Endothelium-derived nitric oxide mediates the antiadrenergic effect of human vasostatin-1 in rat ventricular myocardium

Gallo, Maria Pia; Levi, Renzo; Ramella, Roberta; Brero, Alessia; Boero, Ombretta; Tota, Bruno; Alloatti, Giuseppe

doi:10.1152/ajpheart.01253.2006

Cited by 52 publications

(60 citation statements)

References 27 publications

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“…In a previous work we showed a PI3K-dependent increase in NO production in VS-1-treated BAE-1 cells [Gallo et al, 2007]. In the present report we observed that VS-1 induces a HSPGs-PI3K-dependent endocytosis of caveolae.…”

Section: Vs-1 Induces a Pi3k And Proteoglycan-dependent Enos Phosphorsupporting

confidence: 73%

“…In a recent report we showed that in BAE-1 cells VS-1 induced a PI3K-dependent NO release [Gallo et al, 2007]. To investigate the role of the PI3K pathway also in the VS-1-dependent endocytotic vesicles formation, we performed the FM 1-43 experiments in the presence of the PI3K inhibitor Wortmannin (100 nM).…”

Section: Heparinase and Wortmannin Abolish The Vs-1-dependent Vesiclementioning

confidence: 99%

“…As VS-1 stimulates NO production [Gallo et al, 2007], we hypothesized that the endocytotic process triggered by this endogenous peptide was caveolae dependent. To verify this hypothesis we followed the cellular localization of caveolin 1 (Cav1) by immunofluorescence experiments in different conditions (Fig.…”

Section: The Vs-1-induced Endocytosis Involves Caveolin 1 Traffickingmentioning

confidence: 99%

“…In previous studies [Gallo et al, 2007;Cerra et al, 2008] we showed that VS-1 induces a PI3K-dependent nitric oxide (NO) release by endothelial cells, providing an unifying working hypothesis for explaining at the cellular level both the mechanism of the cardiac inotropic effect of VS-1 and of the vasodilation observed in some vascular preparations [Aardal and Helle, 1992;Angeletti et al, 1994;Brekke et al, 2002]. However, in the absence of a typical high-affinity membrane receptor, the initiating step required for this intracellular cascade remains unrevealed.…”

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confidence: 95%

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Vasostatin 1 activates eNOS in endothelial cells through a proteoglycan‐dependent mechanism

Ramella

Boero

Alloatti

et al. 2010

J of Cellular Biochemistry

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Accumulating evidences point to a significant role for the chromogranin A (CgA)-derived peptide vasostatin 1 (VS-1) in the protective modulation of the cardiovascular activity, because of its ability to counteract the adrenergic signal. We have recently shown that VS-1 induces a PI3K-dependent-nitric oxide (NO) release by endothelial cells, contributing to explain the mechanism of its cardio-suppressive and vasodilator properties. However, the cellular processes upstream the eNOS activation exerted by this peptide are still unknown, as typical high-affinity receptors have not been identified. Here we hypothesize that in endothelial cells VS-1 acts, on the basis of its cationic and amphipathic properties, as a cell penetrating peptide, binding to heparan sulfate proteoglycans (HSPGs) and activating eNOS phosphorylation (Ser1179) through a PI3K-dependent, endocytosis-coupled mechanism. In bovine aortic endothelial cells (BAE-1 cells) endocytotic vesicles trafficking was quantified by confocal microscopy with a water-soluble membrane dye; caveolin 1 (Cav1) shift from plasma membrane was studied by immunofluorescence staining; VS-1-dependent eNOS phosphorylation was assessed by immunofluorescence and immunoblot analysis. Our experiments demonstrate that VS-1 induces a marked increase in the caveolae-dependent endocytosis, (115 +/- 23% endocytotic spots/cell/field in VS-1-treated cells with respect to control cells), that is significantly reduced by both heparinase III (HEP, 17 +/- 15% above control) and Wortmannin (Wm, 7 +/- 22% above control). Heparinase, Wortmannin, and methyl-beta-cyclodextrin (MbetaCD) abolish the VS-1-dependent eNOS phosphorylation (P(Ser1179)eNOS). These results suggest a novel signal transduction pathway for endogenous cationic and amphipathic peptides in endothelial cells: HSPGs interaction and caveolae endocytosis, coupled with a PI3K-dependent eNOS phosphorylation.

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Section: Vs-1 Induces a Pi3k And Proteoglycan-dependent Enos Phosphorsupporting

confidence: 73%

Section: Heparinase and Wortmannin Abolish The Vs-1-dependent Vesiclementioning

confidence: 99%

Section: The Vs-1-induced Endocytosis Involves Caveolin 1 Traffickingmentioning

confidence: 99%

mentioning

confidence: 95%

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Vasostatin 1 activates eNOS in endothelial cells through a proteoglycan‐dependent mechanism

Ramella

Boero

Alloatti

et al. 2010

J of Cellular Biochemistry

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“…In this regard, the electrophysiological and fluorimetric confocal imaging investigations carried out by Gallo and co-workers on rat papillary muscles and bovine aortic endothelial cells (BAE-1) reveal the major involvement of the endothelium-produced NO and of phosphatidylinositol 3-kinase (PI3K) in transducing the cardiac effects of recombinant human VS-1 (hrSTA-CgA 1-76 ) (Gallo et al, 2007). Therefore, the antiadrenergic effect elicited by VS-1 appears mainly due to a PI3K-dependent NO release by endothelial cells, rather than to a direct action on cardiomyocytes (Gallo et al, 2007). These data were further corroborated by a recent study .…”

Section: Action Mechanism(s) Of Vsmentioning

confidence: 99%

Catecholamines, cardiac natriuretic peptides and chromogranin A: evolution and physiopathology of a ‘whip-brake’ system of the endocrine heart

Tota

Cerra

Gattuso

2010

Journal of Experimental Biology

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Summary In the past 50 years, extensive evidence has shown the ability of vertebrate cardiac non-neuronal cells to synthesize and release catecholamines (CA). This formed the mindset behind the search for the intrinsic endocrine heart properties, culminating in 1981 with the discovery of the natriuretic peptides (NP). CA and NP, co-existing in the endocrine secretion granules and acting as major cardiovascular regulators in health and disease, have become of great biomedical relevance for their potent diagnostic and therapeutic use. The concept of the endocrine heart was later enriched by the identification of a growing number of cardiac hormonal substances involved in organ modulation under normal and stress-induced conditions. Recently, chromogranin A (CgA), a major constituent of the secretory granules, and its derived cardio-suppressive and antiadrenergic peptides, vasostatin-1 and catestatin, were shown as new players in this framework, functioning as cardiac counter-regulators in ‘zero steady-state error’ homeostasis, particularly under intense excitatory stimuli, e.g. CA-induced myocardial stress. Here, we present evidence for the hypothesis that is gaining support, particularly among human cardiologists. The actions of CA, NP and CgA, we argue, may be viewed as a hallmark of the cardiac capacity to organize ‘whip-brake’ connection-integration processes in spatio-temporal networks. The involvement of the nitric oxide synthase (NOS)/nitric oxide (NO) system in this configuration is discussed. The use of fish and amphibian paradigms will illustrate the ways that incipient endocrine-humoral agents have evolved as components of cardiac molecular loops and important intermediates during evolutionary transitions, or in a distinct phylogenetic lineage, or under stress challenges. This may help to grasp the old evolutionary roots of these intracardiac endocrine/paracrine networks and how they have evolved from relatively less complicated designs. The latter can also be used as an intellectual tool to disentangle the experimental complexity of the mammalian and human endocrine hearts, suggesting future investigational avenues.

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Overexpression of vasostatin‐1 protects hypoxia/reoxygenation injuries in cardiomyocytes–endothelial cells transwell co‐culture system

Liu

Yang

Shi

et al. 2013

Cell Biology International

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Vasostatin-1 (VS-1) plays important roles in myocardial ischemia/reperfusion injury. We have explored the protective effects of VS-1 on cardiomyocytes using cardiomyocyte-endothelial cells Transwell Co-culture System. Cardiomyocytes and rat aortic endothelial cells (RAECs) were prepared from ventricles and thoraco-abdominal aorta of Sprague-Dawley rats. The experiment used cardiomyocytes alone culture group (C) and cardiomyocytes-RAECs co-culture group (T), each with three subgroups: C-Ad-Null, C-Ad-VS-1, C-Hb (Ad-VS-1 + NO scavenger Hb), or T-Ad-Null, T-Ad-VS-1 transfection, T-Hb. After 48 h incubation, all groups were treated with hypoxia for 60 min and then reoxygenated for 120 min. We also investigated endothelial cells-mediated cardiomyocytes protection. RAECs were treated with hypoxia for 30 min and reoxygenated with normal cardiomyocytes for 120 min. The cardiomyocytes apoptosis rate, aspartate aminotransferase (AST) and creatine kinase isozyme MB (CK-MB) were recorded. As expected, cardiomyocytes apoptosis, AST and CK-MB were significantly increased in the T-Ad-Null group than in the C-Ad-Null group. VS transfection significantly reduced these levels. However, apoptosis, AST and CK-MB levels were increased again after Hb treatment, returning to the similar level of the C-Ad-null group in the C-Hb group, but still significantly lower in the T-Hb group compared with the T-Ad-null group. RAEC injury caused cardiomyocyte injury, and VS-1 transfection of the RAEC decreased apoptosis and the levels of AST and CK-MB. The findings suggest that VS-1 exerts protective effects on the cardiomyocytes directly or indirectly by cardiomyocyte-endothelial cells interaction.

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Endothelium-derived nitric oxide mediates the antiadrenergic effect of human vasostatin-1 in rat ventricular myocardium

Cited by 52 publications

References 27 publications

Vasostatin 1 activates eNOS in endothelial cells through a proteoglycan‐dependent mechanism

Vasostatin 1 activates eNOS in endothelial cells through a proteoglycan‐dependent mechanism

Catecholamines, cardiac natriuretic peptides and chromogranin A: evolution and physiopathology of a ‘whip-brake’ system of the endocrine heart

Overexpression of vasostatin‐1 protects hypoxia/reoxygenation injuries in cardiomyocytes–endothelial cells transwell co‐culture system

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