Role of CaMKII in hydrogen peroxide activation of ERK1/2, p38 MAPK, HSP27 and actin reorganization in endothelial cells

Nguyen, Andrew; Chen, Peng; Cai, Hua

doi:10.1016/j.febslet.2004.06.061

Cited by 88 publications

(63 citation statements)

References 35 publications

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“…Specifically, H 2 O 2 has previously been shown to induce stress fibers in endothelial cells, inhibiting normal motility. NO, by scavenging super oxide and indirectly reducing H 2 O 2 levels, could prevent H 2 O 2 induction of cytoskeletal reorganization via calcium/calmodulindependent protein kinase II, Janus kinase 2 and mitogenactivated protein kinase, and extracellular signal-related kinase (37). However, we believe this is less likely since the reactive oxygen scavenger uric acid could not fully correct the migration defect in CD34ϩ cells (data not shown).…”

Section: Discussionmentioning

confidence: 54%

Nitric Oxide Cytoskeletal–Induced Alterations Reverse the Endothelial Progenitor Cell Migratory Defect Associated With Diabetes

et al. 2006

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Stromal-derived factor-1 (SDF-1) is a critical chemokine for endothelial progenitor cell (EPC) recruitment to areas of ischemia, allowing these cells to participate in compensatory angiogenesis. The SDF-1 receptor, CXCR4, is expressed in developing blood vessels as well as on CD34؉ EPCs. We describe that picomolar and nanomolar concentrations of SDF-1 differentially influence neovascularization, inducing CD34؉ cell migration and EPC tube formation. CD34؉ cells isolated from diabetic patients demonstrate a marked defect in migration to SDF-1. This defect is associated, in some but not all patients, with a cell surface activity of CD26/dipeptidyl peptidase IV, an enzyme that inactivates SDF-1. Diabetic CD34؉ cells also do not migrate in response to vascular endothelial growth factor and are structurally rigid. However, incubating CD34؉ cells with a nitric oxide (NO) donor corrects this migration defect and corrects the cell deformability. In addition, exogenous NO alters vasodilator-stimulated phosphoprotein and mammalian-enabled distribution in EPCs. These data support a common downstream cytoskeletal alteration in diabetic CD34؉ cells that is independent of growth factor receptor activation and is correctable with exogenous NO. This inability of diabetic EPCs to respond to SDF-1 may contribute to aberrant tissue vascularization and endothelial repair in diabetic patients. Diabetes 55: 102-109, 2006

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Section: Discussionmentioning

confidence: 54%

Nitric Oxide Cytoskeletal–Induced Alterations Reverse the Endothelial Progenitor Cell Migratory Defect Associated With Diabetes

et al. 2006

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“…21,[28][29][30] Here, we also showed that TGF-b1 induces Hsp27 phosphorylation via the activation of p38MAPK in hPDL cells. The p38MAPK-specific inhibitor SB203580 blocked the phosphorylation of Hsp27 and the migration of hPDL cells.…”

Section: Discussionmentioning

confidence: 67%

“…31) Therefore our results suggest that the phosphorylation of Hsp27 is dependent on p38MAPK activation, in agreement with previous observations. [28][29][30] However, there was no significant change in the activation of integrin b1/Akt signaling in TGF- b1-stimulated hPDL cells. Based on these findings, it is possible that TGF-b1-induced p38MAPK/Hsp27 pathway may regulate an important role in hPDL cell migration (Fig.…”

Section: Discussionmentioning

confidence: 78%

Transforming Growth Factor .BETA.1 Promotes Migration of Human Periodontal Ligament Cells through Heat Shock Protein 27 Phosphorylation

Kwon

Kim

Fujii

et al. 2011

Biological & Pharmaceutical Bulletin

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The human periodontal ligament (hPDL) is a highly specialized connective tissue located between the tooth root and alveolar bone. Once the hPDL is severely damaged by periodontal disease, its regeneration is known to be difficult. 1) hPDL cells can serve as an in vitro model to determine the effects of growth factors implicated in periodontal repair or regeneration. Cell migration generally plays roles in tissue formation and wound healing as tissue repair takes place following an injury, which involves the processes of inflammation, new tissue formation, and scar formation.2,3) The migration of hPDL cells is also a critical function in the initiation of periodontal wound healing. 2,4) Transforming growth factor b1 (TGF-b1) is a multifunctional peptide that regulates various cellular activities, including proliferation, differentiation, and expression of extracellular matrix proteins.5) TGF-b1 is a potent modulator of tissue repair in various tissues. It was reported that TGF-b1 alone or in combination with other growth factors accelerates various phases of wound healing.6,7) TGF-b1 may also play an important role in the modulation of tissue formation and development of the periodontium.8) The addition of TGF-b1 to gingival and periodontal ligament fibroblast cell cultures was shown to enhance RNA and protein synthesis. 9)Heat shock protein 27 (Hsp27) acts as ATP-independent molecular chaperone.10) In addition to its chaperone function, Hsp27 also seems to be an important regulator of structural integrity and membrane stability, actin polymerization and intermediate filament cytoskeleton formation, cell migration, epithelial cell-cell adhesion, cell cycle progression, proinflammatory gene expression, signal transduction pathways, mRNA stabilization, differentiation, and apoptosis.11,12) Previous results strongly suggested that phosphorylated Hsp27 was critically involved in the migration process, possibly through the association with signal transducer and activator of transcription 3 (STAT3) and focal adhesion kinase (FAK).13) Cell migration is regulated by various signaling pathway including the b1 integrin, Akt, extracellular signalregulated kinase (ERK) and nuclear factor-kappaB-dependent pathways through TGF-b1 in human cancer cells.14,15) In our previous study, we confirmed that TGF-b1-induced Hsp27 activation promotes the migration of mouse dental papilla-derived MDPC-23 cells.16) Dentinal healing and repair are the result of successive and interrelated processes that include proliferation, chemotaxis, and differentiation of dental pulp cells into odontoblasts, leading to reparative dentin formation. 17) However, the underlying mechanism of TGF-b1 responsible for regulating hPDL cell migration has not been fully elucidated. Because hPDL cells are responsible for tissue regeneration and mineralized tissue matrix formation, and cell migration are critical processes in tissue regeneration, it is valuable to clarify the precise mechanism of the cell migration of hPDL cells. In this study, we therefore investig...

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“…Although evidences exist that hydrogen peroxide activates p44/p42 MAPK in mammalian cells, our results show for the first time activation of p44/p42 MAPK by hydrogen peroxide in the yeast S. cerevisiae (Hannken et al, 2000;Nguyen et al, 2004;van Rossum et al, 2004). Interestingly Mkp1, a Pneumocystis carinii homologue of Mpk1, has been found to be activated by the same oxidant (Fox and Smulian, 1999).…”

Section: Discussionmentioning

confidence: 69%

Oxidative Stress ActivatesFUS1andRLM1Transcription in the YeastSaccharomyces cerevisiaein an Oxidant-dependent Manner

Staleva

Hall

Orlow

2004

MBoC

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Mating in haploid Saccharomyces cerevisiae occurs after activation of the pheromone response pathway. Biochemical components of this pathway are involved in other yeast signal transduction networks. To understand more about the coordination between signaling pathways, we used a "chemical genetic" approach, searching for compounds that would activate the pheromone-responsive gene FUS1 and RLM1, a reporter for the cell integrity pathway. We found that catecholamines (L-3,4-hydroxyphenylalanine [L-dopa], dopamine, adrenaline, and noradrenaline) elevate FUS1 and RLM1 transcription. N-Acetyl-cysteine, a powerful antioxidant in yeast, completely reversed this effect, suggesting that FUS1 and RLM1 activation in response to catecholamines is a result of oxidative stress. The oxidant hydrogen peroxide also was found to activate transcription of an RLM1 reporter. Further genetic analysis combined with immunoblotting revealed that Kss1, one of the mating mitogen-activated protein kinases (MAPKs), and Mpk1, an MAPK of the cell integrity pathway, participated in L-dopa-induced stimulation of FUS1 and RLM1 transcription. We also report that Mpk1 and Hog1, the high osmolarity MAPK, were phosphorylated upon induction by hydrogen peroxide. Together, our results demonstrate that cells respond to oxidative stress via different signal transduction machinery dependent upon the nature of the oxidant. INTRODUCTIONIn the haploid cells of the yeast Saccharomyces cerevisiae, four essential MAPK cascades (Figure 1) respond to different external signals to mediate specific responses. The mating pathway is activated by peptide pheromones and induces cell-cycle arrest and the morphological changes required for mating (Elion, 1998;Gustin et al., 1998). The invasive growth pathway is activated by starvation and induces foraging into the agar substratum. The high osmolarity glycerol (HOG) pathway increases intracellular glycerol levels in response to hypertonic stress, whereas the cell integrity pathway is activated by hypotonic stress, heat shock, or impaired cell wall synthesis. Recently, an additional MAPK cascade has been described: the Kss1 vegetative growth pathway (Lee and Elion, 1999). The Kss1 pathway may be activated by cell wall stress or changes in osmolarity (Cullen et al., 2000).The mating pathway is the most studied cellular response to an external signal. As a relatively simple G protein-coupled cascade, it is a widely used model to study mammalian G protein-coupled receptors. The mating cascade includes pheromone receptors (Ste2 and Ste3), G proteins (Gpa1, Ste4, and Ste18), the p21 activating protein kinase Ste20, a mitogen-activated protein kinase kinase kinase (MAPKKK) Ste11, a mitogen-activated protein kinase kinase (MAPKK) Ste7, a scaffolding protein Ste5 and two MAPKs (Fus3 and Kss1) (Gustin et al., 1998;Madhani and Fink, 1998;Farley et al., 1999). Targets of the terminal MAPK include Ste12, a factor required for transcription of pheromone-responsive genes, and Far1, a bifunctional protein required for polarization and G1...

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Role of CaMKII in hydrogen peroxide activation of ERK1/2, p38 MAPK, HSP27 and actin reorganization in endothelial cells

Cited by 88 publications

References 35 publications

Nitric Oxide Cytoskeletal–Induced Alterations Reverse the Endothelial Progenitor Cell Migratory Defect Associated With Diabetes

Nitric Oxide Cytoskeletal–Induced Alterations Reverse the Endothelial Progenitor Cell Migratory Defect Associated With Diabetes

Transforming Growth Factor .BETA.1 Promotes Migration of Human Periodontal Ligament Cells through Heat Shock Protein 27 Phosphorylation

Oxidative Stress ActivatesFUS1andRLM1Transcription in the YeastSaccharomyces cerevisiaein an Oxidant-dependent Manner

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