Induction of the antioxidant stress proteins heme oxygenase‐1 and MSP23 by stress agents and oxidised LDL in cultured vascular smooth muscle cells

Siow, Richard; Ishii, Tetsuro; Sato, Hiroki; Taketani, Shigeru; Leake, David S.; Sweiry, J H; Pearson, Jeremy D.; Bannai, Shiro; Mann, Giovanni E.

doi:10.1016/0014-5793(95)00650-x

Cited by 86 publications

(45 citation statements)

References 26 publications

(26 reference statements)

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“…This induction was dose dependent, and mRNA continued to accumulate for at least 48 h. Since coculture cells can further oxidize LDL during the incubation, newly formed oxidized LDL may evoke the HO-1 gene response continuously (32,33). A study of HO-1 expression in response to copper-oxidized LDL yielded similar results in porcine aortic smooth muscle cell cultures (38,39). In this study, we observed that this induction also occurred in monolayers of HAEC and HASMC cultured separately (Fig.…”

Section: Discussionmentioning

confidence: 74%

“…In contrast, the mechanisms of endogenous prevention of LDL oxidation other than those related to HDL, or exogenous antioxidants like probucol (36) or ␣ -tocopherol (37) are not generally well understood. It was recently reported using in vitro studies that oxidized LDL triggers expression of HO-1, heat shock protein 70 (HSP 70), macrophage stress protein 23 (MSP23), and a 150-kD oxygen-regulated protein (ORP150) as stress proteins in vascular endothelial cells, vascular smooth muscle cells, macrophages, and renal tubular epithelial cells (38)(39)(40)(41). However, the functions of these stress proteins are unknown.…”

Section: Introductionmentioning

confidence: 99%

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Induction of heme oxygenase-1 inhibits the monocyte transmigration induced by mildly oxidized LDL.

Ishikawa¹,

Navab²,

Leitinger³

et al. 1997

J. Clin. Invest.

273

188

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Heme catabolic processes produce the antioxidants biliverdin and bilirubin, as well as the potent prooxidant free iron. Since these products have opposing effects on oxidative stress, it is not clear whether heme catabolism promotes or inhibits inflammatory processes, including atherosclerotic lesion formation. Heme oxygenase (HO) catalyzes the rate-limiting step of heme catabolism. We used cocultures of human aortic endothelial cells and smooth muscle cells to examine the possible role of HO in early atherosclerosis. Heme oxygenase-1 (HO-1), the inducible isoform of HO, was highly induced by mildly oxidized LDL, and augmented induction was observed with hemin pretreatment. This augmented HO-1 induction resulted in the reduction of monocyte chemotaxis in response to LDL oxidation. Conversely, inhibition of HO by a specific inhibitor, Sn-protoporphyrin IX, enhanced chemotaxis. Furthermore, pretreatment with biliverdin or bilirubin, the products of HO, reduced chemotaxis. Oxidized phospholipids in the mildly oxidized LDL appear to be responsible for HO-1 induction, since oxidized but not native arachidonic acid-containing phospholipids also induced HO-1. These results suggest that HO-1 induced by mildly oxidized LDL may protect against the induction of inflammatory responses in artery wall cells through the production of the antioxidants biliverdin and bilirubin. ( J. Clin. Invest. 1997.

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Section: Discussionmentioning

confidence: 74%

Section: Introductionmentioning

confidence: 99%

Induction of heme oxygenase-1 inhibits the monocyte transmigration induced by mildly oxidized LDL.

Ishikawa¹,

Navab²,

Leitinger³

et al. 1997

J. Clin. Invest.

273

188

View full text Add to dashboard Cite

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“…The gene with the greatest level of increase in response to oxLDL was heme oxygenase 1 (HMOX1) ( Table 4). Several lines of evidence suggest that HMOX1 expression can be increased several fold by stimuli that induce cellular oxidative stress, including oxidized LDL (29,30). HMOX1 induction is known to lead to an increase in catalytic free iron release.…”

Section: Genes Uniquely Regulated By Ox-ldlmentioning

confidence: 99%

Oxidized LDL immune complexes and oxidized LDL differentially affect the expression of genes involved with inflammation and survival in human U937 monocytic cells

et al. 2009

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Objective-To compare the global effects of oxidized LDL (oxLDL) and oxLDL-containing immune complexes (oxLDL-IC) on gene expression in human monocytic cells and to identify differentially expressed genes involved with inflammation and survival.Methods and Results-U937 cells were treated with oxLDL-IC, oxLDL, Keyhole limpet hemocyanin immune complexes (KLH-IC), or vehicle for 4 h. Transcriptome profiling was performed using DNA microarrays. oxLDL-IC uniquely affected the expression of genes involved with pro-survival (RAD54B, RUFY3, SNRPB2, and ZBTB24). oxLDL-IC also regulated many genes in a manner similar to KLH-IC. Functional categorization of these genes revealed that 39% are involved with stress responses, including the unfolded protein response which impacts cell survival, 19% with regulation of transcription, 10% with endocytosis and intracellular transport of protein and lipid, and 16% with inflammatory responses including regulation of I-κB/NF-κB cascade and cytokine activity. One gene in particular, HSP70 6, greatly up-regulated by ox-LDL-IC, was found to be required for the process by which oxLDL-IC augments IL1-β secretion. The study also revealed genes uniquely up-regulated by oxLDL including genes involved with growth inhibition (OKL38, NEK3, and FTH1), oxidoreductase activity (SPXN1 and HMOX1), and transport of amino acids and fatty acids (SLC7A11 and ADFP).Conclusions-These findings highlight early transcriptional responses elicited by oxLDL-IC that may underlie its cytoprotective and pro-inflammatory effects. Cross-linking of Fcγ receptors appears to be the trigger for most of the transcriptional responses to oxLDL-IC. The findings further strengthen the hypothesis that oxLDL and oxLDL-IC elicit disparate inflammatory responses and play distinct roles in the process of atherosclerosis.

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“…Prx I is a physiological inhibitor of cAbl kinase activity [34]. It is induced by oxidative stress in peritoneal macrophages exposed to heavy metals, oxidized low-density lipoproteins or heme [30,35,36,37].…”

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confidence: 99%

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

et al. 2002

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Aims/hypothesis. Insulin-producing beta cells are destroyed by oxidative and nitrosative stress during the pathogenesis of Type I (insulin-dependent) diabetes mellitus. These cells are more sensitive than others due to their deficiency of well known antioxidant enzymes like superoxide dismutase, glutathione peroxidase and catalase. However the peroxiredoxins discovered in the past decade form a large family of highly conserved thioredoxin-dependent peroxide reductases, which are present in most tissues. We investigated whether peroxiredoxins I and II are present in pancreatic beta cells and if they are inducible by oxidative and nitrosative stress. Methods. To detect these enzymes in insulin-producing beta cells we used semiquantitative RT-PCR, western blots and immunohistochemistry. The expression of peroxiredoxins I and II was analysed after treatment with cytokines, hydrogen peroxide, alloxan or streptozotocin in the rat insulinoma cells INS-1 using RT-PCR and western blots. Results. We show that peroxiredoxins I and II are present in the cytoplasm of pancreatic islet cells as well as in insulinoma cell lines βTC6-F7 and INS-1. Peroxiredoxins I and II were up-regulated by all stress agents used. Conclusion/interpretation. Beta cells, undersupplied with well characterized antioxidant enzymes, possess an additional antioxidant system which is inducible by oxidative as well as nitrosative stress. [Diabetologia (2002) 45:867-876]

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Induction of the antioxidant stress proteins heme oxygenase‐1 and MSP23 by stress agents and oxidised LDL in cultured vascular smooth muscle cells

Cited by 86 publications

References 26 publications

Induction of heme oxygenase-1 inhibits the monocyte transmigration induced by mildly oxidized LDL.

Induction of heme oxygenase-1 inhibits the monocyte transmigration induced by mildly oxidized LDL.

Oxidized LDL immune complexes and oxidized LDL differentially affect the expression of genes involved with inflammation and survival in human U937 monocytic cells

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

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