocked by the ANG-(1-7) antagonist A-779 (52). Enhanced phosphatidylcholine biosynthesis by ANG-(1-7) in the rat renal cortex is mediated by a non-AT1/AT2 receptor (53). The generation of ANG IV [ANG-(3-7)] (from the NH2-terminal metabolism of ANG-(1-7) is implicated in eliciting a decrease in energy-dependent solute transport in proximal renal tubules (56).…”

Section: Actions On Electrolyte Transport Across Renal Tubulesmentioning

confidence: 99%

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The ANG-(1–7)/ACE2/mas axis in the regulation of nephron function

Ferrario

Varagić

2010

American Journal of Physiology-Renal Physiology

135

144

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The study of experimental hypertension and the development of drugs with selective inhibitory effects on the enzymes and receptors constituting the components of the circulating and tissue renin-angiotensin systems have led to newer concepts of how this system participates in both physiology and pathology. Over the last decade, a renewed emphasis on understanding the role of angiotensin-(1-7) and angiotensin-converting enzyme 2 in the regulation of blood pressure and renal function has shed new light on the complexity of the mechanisms by which these components of the renin angiotensin system act in the heart and in the kidneys to exert a negative regulatory influence on angiotensin converting enzyme and angiotensin II. The vasodepressor axis composed of angiotensin-(1-7)/angiotensin-converting enzyme 2/mas receptor emerges as a site for therapeutic interventions within the renin-angiotensin system. This review summarizes the evolving knowledge of the counterregulatory arm of the renin-angiotensin system in the control of nephron function and renal disease.

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mentioning

confidence: 63%

Section: Actions On Electrolyte Transport Across Renal Tubulesmentioning

confidence: 99%

The ANG-(1–7)/ACE2/mas axis in the regulation of nephron function

Ferrario

Varagić

2010

American Journal of Physiology-Renal Physiology

135

144

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“…One example is the use of angiotensin converting enzyme 2 (ACE2), which catalyzes the production of the potent vasodilator angiotensin 1-7 (ANG1-7) (229). ANG1-7 works via a non-PKC pathway (269) and counteracts the influences of the PKC-linked AT-1 receptor on cardiac hypertrophy (179,717,976). Lentiviral-mediated gene transfer of ACE2 produced strong cardiac expression and renal expression, albeit to a lesser extent.…”

Section: Signaling Upstream From Pkcmentioning

confidence: 99%

Designing Heart Performance by Gene Transfer

Davis¹,

Westfall²,

Townsend³

et al. 2008

Physiological Reviews

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The birth of molecular cardiology can be traced to the development and implementation of high-fidelity genetic approaches for manipulating the heart. Recombinant viral vector-based technology offers a highly effective approach to genetically engineer cardiac muscle in vitro and in vivo. This review highlights discoveries made in cardiac muscle physiology through the use of targeted viral-mediated genetic modification. Here the history of cardiac gene transfer technology and the strengths and limitations of viral and nonviral vectors for gene delivery are reviewed. A comprehensive account is given of the application of gene transfer technology for studying key cardiac muscle targets including Ca2+handling, the sarcomere, the cytoskeleton, and signaling molecules and their posttranslational modifications. The primary objective of this review is to provide a thorough analysis of gene transfer studies for understanding cardiac physiology in health and disease. By comparing results obtained from gene transfer with those obtained from transgenesis and biophysical and biochemical methodologies, this review provides a global view of cardiac structure-function with an eye towards future areas of research. The data presented here serve as a basis for discovery of new therapeutic targets for remediation of acquired and inherited cardiac diseases.

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“…3 Prolonged stimulation of Mas R with Ang-(1-7) or with high concentrations of the ligand caused an attenuation of R responsiveness, 4-6 suggesting receptor desensitization. Receptor desensitization represents an important physiological “feedback” mechanism that protects against both acute and chronic R overstimulation and is the consequence of a combination of different mechanisms.…”

Section: Introductionmentioning

confidence: 99%

Angiotensin (1-7) Induces Mas Receptor Internalization

et al. 2011

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Angiotensin (Ang) (1-7) is the endogenous ligand for the G protein-coupled receptor Mas, a receptor (R) associated with cardiac, renal and cerebral protective responses. Physiological evidence suggests that Mas R undergoes agonist-dependent desensitization, but the underlying molecular mechanism regulating R activity is unknown. We investigated the hypothesis that Mas R desensitizes and internalizes upon stimulation with Ang-(1-7). For this purpose, we generated a chimera between the Mas R and the fluorescent protein YFP (MasR-YFP). MasR-YFP transfected HEK 293T cells were incubated with Ang-(1-7) and the relative cellular distribution of MasR-YFP was observed by confocal microscopy. In resting cells, MasR-YFP was mostly localized to the cell membrane. Ang-(1-7) induced a redistribution of MasR-YFP to intracellular vesicles of various sizes after 5 min. Following the time course of [125I]Ang-(1-7) endocytosis we observed that half of MasR-YFP underwent endocytosis after 10 min and this was blocked by a Mas R antagonist. MasR-YFP colocalized with Rab5, the early endosome antigen 1 and the adaptor protein complex 2, indicating that the R is internalized through a clathrin-mediated pathway and targeted to early endosomes after Ang-(1-7) stimulation. A fraction of MasR-YFP also colocalized with caveolin-1 suggesting that at some point MasR-YFP traverses caveolin-1 positive compartments. In conclusion, Mas R undergoes endocytosis upon stimulation with Ang-(1-7) and this event may explain the desensitization of Mas R responsiveness. In this way, Mas R activity and density may be tightly controlled by the cell.

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Enhancement of phosphatidylcholine biosynthesis by angiotensin-(1–7) in the rat renal cortex

Cited by 15 publications

References 29 publications

The ANG-(1–7)/ACE2/mas axis in the regulation of nephron function

The ANG-(1–7)/ACE2/mas axis in the regulation of nephron function

Designing Heart Performance by Gene Transfer

Angiotensin (1-7) Induces Mas Receptor Internalization

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