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• W2145087663 abstract "HomeArteriosclerosis, Thrombosis, and Vascular BiologyVol. 26, No. 4Mitochondrial Redox Control of Matrix Metalloproteinase Signaling in Resistance Arteries Free AccessEditorialPDF/EPUBAboutView PDFView EPUBSections ToolsAdd to favoritesDownload citationsTrack citationsPermissions ShareShare onFacebookTwitterLinked InMendeleyReddit Jump toFree AccessEditorialPDF/EPUBMitochondrial Redox Control of Matrix Metalloproteinase Signaling in Resistance Arteries Rhian M. Touyz Rhian M. TouyzRhian M. Touyz From the Kidney Research Centre, Ottawa Health Research Institute, University of Ottawa, Ontario, Canada. Search for more papers by this author Originally published1 Apr 2006https://doi.org/10.1161/01.ATV.0000216428.90962.60Arteriosclerosis, Thrombosis, and Vascular Biology. 2006;26:685–688The importance of free radicals in the regulation of vascular tone was recognized in the late 1980s, when endothelium-derived relaxing factor was identified to be NO.1,2 More recently, it has become clear that other free radicals, such as superoxide (O2−), hydrogen peroxide (H2O2), and peroxynitrite (ONOO-) also modulate vascular reactivity.3,4 However, the exact role of reactive oxygen species (ROS) in the regulation of vascular contraction and relaxation remains elusive because vascular effects of free radicals are heterogeneous. Responses may differ depending on the species studied, the vascular bed under investigation, whether the endothelium is intact or denuded, and if studies are conducted in vitro or in vivo.5,6 Furthermore, vascular actions of ROS may be direct or indirect and responses vary depending on the source of the free radicals and their site of compartmentalization.See page 819Superoxide has been implicated both as a vasoconstrictor and as a vasodilator. In cerebral vessels, low concentrations of O2−, generated by NADPH oxidase or xanthine oxidase, induce vasodilation.7 These effects may be mediated directly by activating potassium channels or indirectly through interactions with NO.8 On the other hand, high concentrations of O2− are potent vasoconstrictors, probably induced by ROS-stimulated increase in intracellular free Ca2+ concentration ([Ca2+]i) or by increasing ONOO- production through interactions with NO.9,10 The inactivation of NO by superoxide results in the loss of the vasodilator effect of NO, which, together with the direct contractile actions of ONOO-, leads to vasoconstriction. Similar biphasic dose-dependent responses have been observed in aorta and resistance arteries11,12 and in cultured vascular smooth muscle cells.13H2O2, which is lipid soluble and more stable than O2−, has been considered to be an endothelium-derived hyperpolarizing factor in some vascular beds.14,15 However, H2O2 may function as an endothelium-derived relaxing factor without producing hyperpolarization of underlying vascular muscle.16 Furthermore, in some vessels, H2O2 induces vasoconstriction and actually attenuates vasodilation.17–19 To further highlight the complex nature of ROS in vascular biology, it is now well accepted that ROS function not only as modulators of vascular tone but also as important mediators of vascular growth, inflammation, and fibrosis.20Cellular mechanisms whereby ROS mediate their pleiotropic vascular effects are complex. Multiple signaling pathways stimulated by myriad vasoactive agents, such as angiotensin II (Ang II), endothelin-1, and aldosterone, and numerous redox-sensitive signaling molecules, including mitogen-activated protein kinases, tyrosine kinases, protein tyrosine phosphatases, matrix metalloproteinases (MMPs), and transcription factors, have been implicated.21–24In the present issue of Arteriosclerosis, Thombosis, and Vascular Biology, Hao et al extend our understanding of how G-protein–coupled receptors (GPCRs) modulate redox-sensitive vascular tone, and these authors provide novel mechanistic insights as to how ROS can elicit both vasoconstriction and growth.25 In particular, using α1-adrenergic receptors as a model of GPCR activators, they demonstrate in rat resistance arteries that MMP transactivation of the epidermal growth factor receptor (EGFR) modulates vascular tone and hypertrophy through mitochondrial-derived ROS (Figure). These findings suggest that MMP–ROS signaling may be a common pathway linking apparently unrelated events, which are critically involved in the pathobiology of vascular disease. Download figureDownload PowerPointPutative mechanisms whereby α-adrenoceptors influence vascular responses through mitochondrial-derived ROS. Activation of α-adrenoceptors by phenylephrine transactivates EGFR through MMP-7, which mediates mitochondrial-derived generation of O2−. Mitochondrial ROS spillover into the cytoplasm increases concentrations of intracellular ROS, which influence redox-sensitive signaling events leading to vasoconstriction and vascular growth. Molecular mechanisms by which EGFR mediates activation of mitochondrial enzyme are unclear. ProHB-EGF indicates product of HB-EGF gene; ?, unknown pathway.A link between ROS and MMPs has been identified previously. ROS regulate MMP gene expression and activation of proenzymes. MMP-1, MMP-2, MMP-7, and MMP-9 are activated by ROS through interactions with thiol groups, in which the thiol residue is converted by ROS to sulfinic acid.26,27 Redox-sensitive MMP activation promotes collagen degradation and remodeling of extracellular matrix. MMPs are also critically involved in GPCR-mediated transactivation of growth factor receptors. EGFR transactivation requires MMP-dependent extracellular cleavage of pro–heparin-binding epidermal growth factor (HB-EGF), which liberates a soluble HB-EGF that activates EGFR.28 This “triple membrane-passing signaling” paradigm has been demonstrated for various GPCRs in different cellular backgrounds. In particular, triple membrane-passing signaling is pertinent to Ang II–mediated cell proliferation and growth in cardiac and vascular cells.29 Here we learn that α-adrenoceptors also transactivate EGFR through MMPs, specifically MMP-7, and that this signaling pathway regulates redox-sensitive vascular contraction.25 The exact mechanisms involved in MMP mobilization and HB-EGF liberation are not yet established, but based on the findings of Hao et al,25 they do not seem to involve ROS because ROS scavenging did not influence MMP transactivation. On the other hand, ROS scavenging by l-N-acetylcysteine, superoxide dismutase, manganese (III) tetrakis (4-benzoic acid) porphrin (MnTBAP) (cell-permeable superoxide dismutase mimetic), and diphenylene iodinium inhibited adrenergic-stimulated vasoconstriction. Together, it seems that MMPs are upstream of ROS generation, at least in phenylephrine-induced contraction of rat small mesenteric arteries.What is particularly interesting, and rather unexpected, in the study of Hao et al25 is the finding that agonist-stimulated vascular tone in the vasculature is independent of NAD(P)H oxidase because nonphagocytic NAD(P)H oxidase is generally considered the primary source of ROS in the vascular wall.30 NAD(P)H oxidase is a multisubunit enzyme that is activated by Ang II, aldosterone, growth factors, and stretch and is upregulated in conditions associated with oxidative stress and vascular damage.31,32 NADPH-driven generation of ROS promotes vascular growth, fibrosis, inflammation, and contraction.20,30–32 In the study of Hao,25 using various approaches to inhibit activation of NAD(P)H oxidase, including gp91ds-tat and apocynin, contractile responses to phenylephrine were unaffected, indicating that NAD(P)H oxidase does not contribute significantly to adrenergic-regulated vascular tone. Reasons why α-adrenoceptors do not couple to NAD(P)H oxidase, unlike most GPCRs which do, are unclear.If NAD(P)H oxidase is not responsible for adrenoceptor-mediated vascular ROS formation, what is? The authors provide convincing evidence that mitochondria are critically involved. Mitochondria play a complex multifactorial role in the cell. In addition to their primary function in ATP generation, the organelles sequester Ca2+, and both generate and detoxify ROS. All these functions are intimately interlinked through the central bioenergetic parameter of the proton electrochemical gradient across the inner mitochondrial membrane.33–35 In the study under consideration, pharmacological manipulation of mitochondrial electron transport by rotenone (complex I inhibitor), antimycin A (complex III inhibitor), cyanide (complex IV inhibitor), and oligomycin (complex V ATP synthase inhibitor), as well as the mitochondrial respiratory chain uncoupler carbonylcyanide m-chlorophenylhydrazone, all opposed adrenergic-mediated vasoconstriction, indicating the importance of mitochondria.25 To further support this, a mitochondria-selective ROS scavenger and fluorescent probe, Mito Tracker Red CM-H2XRos, was used to track mitochondrial ROS formation in agonist-stimulated vessels. It is intriguing that inhibition of complexes I, III, IV, and V blocked phenylephrine-induced vascular tone because it is primarily complex I and complex III that normally generate O2−.36,37 Also, because complex IV (cytochrome c oxidase) may act as a peroxidase, which scavenges free radicals,36,37 its role in adrenergic-associated oxidative stress is unclear.There is growing evidence to confirm the findings of Hao et al25 that mitochondria are important sources of vascular ROS. Endothelin-1 promotes oxidative stress through mitochondrial ROS in human vascular smooth muscle cells38 and in deoxycorticosterone acetate–salt hypertension.39 Advanced glycation end-products increase mitochondrial-derived ROS in cultured vascular smooth muscle cells.40 Bailey et al reported that ROS from smooth muscle mitochondria initiate cold-induced constriction of mouse cutaneous arteries by selectively increasing the activity of smooth muscle α2-adrenoceptors.41There are some limitations that should be kept in mind when interpreting the findings of the study by Hao et al.25 First, numerous pharmacological agents were used in whole vessels. In such preparations in which cell type is heterogeneous and in which different species of free radicals localize in different vascular and subcellular compartments, the specificity of pharmacological manipulators used remains questionable. Second, for mitochondrial-derived ROS to be detected in the arterial releasate, as demonstrated in response to phenylephrine, levels of mitochondrial ROS must be very high or mitochondrial antioxidant defense systems must be overwhelmed, indicating possible mitochondrial damage. Third, although the authors demonstrated an association between α-adrenoceptors, MMP-7, EGFR, and mitochondrial ROS-generating systems, the exact molecular mechanisms linking these components is unknown. Furthermore, it remains to be determined how mitochondrial ROS actually influence the contractile machinery in mesenteric arteries.Nevertheless, the study under consideration has important strengths that need to be highlighted. First, the authors identified that in response to phenylephrine, ROS is generated through NAD(P)H oxidase–independent, mitochondrial-dependent enzymes. Others also recently demonstrated the importance of redox-mediated contraction independently of NADPH oxidase.42 Second, it is clearly demonstrated, using small interfering RNA and pharmacological tools, that MMP-7–EGFR transactivation is upstream and not downstream of ROS, as generally accepted. Finally, the study provides new insights into common signaling pathways, which may influence both constriction and growth, important processes in vascular pathology.In recent years, our perception of GPCR modulation of vascular tone by ROS has expanded considerably. We are beginning to appreciate that in addition to regulating vascular growth and inflammation, ROS can influence contraction and dilation and that responses are highly variable depending on the agonist, the vascular bed, and the species generated. However, at present, it is still unclear exactly what the regulatory functions of ROS are with respect to vascular contraction/dilation in physiological conditions, and it is even more confusing and puzzling when attempting to unravel the role of these complex processes in pathological situations. Clearly, future research must focus on the significance of redox-sensitive vascular tone and on the molecular mechanisms whereby ROS regulate vascular contraction/dilation. Thus, the study of Hao et al25 is important because it describes a novel signaling pathway involving MMPs, EGFR, and mitochondria, whereby GPCRs, specifically α1-adrenergic receptors, regulate vascular contraction through ROS. Such findings, together with those of other findings,43,44 contribute to the further understanding of how vasoactive agonists that induce MMP transactivation of the EGFR modulate redox-sensitive vascular tone.FootnotesCorrespondence to Rhian M Touyz, MD, PhD, Canada Research Chair in Hypertension, Ottawa Health Research Institute, University of Ottawa, 451 Smyth Rd, Ottawa, ON, KIH 8M5. E-mail [email protected] References 1 Moncada S, Higgs EA. The discovery of nitric oxide and its role in vascular biology. Br J Pharmacol. 2006; 147: S193–S201.CrossrefMedlineGoogle Scholar2 Furchgott RF, Carvalho MH, Khan MT, Matsunaga K. Evidence for endothelium-dependent vasodilation of resistance vessels by acetylcholine. Blood Vessels. 1987; 24: 145–149.MedlineGoogle Scholar3 Touyz RM. Reactive oxygen species as mediators of calcium signaling by angiotensin II: implications in vascular physiology and pathophysiology. Antioxid Redox Signal. 2005; 7: 1302–1314.CrossrefMedlineGoogle Scholar4 Srivastava P, Rajanikanth M, Raghavan SA, Dikshit M. Role of endogenous reactive oxygen derived species and cyclooxygenase mediators in 5-hydroxytryptamine-induced contractions in rat aorta: relationship to nitric oxide. Pharmacol Res. 2002; 45: 375–382.CrossrefMedlineGoogle Scholar5 Yang D, Feletou M, Boulanger CM, Wu HF, Levens N, Zhang JN, Vanhoutte PM. Oxygen-derived free radicals mediate endothelium-dependent contractions to acetylcholine in aortas from spontaneously hypertensive rats. Br J Pharmacol. 2002; 136: 104–110.CrossrefMedlineGoogle Scholar6 Fujimoto S, Asano T, Sakai M, Sakurai K, Takagi D, Yoshimoto N, Itoh T. Mechanisms of hydrogen peroxide-induced relaxation in rabbit mesenteric small artery. Eur J Pharmacol. 2001; 412: 291–300.CrossrefMedlineGoogle Scholar7 Faraci FM. Reactive oxygen species: influence on cerebral vascular tone. J Appl Physiol. 2006; 100: 739–743.CrossrefMedlineGoogle Scholar8 Ohashi M, Faraci F, Heistad D. Peroxynitrite hyperpolarizes smooth muscle and relaxes internal carotid artery in rabbit via ATP-sensitive K+ channels. Am J Physiol Heart Circ Physiol. 2005; 289: H2244–H2250.CrossrefMedlineGoogle Scholar9 Wang D, Chabrashvili T, Wilcox CS. Enhanced contractility of renal afferent arterioles from angiotensin-infused rabbits: roles of oxidative stress, thromboxane prostanoid receptors, and endothelium. Circ Res. 2004; 94: 1436–1442.LinkGoogle Scholar10 Belik J, Jankov RP, Pan J, Tanswell AK. Peroxynitrite inhibits relaxation and induces pulmonary artery muscle contraction in the newborn rat. Free Radic Biol Med. 2004; 37: 1384–1392.CrossrefMedlineGoogle Scholar11 Gao YJ, Hirota S, Zhang DW, Janssen LJ, Lee RM. Mechanisms of hydrogen-peroxide-induced biphasic response in rat mesenteric artery. Br J Pharmacol. 2003; 138: 1085–1092.CrossrefMedlineGoogle Scholar12 Ghosh M, Wang HD, McNeill JR. Role of oxidative stress and nitric oxide in regulation of spontaneous tone in aorta of DOCA-salt hypertensive rats. Br J Pharmacol. 2004; 141: 562–573.CrossrefMedlineGoogle Scholar13 Tabet F, Savoia C, Schiffrin EL, Touyz RM. Differential calcium regulation by hydrogen peroxide and superoxide in vascular smooth muscle cells from spontaneously hypertensive rats. J Cardiovasc Pharmacol. 2004; 44: 200–208.CrossrefMedlineGoogle Scholar14 Shimokawa H, Matoba T. Hydrogen peroxide as an endothelium-derived hyperpolarizing factor. Pharmacol Res. 2004; 49: 543–549.CrossrefMedlineGoogle Scholar15 Matoba T, Shimokawa H. Hydrogen peroxide is an endothelium-derived hyperpolarizing factor in animals and humans. J Pharmacol Sci. 2003; 92: 1–6.CrossrefMedlineGoogle Scholar16 Cai H. Hydrogen peroxide regulation of endothelial function: origins, mechanisms, and consequences. Cardiovasc Res. 2005; 68: 26–36.CrossrefMedlineGoogle Scholar17 Gao YJ, Lee RM. Hydrogen peroxide induces a greater contraction in mesenteric arteries of spontaneously hypertensive rats through thromboxane A(2) production. Br J Pharmacol. 2001; 134: 1639–1646.CrossrefMedlineGoogle Scholar18 Suvorava T, Lauer N, Kumpf S, Jacob R, Meyer W, Kojda G. Endogenous vascular hydrogen peroxide regulates arteriolar tension in vivo. Circulation. 2005; 112: 2487–2495.LinkGoogle Scholar19 Lucchesi PA, Belmadani S, Matrougui K. Hydrogen peroxide acts as both vasodilator and vasoconstrictor in the control of perfused mouse mesenteric resistance arteries. J Hypertens. 2005; 23: 571–579.CrossrefMedlineGoogle Scholar20 Touyz RM, Schiffrin EL. Reactive oxygen species in vascular biology: implications in hypertension. Histochem Cell Biol. 2004; 122: 339–352.CrossrefMedlineGoogle Scholar21 Wolin MS, Ahmad M, Gupte SA. Oxidant and redox signaling in vascular oxygen sensing mechanisms: basic concepts, current controversies, and potential importance of cytosolic NADPH. 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Vascular responses to {alpha}1-adrenergic receptors in small rat mesenteric arteries depend on mitochondrial reactive oxygen species. Arterioscler Thromb Vasc Biol. 2006; 26: 819–825.LinkGoogle Scholar26 Nelson KK, Melendez JA. Mitochondrial redox control of matrix metalloproteinases. Free Radic Biol Med. 2004; 37: 768–784.CrossrefMedlineGoogle Scholar27 Smith NJ, Chan H-W, Osborne JE, Thomas WG. What’s new in the renin-angiotensin system? Hijacking epidermal growth factor receptors by angiotensin II: new possibilities for understanding and treating cardiac hypertrophy. Cell Mol Life Sci. 2004; 61: 2695–2703.CrossrefMedlineGoogle Scholar28 Cheng-Hsien C, Yung-Ho H, Yuh-Mou S, Chun-Cheng H, Horng-Mo L, Huei-Mei H, Tso-Hsiao C. Src homology 2-containing phosphotyrosine phosphatase regulates endothelin-1-induced epidermal growth factor receptor transactivation in rat renal tubular cell NRK-52E. Pflugers Arch. 2005; 28: 1–9.Google Scholar29 Daub H, Weiss FU, Wallasch C, Ullrich A. Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors. Nature. 1996; 379: 557–560.CrossrefMedlineGoogle Scholar30 Lassegue B, Clempus RE. Vascular NAD(P)H oxidases: specific features, expression, and regulation. Am J Physiol Regul Integr Comp Physiol. 2003; 285: R277–R297.CrossrefMedlineGoogle Scholar31 Cai H, Griendling KK, Harrison DG. The vascular NAD(P)H oxidases as therapeutic targets in cardiovascular diseases. Trends Pharmacol Sci. 2003; 24: 471–478.CrossrefMedlineGoogle Scholar32 Guzik TJ, Sadowski J, Guzik B, Jopek A, Kapelak B, Przybylowski P, Wierzbicki K, Korbut R, Harrison DG, Channon KM. Coronary artery superoxide production and nox isoform expression in human coronary artery disease. Arterioscler Thromb Vasc Biol. 2006; 26: 333–339.LinkGoogle Scholar33 Brand MD, Affourtit C, Esteves TC, Green K, Lambert AJ, Miwa S, Pakay JL, Parker N. Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins. Free Radic Biol Med. 2004; 37: 755–767.CrossrefMedlineGoogle Scholar34 Xi Q, Cheranov SY, Jaggar JH. Mitochondria-derived reactive oxygen species dilate cerebral arteries by activating Ca2+ sparks. Circ Res. 2005; 97: 354–362.LinkGoogle Scholar35 Turrens JF. Mitochondrial formation of reactive oxygen species. J Physiol. 2003; 552: 335–244.CrossrefMedlineGoogle Scholar36 Hannan RD. Jezek P, Hlavata L. Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism. Int J Biochem Cell Biol. 2005; 37: 2478–2503.CrossrefMedlineGoogle Scholar37 Orii Y. The cytochrome c peroxidase activity of cytochrome oxidase. J Biol Chem. 1982; 257: 9246–9248.CrossrefMedlineGoogle Scholar38 Touyz RM, Yao G, Viel E, Amiri F, Schiffrin EL. Angiotensin II and endothelin-1 regulate MAP kinases through different redox-dependent mechanisms in human vascular smooth muscle cells. J Hypertens. 2004; 22: 1141–1149.CrossrefMedlineGoogle Scholar39 Callera GE, Tostes RC, Yogi A, Montezano AC, Touyz RM. Endothelin-1-induced oxidative stress in DOCA-salt hypertension involves NADPH-oxidase-independent mechanisms. Clin Sci (Lond). 2006; 110: 243–253.CrossrefMedlineGoogle Scholar40 Basta G, Lazzerini G, Del Turco S, Ratto GM, Schmidt AM, De Caterina R. At least 2 distinct pathways generating reactive oxygen species mediate vascular cell adhesion molecule-1 induction by advanced glycation end products. Arterioscler Thromb Vasc Biol. 2005; 25: 1401–1407.LinkGoogle Scholar41 Bailey SR, Mitra S, Flavahan S, Flavahan NA. Reactive oxygen species from smooth muscle mitochondria initiate cold-induced constriction of cutaneous arteries. Am J Physiol Heart Circ Physiol. 2005; 289: H243–H250.CrossrefMedlineGoogle Scholar42 Judkins CP, Sobey CG, Dang TT, Miller AA, Dusting GJ, Drummond GR. NADPH-induced contractions of mouse aorta do not involve NADPH oxidase: a role for P2X receptors. J Pharmacol Exp Ther. 2006;Jan 11;[Epub ahead of print].Google Scholar43 Chen CH, Cheng TH, Lin H, Shih NL, Chen YL, Chen YS, Cheng CF, Lian WS, Meng TC, Chiu WT, Chen JJ. Reactive oxygen species generation is involved in epidermal growth factor receptor transactivation through the transient oxidization of SHP-2 in endothelin-1 signaling pathway in rat cardiac fibroblasts. Mol Pharmacol. 2006;Jan 3;[Epub ahead of print].Google Scholar44 Shah BH, Shah FB, Catt KJ. Role of metalloproteinase-dependent EGF receptor activation in alpha-adrenoceptor-stimulated MAP kinase phosphorylation in GT1–7 neurons. 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Fernandez-Patron C (2007) Therapeutic potential of the epidermal growth factor receptor transactivation in hypertension: a convergent signaling pathway of vascular tone, oxidative stress, and hypertrophic growth downstream of vasoactive G-protein-coupled receptors?This paper is one of a selection of papers published in this Special Issue, entitled Young Investigators' Forum., Canadian Journal of Physiology and Pharmacology, 10.1139/y06-097, 85:1, (97-104), Online publication date: 1-Jan-2007. April 2006Vol 26, Issue 4 Advertisement Article InformationMetrics https://doi.org/10.1161/01.ATV.0000216428.90962.60PMID: 16556862 Originally publishedApril 1, 2006 Keywordsadrenergic receptorstransactivationreactive oxygen speciesepidermal growth factor receptorvascular tonesignal transductionPDF download Advertisement" @default.
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• W2145087663 title "Mitochondrial Redox Control of Matrix Metalloproteinase Signaling in Resistance Arteries" @default.
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