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1.
001-es BibID:
BIBFORM023026
Első szerző:
Cheng, Caroline
Cím:
Heme Oxygenase 1 Determines Atherosclerotic Lesion Progression Into a Vulnerable Plaque / Cheng, C., Noordeloos, A. M., Jeney, V., Soares, M. P., Moll, F., Pasterkamp, G., Serruys, P. W., Duckers, H. J.
Dátum:
2009
ISSN:
0009-7322
Megjegyzések:
Background-The molecular regulation for the transition from stable to vulnerable plaque remains to be elucidated. Heme oxygenase 1 (HO-1) and its metabolites have been implicated in the cytoprotective defense against oxidative injury in atherogenesis. In this study, we sought to assess the role of HO-1 in the progression toward plaque instability in carotid artery disease in patients and in a murine model of vulnerable plaque development. Methods and Results-Atherectomy biopsy from 112 patients with clinical carotid artery disease was collected and stratified according to characteristics of plaque vulnerability. HO-1 expression correlated closely with features of vulnerable human atheromatous plaque (P<0.005), including macrophage and lipid accumulation, and was inversely correlated with intraplaque vascular smooth muscle cells and collagen deposition. HO-1 expression levels correlated with the plaque destabilizing factors matrix metalloproteinase-9, interleukin-8, and interleukin-6. Likewise, in a vulnerable plaque model using apolipoprotein E(-/-) mice, HO-1 expression was upregulated in vulnerable versus stable lesions. HO-1 induction by cobalt protoporphyrin impeded lesion progression into vulnerable plaques, indicated by a reduction in necrotic core size and intraplaque lipid accumulation, whereas cap thickness and vascular smooth muscle cells were increased. In contrast, inhibition of HO-1 by zinc protoporphyrin augmented plaque vulnerability. Plaque stabilizing was prominent after adenoviral transduction of HO-1 compared with sham virus-treated animals, providing proof that the observed effects on plaque vulnerability were HO-1 specific. Conclusions-Here we demonstrate in a well-defined patient group and a murine vulnerable plaque model that HO-1 induction reverses plaque progression from a vulnerable plaque to a more stable phenotype as part of a compensatory atheroprotective response.
Tárgyszavak:
Orvostudományok
Elméleti orvostudományok
idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:
Circulation. - 119 : 23 (2009), p. 3017-3027. -
További szerzők:
Noordeloos, Annemarie M.
Jeney Viktória (1971-) (vegyész, kémia tanár)
Soares, Miguel P.
Moll, Frans
Pasterkamp, Gerard
Serruys, Patrick W.
Duckers, Henricus J.
Internet cím:
Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:
2.
001-es BibID:
BIBFORM023031
Első szerző:
Jeney Viktória (vegyész, kémia tanár)
Cím:
Role of Antioxidant-1 in Extracellular Superoxide Dismutase Function and Expression / Viktoria Jeney, Shinichi Itoh, Maria Wendt, Quinton Gradek, Masuko Ushio-Fukai, David G. Harrison, Tohru Fukai
Dátum:
2005
ISSN:
0009-7330
Megjegyzések:
The extracellular superoxide dismutase (ecSOD or SOD3) is a copper-containing enzyme which is highly expressed in the vasculature. Copper-containing enzymes require copper chaperones for their activity however the chaperone which delivers copper to SOD3 has not previously been defined. Atox1 is a copper chaperone proposed to deliver copper to the trans-Golgi network. Because SOD3 is secreted via the trans-Golgi network, we sought to determine whether Atox1 acts as a copper chaperone for SOD3. Using recombinant human SOD3, we found that the specific activity of SOD3 directly correlates with its copper content (R-2 = 0.99). SOD3 specific activity in the conditioned medium from cultured Atox1(-/-) fibroblasts was markedly decreased, but could be recovered to that of wild-type cells by copper addition. These results indicated that Atox1 is required for delivering copper to SOD3 for its full activity. Unexpectedly, the protein and mRNA levels of SOD3 were dramatically decreased in cultured Atox1(-/-) fibroblasts. This was associated with a marked decrease in SOD3 transcription rate but no change in SOD3 mRNA stability. Overexpression of Atox1 markedly increased SOD3 mRNA in both Atox1(-/-) and Atox1(-/-) cells. These findings indicate that Atox1 positively regulates SOD3 transcription. Because SOD3 protein is upregulated in atherosclerotic vessels, we examined expression of Atox1 in vessels from ApoE(-/-) mice. Western and immunohistochemical analysis in ApoE(-/-) mice revealed that both Atox1 and SOD3 protein levels are markedly increased in atherosclerotic intimal lesions. In summary, Atox1 functions not only as a copper chaperone for SOD3 but also as a positive regulator for SOD3 transcription and may have an important role in modulating oxidative stress in the cardiovascular system.
Tárgyszavak:
Orvostudományok
Elméleti orvostudományok
idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:
Circulation Research. - 96 : 7 (2005), p. 723-729. -
További szerzők:
Itoh, Shinichi
Wendt, Maria
Gradek, Quinton
Ushio-Fukai, Masuko
Harrison, David G.
Fukai, Tohru
Internet cím:
Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:
3.
001-es BibID:
BIBFORM023034
Első szerző:
Nguyen, Andrew D.
Cím:
Fibulin-5 Is a Novel Binding Protein for Extracellular Superoxide Dismutase / Andrew D. Nguyen, Shinichi Itoh, Viktoria Jeney, Hiromi Yanagisawa, Mitsuaki Fujimoto, Masuko Ushio-Fukai, Tohru Fukai
Dátum:
2004
ISSN:
0009-7330
Megjegyzések:
The extracellular superoxide dismutase (ecSOD) plays an important role in atherosclerosis and endothelial function by modulating levels of the superoxide anion (O-2(.-)) in the extracellular space. Although heparan sulfate proteoglycan is an important ligand for ecSOD, little is known about other biological binding partners of ecSOD. The goal of this study was to identify novel proteins that interact with ecSOD. A yeast two-hybrid screening of a human aorta cDNA library using ecSOD as bait identified fibulin-5 as a predominant binding protein for ecSOD. Further analysis showed that the binding domain of ecSOD within fibulin-5 mapped to its C-terminal domain. In vitro pulldown assays and coimmunoprecipitation analysis further confirmed that ecSOD interacts with fibulin-5 in vitro and in vivo. Studies using fibulin-5(-/-) mice indicated that fibulin-5 is required for binding of ecSOD to vascular tissue. Importantly, the decrease in tissue-bound ecSOD levels in aortas from fibulin-5(-/-) mice was associated with an increase in vascular O-2(.-) levels. Furthermore, immunohistochemical analysis using ApoE(-/-) mice suggested a codistribution of ecSOD and fibulin-5 in atherosclerotic vessels. In summary, we provide in this study the first evidence that the ecSOD-fibulin-5 interaction is required for ecSOD binding to vascular tissues, thereby regulating vascular O-2(.-) levels. This interaction may represent a novel mechanism for controlling vascular redox state in the extracellular space in various cardiovascular diseases such as atherosclerosis and hypertension in which oxidative stress is increased.
Tárgyszavak:
Orvostudományok
Elméleti orvostudományok
idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:
Circulation Research. - 95 : 11 (2004), p. 1067-1074. -
További szerzők:
Itoh, Shinichi
Jeney Viktória (1971-) (vegyész, kémia tanár)
Yanagisawa, Hiromi
Fujimoto, Mitsuaki
Ushio-Fukai, Masuko
Fukai, Tohru
Internet cím:
Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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