Identification of oxidative stress‐regulated genes in rat aortic smooth muscle cells by suppression subtractive hybridization

Sakamoto, Kenya; Yamasaki, Yoshimitsu; Kaneto, Hideaki; Fujitani, Yoshio; Matsuoka, Taka‐aki; Yoshioka, Ryo; Tagawa, Tomoko; Matsuhisa, Munehide; Kajimoto, Yoshitaka; Hori, Masatsugu

doi:10.1016/s0014-5793(99)01419-2

Cited by 18 publications

(18 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Based on the excess of free ROS observed after glucose normalisation and the ability of different mechanisms to inhibit ROS and interrupt aspects of the persistence of high glucose stress, an excess of intracellular ROS in target cells is a likely candidate. In addition, although the particular regulatory mechanisms of the high glucose stress markers assessed in this paper differ, all of these markers are directly or indirectly induced by ROS [34,[37][38][39][40][41][42], again implicating an excess of cellular ROS in the 'memory' phenomenon. Interestingly, ALA and in particular overexpression of UCP2 were able to reduce the 'memory' effect for all the studied parameters, suggesting that persistent mitochondrial generation of ROS plays a key role in producing this phenomenon.…”

Section: Discussionmentioning

confidence: 99%

Reactive oxygen species mediate a cellular ‘memory’ of high glucose stress signalling

et al. 2007

View full text Add to dashboard Cite

Aims/hypothesis A long-term 'memory' of hyperglycaemic stress, even when glycaemia is normalised, has been previously reported in endothelial cells. In this report we sought to duplicate and extend this finding. Materials and methods HUVECs and ARPE-19 retinal cells were incubated in 5 or in 30 mmol/l glucose for 3 weeks or subjected to 1 week of normal glucose after being exposed for 2 weeks to continuous high glucose. HUVECs were also treated in this last condition with several antioxidants. Similarly, four groups of rats were studied for 3 weeks: (1) normal rats; (2) diabetic rats not treated with insulin; (3) diabetic rats treated with insulin during the last week; and (4) diabetic rats treated with insulin plus α-lipoic acid in the last week. Results In human endothelial cells and ARPE-19 retinal cells in culture, as well as in the retina of diabetic rats, levels of the following markers of high glucose stress remained induced for 1 week after levels of glucose had normalised: protein kinase C-β, NAD(P)H oxidase subunit p47phox, BCL-2-associated X protein, 3-nitrotyrosine, fibronectin, poly(ADPribose) Blockade of reactive species using different approaches, i.e. the mitochondrial antioxidant α-lipoic acid, overexpression of uncoupling protein 2, oxypurinol, apocynin and the poly(ADP-ribose) polymerase inhibitor PJ34, interrupted the induction both of high glucose stress markers and of the fluorescent reactive oxygen species (ROS) probe CM-H 2 DCFDA in human endothelial cells. Similar results were obtained in the retina of diabetic rats with α-lipoic acid added to the last week of normalised glucose. Conclusions/interpretation These results provide proofof-principle of a ROS-mediated cellular persistence of vascular stress after glucose normalisation.

show abstract

Section: Discussionmentioning

confidence: 99%

Reactive oxygen species mediate a cellular ‘memory’ of high glucose stress signalling

et al. 2007

View full text Add to dashboard Cite

show abstract

“…Homologues of p100 protein exist in a number of species, and these have been implicated in a variety of physiological processes. Human p100 in HeLa cells has been implicated in Epstein-Barr virus-host cell interaction (Tong et al 1995), a p100 homologue in the fungus Histoplasma capsulatum has been implicated in infection of macrophages (Porta et al 1999), and a rat homologue is increased in vascular smooth muscle cells in response to oxidative stress (Sakamoto et al 1999). In addition, the p100 interaction with c-myb raises the possibility that it is involved in growth and differentiation (Leverson et al 1998) and p100 has recently been associated with milk lipid transport and secretion (Keenan et al 2000).…”

Section: Discussionmentioning

confidence: 99%

“…Pim-1 has been shown to phosphorylate p100 in vitro (Leverson et al 1998). The cDNA nucleotide and amino acid sequences have been reported for human p100 (Tong et al 1995) as well as homologues in rat (Sakamoto et al 1999) and a fungal pathogen, Histoplasma capsulatum (Porta et al 1999). In the latter two species, p100 was identified by differential expression in rat aorta smooth muscle cells in response to oxidative stress, and in the fungal cells during infection of murine macrophages.…”

Section: Introductionmentioning

confidence: 99%

The p100 coactivator is present in the nuclei of mammary epithelial cells and its abundance is increased in response to prolactin in culture and in mammary tissue during lactation

Broadhurst¹,

Wheeler²

2001

Journal of Endocrinology

View full text Add to dashboard Cite

The p100 coactivator, first identified as a coactivator of the Epstein-Barr virus-encoded transcription factor, EBNA-2, in cultured cells, interacts with a number of transcription factors. However, the role of p100 in animals is unclear. We found that the abundance of p100 is closely associated with the lactating state in mammary tissue of mice and cows. Using two antibodies against independent parts of the protein, p100 immunoreactivity was localised to mammary epithelial cells, and was enriched in both nuclei and endoplasmic reticulum/organelle fractions. Stimulation of -casein expression in cultured mammary epithelial cells was associated with an increase in abundance of the p100 protein. The relative abundance of p100 mRNA was not altered in mammary tissue throughout the gestationlactation cycle, indicating that the abundance of p100 is altered by a post-transcriptional mechanism. Further work is required to clarify the function of p100 in mammary epithelial cells.

show abstract

“…Both the function and the subcellular location of SND1 protein family members have been studied from very different points of view. Initially, p100 was described as a transcriptional coactivator [33], but further studies detected p100 in a wide variety of tissues and related it to a variety of physiologic events, such as artery injuries connected to oxidative stress [29] and milk precursory lipid droplets in the mammary gland [15].…”

Section: Introductionmentioning

confidence: 99%

Association of SND1 protein to low density lipid droplets in liver steatosis

et al. 2010

View full text Add to dashboard Cite

Although the human homologue of SND p102, p100 coactivator, was initially described as a nuclear protein, the p100 coactivator protein family members have non-nuclear localization in mammalian cells with active lipid handling, storage, and secretion. However, their role in lipid homeostasis remains unresolved. Here, we investigate the distribution of the rat homologue SND p102 (also called SND1) and its association with newly formed lipid droplets in the liver parenchyma and cultured hepatocytes. Sucrose gradient fractionation showed that SND p102 cofractionated with endoplasmic reticulum and Golgi markers. Such cofractionation was not altered in regenerating steatotic rat liver. However, SND p102 was also detected in lipid droplets from regenerating liver, showing a specific directionalization to the least dense ones. Confocal microscopy of cultured hepatocytes confirmed the findings of gradient fractionation. In addition, p100 coactivator was consistently encountered in microsomes and lipid droplets in control and oleate-treated HepG2 cells. The total amount of SND p102 in hepatocytes was similar in both conditions, suggesting a specific translocation of the protein. Our findings indicate that SND p102 and the human p100 coactivator have a ubiquitous cytoplasmic distribution in hepatocytes and that steatogenic conditions promote the targeting of SND p102 from other cell compartments to specific low density lipid droplets.

show abstract

Identification of oxidative stress‐regulated genes in rat aortic smooth muscle cells by suppression subtractive hybridization

Cited by 18 publications

References 34 publications

Reactive oxygen species mediate a cellular ‘memory’ of high glucose stress signalling

Reactive oxygen species mediate a cellular ‘memory’ of high glucose stress signalling

The p100 coactivator is present in the nuclei of mammary epithelial cells and its abundance is increased in response to prolactin in culture and in mammary tissue during lactation

Association of SND1 protein to low density lipid droplets in liver steatosis

Contact Info

Product

Resources

About