Rac1, and not Rac2, is involved in the regulation of the intracellular hydrogen peroxide level in HepG2 cells

Cool, Robbert H.; Merten, E.; Theiss, Christiane; Acker, H.

doi:10.1042/bj3320005

Cited by 42 publications

(24 citation statements)

References 42 publications

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“…This latter finding is in contrast to the effect of Rac1V12 on H 2 O 2 production in HeLa cells (16). However, our findings agree with studies looking at the role of Rac1 in ROS generation, specifically in HepG2 cells (33). Such studies have shown only a very modest increase in intracellular ROS in HepG2 cells expressing Rac1V12, and only after NAD(P)H stimulation.…”

Section: Fig 1 Expression Of Rac1n17 Suppresses Hypoxia/reoxygenatisupporting

confidence: 89%

Rac1 Regulates Stress-induced, Redox-dependent Heat Shock Factor Activation

Ozaki¹,

Deshpande²,

Angkeow³

et al. 2000

Journal of Biological Chemistry

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The signaling pathway by which environmental stresses activate heat shock factors (HSFs) is not completely understood. We show that the small GTPase rac1, and Rac1-regulated reactive oxygen species (ROS) play an important role in stress-stimulated heat shock response. A dominant-negative allele of Rac1 (Rac1N17) inhibits the hypoxia/reoxygenation and sodium arsenite-induced transcriptional activity of HSF-1 and the transcription of heat shock protein 70. Rac1N17 also suppresses the production of intracellular ROS induced by hypoxia/reoxygenation or sodium arsenite. Moreover, direct suppression of intracellular ROS levels by antioxidants decreases stress-stimulated HSF activity. However, expression of a constitutively active mutant of Rac1 (Rac1V12) in the absence of extracellular stresses does not increase intracellular ROS levels or induce the heat shock response. These results show that Rac1 is a necessary but insufficient component of the stress-induced signaling pathway that leads to ROS production, activation of HSFs, and transcription of heat shock proteins.

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Section: Fig 1 Expression Of Rac1n17 Suppresses Hypoxia/reoxygenatisupporting

confidence: 89%

Rac1 Regulates Stress-induced, Redox-dependent Heat Shock Factor Activation

Ozaki¹,

Deshpande²,

Angkeow³

et al. 2000

Journal of Biological Chemistry

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“…Other studies have also implicated that ROS are involved in the regulation of KCC activity in red blood cells (Muzyamba et al, 2000;Gibson et al, 2003). NEM appeared to generate ROS by activation of the NADPH oxidase which is known to exist in HepG2 cells (Ehleben et al, 1997;Cool et al, 1998). In this study we demonstrated that AA itself generated ROS through activation of the NADPH oxidase in HepG2 cells.…”

Section: Discussionsupporting

confidence: 69%

Arachidonic Acid Activates K+-Cl--cotransport in HepG2 Human Hepatoblastoma Cells

Lee

2009

Korean J Physiol Pharmacol

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“…The closely related small GTP-binding proteins Rac1, Rac2, and Rac3 are part of a larger Rho subfamily of Ras proteins. Rac1 controls actin redistribution to membrane ruffles in fibroblasts and other cell types, as well as the activation of the NADPH oxidase in both phagocytes as well as non-phagocytic cells (11,14,38). Direct evidence supporting a mitogenic function of oxidants generated by Rac1 has been reported (10,13).…”

Section: Discussionmentioning

confidence: 99%

Oxidant-induced Vascular Endothelial Growth Factor Expression in Human Keratinocytes and Cutaneous Wound Healing

Sen

Khanna

Babior

et al. 2002

Journal of Biological Chemistry

293

218

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Neutrophils and macrophages, recruited to the wound site, release reactive oxygen species by respiratory burst. It is commonly understood that oxidants serve mainly to kill bacteria and prevent wound infection. We tested the hypothesis that oxidants generated at the wound site promote dermal wound repair. We observed that H 2 O 2 potently induces vascular endothelial growth factor (VEGF) expression in human keratinocytes. Deletion mutant studies with a VEGF promoter construct revealed that a GC-rich sequence from bp ؊194 to ؊50 of the VEGF promoter is responsible for the H 2 O 2 response. It was established that at M concentrations oxidant induces VEGF expression and that oxidant-induced VEGF expression is independent of hypoxia-inducible factor (HIF)-1 and dependent on Sp1 activation. To test the effect of NADPH oxidase-generated reactive oxygen species on wound healing in vivo, Rac1 gene transfer was performed to dermal excisional wounds left to heal by secondary intention. Rac1 gene transfer accelerated wound contraction and closure. Rac1 overexpression was associated with higher VEGF expression both in vivo as well in human keratinocytes. Interestingly, Rac1 gene therapy was associated with a more well defined hyperproliferative epithelial region, higher cell density, enhanced deposition of connective tissue, and improved histological architecture. Overall, the histological data indicated that Rac1 might be an important stimulator of various aspects of the repair process, eventually enhancing the wound-healing process as a whole. Taken together, the results of this study indicate that wound healing is subject to redox control.

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Rac1, and not Rac2, is involved in the regulation of the intracellular hydrogen peroxide level in HepG2 cells

Cited by 42 publications

References 42 publications

Rac1 Regulates Stress-induced, Redox-dependent Heat Shock Factor Activation

Rac1 Regulates Stress-induced, Redox-dependent Heat Shock Factor Activation

Arachidonic Acid Activates K+-Cl--cotransport in HepG2 Human Hepatoblastoma Cells

Oxidant-induced Vascular Endothelial Growth Factor Expression in Human Keratinocytes and Cutaneous Wound Healing

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