Expression of transcriptional repressor ATF3/LRF1 in human atherosclerosis: colocalization and possible involvement in cell death of vascular endothelial cells

Nawa, Tigre; Nawa, Makiko; Adachi, Mio; Uchimura, Isao; Shimokawa, Reiko; Fujisawa, Kazuhiko; Tanaka, Akira; Numano, Fujío; Kitajima, Shigetaka

doi:10.1016/s0021-9150(01)00639-6

Cited by 71 publications

(58 citation statements)

References 31 publications

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“…In contrast, some works demonstrated that ATF3 is anti-apoptotic gene [26,39,40]. Recently, researchers concurred that ATF3 can play both pro-apoptotic and cell survival role depending on the type of stimulation and cell context [21,26,32,36,39]. In our study, there were shown the cell hypertrophy of FIR-sensitive cell lines without apoptosis.…”

Section: Discussioncontrasting

confidence: 55%

“…and protein was peaked at 1 h and 2 h after Doxorubicin treatment in cardiac myocytes [39], ATF3 mRNA is rapidly increased in 30 min after TNF-α stimulation in HUVECs and ATF3 protein was also induced with maximum accumulation in 4 h and involved TNF-α induced HUVECs apoptosis in atherosclerotic region [26,39]. Kawauchi et al, reported that the level of ATF3 increased within 4 h after TNF-α stimulation in HUVECs and protected HUVECs from TNF-α inducible cell death by down-regulating the activity of pro-apoptotic gene p53 [40], ATF3 is induced in ovarian cancer cell lines by progesterone after 4 h of culture [31], the increase in ATF3 mRNA was evident in the earliest time point 4h and was maintained through 24 hours of curcumin treatment in some human cancer cell lines [32].…”

Section: Discussionmentioning

confidence: 95%

“…ATF3 mRNA and protein levels are relatively lower in most normal an 5, 21,22]. ATF3 appears to participate in the JNK/ SAPK and IFN-PKR pathway [23,24] and activated by many variant of stimulation including cytokines, genotoxic agents, growth factors such as fibroblast growth factor, epidermal growth factor and hepatocyte growth factor, pro-apoptotic stimuli such as lypopolysaccharide, oxidative stress and compounds with antitumorigenic activities such as the phosphatidylinositol 3-kinase inhibitor LY294002, nonsteroidal antiinflammatory drugs, progesterone and dietary polyphenols as a curcumin from the tumeric plant and catechins in green tea [16,20,21,25,26,[27][28][29][30][31][32][33]. ATF3 also might be involved in homeostasis, wound healing, regenerating liver, cell adhesion, cancer cell invasion and apoptosis [21,22,[34][35][36][37][38].…”

Section: Discussionmentioning

confidence: 99%

“…Then e propound the hypothesis, that ATF3 as a transcriptional repressor under the continuous expression can inhibit the activity of pro-apoptotic genes such a p53, etc [40] although many studies have shown ATF3 is proapoptotic gene [32,36]. In contrast, some works demonstrated that ATF3 is anti-apoptotic gene [26,39,40]. Recently, researchers concurred that ATF3 can play both pro-apoptotic and cell survival role depending on the type of stimulation and cell context [21,26,32,36,39].…”

Section: Discussionmentioning

confidence: 99%

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Far Infrared Ray Radiation Inhibits the Proliferation of A549, HSC3 and Sa3 Cancer Cells through Enhancing the Expression of ATF3 Gene

Yamashita¹,

Dalkhsuren²,

Ishikawa³

et al. 2010

JEMAA

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Far-infrared ray (FIR) is electromagnetic wave between 4 and 1000 μm. FIR causes heating, but how it affects cells is not well understood. In this study, we developed a culture incubator that can continuously irradiate cells with FIR and examined the effects of FIR on five human cancer cell lines, namely A431 (vulva), A549 (lung), HSC3 (tongue), MCF7 (breast) and Sa3 (gingiva). We found that FIR inhibits cell proliferation and induces cell hypertrophy without apoptosis in A549, HSC3 and Sa3 cells. Flow cytometry revealed that the inhibition of proliferation was due to G2/M arrest. Contrary, FIR did not inhibit cell proliferation and cause cell hypertrophy in A431 or MCF7 cells. Microarray analysis revealed that FIR suppressed the expression of cell proliferation-related and stress-responsive genes in FIR-

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Section: Discussioncontrasting

confidence: 55%

Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Far Infrared Ray Radiation Inhibits the Proliferation of A549, HSC3 and Sa3 Cancer Cells through Enhancing the Expression of ATF3 Gene

Yamashita¹,

Dalkhsuren²,

Ishikawa³

et al. 2010

JEMAA

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“…Other target genes for ATF3 repression include gadd153/Chop10, a transcription factor that mediates effects of stress (Wang and Ron, 1996;Wolfgang et al, 1997), and E-selectin, an adhesion receptor activated by TNFα (Nawa et al, 2000). However, the function of ATF3 is still not established: ATF3 is reported to both inhibit Zhang et al, 2002) and promote (Nawa et al, 2002) p53-dependent apoptosis. ATF3 has also been reported to promote adhesion on collagen (Ishiguro et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Wounding activates p38 map kinase and activation transcription factor 3 in leading keratinocytes

Harper

Alvares

Carter

2005

Journal of Cell Science

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Quiescent epidermis anchors to laminin 5 in the basement membrane via integrin α6β4. Wounding elevates expression of laminin 5, generating leading keratinocytes (LKs) that migrate via β1 integrins. Laminin 5 was evaluated as a regulator of cell signaling, and mRNA and protein expression in LKs. An in vitro wound model was developed based on suspension and re-adhesion of quiescent human keratinocytes (HKs). DNA microarrays identified multiple mRNAs elevated 1.5 hours after suspension and re-adhesion including activation transcription factor 3 (ATF3). In vitro and in vivo, levels of ATF3 protein elevate in nuclei of LKs, but not in nuclei of the following cells, 2 hours after suspension or wounding but decline by 12-18 hours post injury. Significantly, null defects in laminin 5 or integrin β4 that inhibit anchorage chronically elevate ATF3 in vivo. This suggests that adhesion to laminin 5, but not other ligands, suppresses activation. On suspension, ATF3 and other transcripts in the microarrays are elevated by phosphorylated p38 mitogen-activated protein kinase (P-p38), a stress kinase that regulates mRNA and cell motility. Inhibition of P-p38 with SB203580 prevents phosphorylation of ATF2, a transcription factor for ATF3 in LKs. Re-adhesion to laminin 5 via α6β4 dephosphorylates P-p38 and suppresses ATF3 protein relative to cells in suspension. Thus, wounding of quiescent HKs disrupts laminin 5 adhesion to activate p38, generating mRNA transcripts that define LKs. Adhesion to deposits of laminin 5 via α6β4 suppresses P-p38 and activation mRNAs including ATF3. Defects in laminin 5 and α6β4 sustain P-p38 with probable pathological effects on transcription and migration. Journal of Cell Science 3472 of polarized lamellipodium in epithelial cells through activation of Rac1 (Choma et al., 2004). This sequence of adhesion and signaling changes allows HKs to make the transition from quiescence to activation in wounds. Similarly, ligation of α3β1 in A549 adenocarcinoma cells by laminin 10/11 or laminin 5 preferentially activates the Rac-MKK-JNK/p38 stress pathway that mediates epithelial migration (Gu et al., 2001;Ono and Han, 2000;Xia and Karin, 2004). In addition to adhesion, interaction of cells with integrin ligands also regulates mRNA transcription and protein translation through activation of p38 MAPK (Balda and Matter, 2003). Ligation of α6β4 activates the Rac-PAK-MKK-p38 pathway to promote expression of IL-6 in thymic epithelial cells (Mainiero et al., 2003). Thus, cell suspension and re-adhesion onto dermal collagen or laminin 5 via integrins activates JNK and/or p38 by phosphorylation to alter protein expression and/or cell motility (Clark et al., 2003;Ono and Han, 2000). Here, we sought to: (1) identify changes in mRNA transcription and protein translation in quiescent keratinocytes as they transition into wound LKs; (2) identify cell signals necessary for the transcriptional changes in LKs; (3) understand the role of laminin 5 adhesion in regulating the signaling and transcriptional changes. We found that sus...

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Activating transcription factor 3 regulates survivability and migration of vascular smooth muscle cells

Meng

Zou

et al. 2011

IUBMB Life

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SummaryActivating transcription factor 3 (ATF3) is a member of the ATF/CREB (CAMP responsive element binding protein) family of transcription factors. The expression and the function of ATF3 in vascular smooth muscle cells (VSMCs) remain unknown. The aim of this work is to determine the expression and possible function of ATF3 in VSMCs. We found that VSMCs expressed ATF3, and expression of ATF3 in VSMCs was induced by a variety of stimuli including serum, angiotensin II, and H 2 O 2 . Knockdown of ATF3 induced apoptosis of VSMCs, caspase-3 cleavage, and cytochrome c release. The results suggest that ATF3 regulates survivability of VSMCs. Moreover, we found that overexpression of ATF3 promoted migration of VSMCs and induced expression of matrix metalloproteinase 1, 3, and 13. These results suggest that ATF3 plays a role in regulating migration of VSMCs. In addition, we found that the expression of ATF3 was upregulated in smooth muscle cells in the injured mouse femoral arteries compared with the uninjured control group. These results suggest that ATF3 is relevant to disease physiology.

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Expression of transcriptional repressor ATF3/LRF1 in human atherosclerosis: colocalization and possible involvement in cell death of vascular endothelial cells

Cited by 71 publications

References 31 publications

Far Infrared Ray Radiation Inhibits the Proliferation of A549, HSC3 and Sa3 Cancer Cells through Enhancing the Expression of ATF3 Gene

Far Infrared Ray Radiation Inhibits the Proliferation of A549, HSC3 and Sa3 Cancer Cells through Enhancing the Expression of ATF3 Gene

Wounding activates p38 map kinase and activation transcription factor 3 in leading keratinocytes

Activating transcription factor 3 regulates survivability and migration of vascular smooth muscle cells

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