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Journal articles on the topic 'ERK5/BMK1'

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Published: 10 March 2023

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1

Nithianandarajah-Jones, Gopika N., Bettina Wilm, Christopher E. P. Goldring, Jürgen Müller, and Michael J. Cross. "The role of ERK5 in endothelial cell function." Biochemical Society Transactions 42, no. 6 (November 17, 2014): 1584–89. http://dx.doi.org/10.1042/bst20140276.

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Extracellular-signal-regulated kinase 5 (ERK5), also termed big MAPK1 (BMK1), is the most recently discovered member of the mitogen-activated protein kinase (MAPK) family. It is expressed in a variety of tissues and is activated by a range of growth factors, cytokines and cellular stresses. Targeted deletion of Erk5 in mice has revealed that the ERK5 signalling cascade is critical for normal cardiovascular development and vascular integrity. In vitro studies have revealed that, in endothelial cells, ERK5 is required for preventing apoptosis, mediating shear-stress signalling and regulating tumour angiogenesis. The present review focuses on our current understanding of the role of ERK5 in regulating endothelial cell function.

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2

Roberts, Owain Llŷr, Katherine Holmes, Jürgen Müller, Darren A. E. Cross, and Michael J. Cross. "ERK5 and the regulation of endothelial cell function." Biochemical Society Transactions 37, no. 6 (November 19, 2009): 1254–59. http://dx.doi.org/10.1042/bst0371254.

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ERK5 (extracellular-signal-regulated kinase 5), also termed BMK1 [big MAPK1 (mitogen-activated protein kinase 1)], is the most recently discovered member of the MAPK family. It is expressed in a variety of tissues and is activated by a range of growth factors, cytokines and cellular stresses. Targeted deletion of Erk5 in mice has revealed that the ERK5 signalling cascade is critical for normal cardiovascular development and vascular integrity. In vitro studies have revealed that in endothelial cells, ERK5 is required for preventing apoptosis, mediating shear-stress signalling, regulating hypoxia, tumour angiogenesis and cell migration. This review focuses on our current understanding of the role of ERK5 in regulating endothelial cell function.

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3

SQUIRES, Matthew S., Paula M. NIXON, and Simon J. COOK. "Cell-cycle arrest by PD184352 requires inhibition of extracellular signal-regulated kinases (ERK) 1/2 but not ERK5/BMK1." Biochemical Journal 366, no. 2 (September 1, 2002): 673–80. http://dx.doi.org/10.1042/bj20020372.

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Serum and growth factors activate both the canonical extracellular signal-regulated kinase (ERK) 1/2 pathway and the ERK5/big mitogen-activated protein kinase 1 (BMK) 1 pathway. Pharmacological inhibition of the ERK1/2 pathway using PD98059 and U0126 prevents cyclin D1 expression and inhibits cell proliferation, arguing that the ERK1/2 pathway is rate limiting for cell-cycle re-entry. However, both PD98059 and U0126 also inhibit the ERK5/BMK1 pathway, raising the possibility that the anti-proliferative effect of such drugs may be due to inhibition of ERK5 or both pathways. Here we characterize the effect of the novel mitogen-activated protein kinase/ERK kinase (MEK) inhibitor, PD184352, on the ERK1/2 and ERK5 pathways in the Chinese hamster fibroblast cell line CCl39. In quiescent cells, serum-stimulated ERK1 activity was completely inhibited by PD184352 with an IC50 below 1μM, whereas ERK5 activation was unaffected even at 20μM. Serum-stimulated DNA synthesis and cyclin D1 expression was inhibited by low doses of PD184352, which abolished ERK1 activity but had no effect on ERK5. Similarly, in cycling cells PD184352 caused a dose-dependent G1 arrest and inhibition of cyclin D1 expression at low doses, which inhibited ERK1 but were without effect on ERK5. These results indicate that the anti-proliferative effect of PD184352 is due to inhibition of the classical ERK1/2 pathway and does not require inhibition of the ERK5 pathway.

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4

Yan, Chen, Honglin Luo, Jiing-Dwan Lee, Jun-ichi Abe, and Bradford C. Berk. "Molecular Cloning of Mouse ERK5/BMK1 Splice Variants and Characterization of ERK5 Functional Domains." Journal of Biological Chemistry 276, no. 14 (January 3, 2001): 10870–78. http://dx.doi.org/10.1074/jbc.m009286200.

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5

Cameron, Scott J., Jun-ichi Abe, Sundeep Malik, Wenyi Che, and Jay Yang. "Differential Role of MEK5α and MEK5β in BMK1/ERK5 Activation." Journal of Biological Chemistry 279, no. 2 (October 28, 2003): 1506–12. http://dx.doi.org/10.1074/jbc.m308755200.

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6

Zheng, Qinlei, Guoyong Yin, Chen Yan, Megan Cavet, and Bradford C. Berk. "14-3-3β Binds to Big Mitogen-activated Protein Kinase 1 (BMK1/ERK5) and Regulates BMK1 Function." Journal of Biological Chemistry 279, no. 10 (December 16, 2003): 8787–91. http://dx.doi.org/10.1074/jbc.m310212200.

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7

Kamakura, Sachiko, Tetsuo Moriguchi, and Eisuke Nishida. "Activation of the Protein Kinase ERK5/BMK1 by Receptor Tyrosine Kinases." Journal of Biological Chemistry 274, no. 37 (September 10, 1999): 26563–71. http://dx.doi.org/10.1074/jbc.274.37.26563.

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8

Reddy, Sekhar P. M., Pavan Adiseshaiah, Paul Shapiro, and Hue Vuong. "BMK1 (ERK5) Regulates Squamous Differentiation MarkerSPRR1BTranscription in Clara-like H441 Cells." American Journal of Respiratory Cell and Molecular Biology 27, no. 1 (July 2002): 64–70. http://dx.doi.org/10.1165/ajrcmb.27.1.20020003oc.

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9

Hayashi, Masaaki, and Jiing-Dwan Lee. "Role of the BMK1/ERK5 signaling pathway: lessons from knockout mice." Journal of Molecular Medicine 82, no. 12 (October 28, 2004): 800–808. http://dx.doi.org/10.1007/s00109-004-0602-8.

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10

Radu, Maria, Karen Lyle, Klaus P. Hoeflich, Olga Villamar-Cruz, Hartmut Koeppen, and Jonathan Chernoff. "p21-Activated Kinase 2 Regulates Endothelial Development and Function through the Bmk1/Erk5 Pathway." Molecular and Cellular Biology 35, no. 23 (September 21, 2015): 3990–4005. http://dx.doi.org/10.1128/mcb.00630-15.

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p21-activated kinases (Paks) have been shown to regulate cytoskeleton rearrangements, cell proliferation, attachment, and migration in a variety of cellular contexts, including endothelial cells. However, the role of endothelial Pak in embryo development has not been reported, and currently, there is no consensus on the endothelial function of individual Pak isoforms, in particular p21-activated kinase 2 (Pak2), the main Pak isoform expressed in endothelial cells. In this work, we employ genetic and molecular studies that show that Pak2, but not Pak1, is a critical mediator of development and maintenance of endothelial cell function. Endothelial depletion of Pak2 leads to early embryo lethality due to flawed blood vessel formation in the embryo body and yolk sac. In adult endothelial cells, Pak2 depletion leads to severe apoptosis and acute angiogenesis defects, and in adult mice, endothelial Pak2 deletion leads to increased vascular permeability. Furthermore, ubiquitous Pak2 deletion is lethal in adult mice. We show that many of these defects are mediated through a newly unveiled Pak2/Bmk1 pathway. Our results demonstrate that endothelial Pak2 is essential during embryogenesis and also for adult blood vessel maintenance, and they also pinpoint the Bmk1/Erk5 pathway as a critical mediator of endothelial Pak2 signaling.

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11

Kato, Yutaka, Richard I. Tapping, Shuang Huang, Mark H. Watson, Richard J. Ulevitch, and Jiing-Dwan Lee. "Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor." Nature 395, no. 6703 (October 1998): 713–16. http://dx.doi.org/10.1038/27234.

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12

McCaw, B. J., S. Y. Chow, E. S. M. Wong, K. L. Tan, H. Guo, and G. R. Guy. "Identification and characterization of mErk5-T, a novel Erk5/Bmk1 splice variant." Gene 345, no. 2 (January 2005): 183–90. http://dx.doi.org/10.1016/j.gene.2004.11.011.

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13

Pi, Xinchun, Chen Yan, and Bradford C. Berk. "Big Mitogen-Activated Protein Kinase (BMK1)/ERK5 Protects Endothelial Cells From Apoptosis." Circulation Research 94, no. 3 (February 20, 2004): 362–69. http://dx.doi.org/10.1161/01.res.0000112406.27800.6f.

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14

Kato, Y. "BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C." EMBO Journal 16, no. 23 (December 1, 1997): 7054–66. http://dx.doi.org/10.1093/emboj/16.23.7054.

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15

Maciejewska, Zuzanna, Aude Pascal, Jacek Z. Kubiak, and Maria A. Ciemerych. "Phosphorylated ERK5/BMK1 transiently accumulates within division spindles in mouse oocytes and preimplantation embryos." Folia Histochemica et Cytobiologica 49, no. 3 (October 28, 2011): 528–34. http://dx.doi.org/10.5603/fhc.2011.0074.

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16

Pi, Xinchun, Gwenaele Garin, Liang Xie, Qinlei Zheng, Heng Wei, Jun-ichi Abe, Chen Yan, and Bradford C. Berk. "BMK1/ERK5 Is a Novel Regulator of Angiogenesis by Destabilizing Hypoxia Inducible Factor 1α." Circulation Research 96, no. 11 (June 10, 2005): 1145–51. http://dx.doi.org/10.1161/01.res.0000168802.43528.e1.

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17

Sun, Weiyong, Kamala Kesavan, Brian C. Schaefer, Timothy P. Garrington, Margaret Ware, Nancy Lassignal Johnson, Erwin W. Gelfand, and Gary L. Johnson. "MEKK2 Associates with the Adapter Protein Lad/RIBP and Regulates the MEK5-BMK1/ERK5 Pathway." Journal of Biological Chemistry 276, no. 7 (November 9, 2000): 5093–100. http://dx.doi.org/10.1074/jbc.m003719200.

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18

Yang, C. C., O. I. Ornatsky, J. C. McDermott, T. F. Cruz, and C. A. Prody. "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1." Nucleic Acids Research 26, no. 20 (October 1, 1998): 4771–77. http://dx.doi.org/10.1093/nar/26.20.4771.

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19

Cameron, Scott J., Seigo Itoh, Christopher P. Baines, Changxi Zhang, Shinsuke Ohta, Wenyi Che, Michael Glassman, et al. "Activation of big MAP kinase 1 (BMK1/ERK5) inhibits cardiac injury after myocardial ischemia and reperfusion." FEBS Letters 566, no. 1-3 (May 21, 2004): 255–60. http://dx.doi.org/10.1016/j.febslet.2004.03.120.

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20

Hayashi, Masaaki, Sung-Woo Kim, Kyoko Imanaka-Yoshida, Toshimichi Yoshida, E. Dale Abel, Brian Eliceiri, Young Yang, Richard J. Ulevitch, and Jiing-Dwan Lee. "Targeted deletion of BMK1/ERK5 in adult mice perturbs vascular integrity and leads to endothelial failure." Journal of Clinical Investigation 113, no. 8 (April 15, 2004): 1138–48. http://dx.doi.org/10.1172/jci200419890.

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21

Arias-González, Laura, Inmaculada Moreno-Gimeno, Antonio Rubio del Campo, Serrano-Oviedo Leticia, María Llanos Valero, Azucena Esparís-Ogando, Miguel Ángel de la Cruz-Morcillo, et al. "ERK5/BMK1 Is a Novel Target of the Tumor Suppressor VHL: Implication in Clear Cell Renal Carcinoma." Neoplasia 15, no. 6 (June 2013): 649—IN17. http://dx.doi.org/10.1593/neo.121896.

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22

Watanabe, N. "Control of body size by SMA-5, a homolog of MAP kinase BMK1/ERK5, in C. elegans." Development 132, no. 14 (July 15, 2005): 3175–84. http://dx.doi.org/10.1242/dev.01895.

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23

Wei, Xudong, Rui-Hua Wei, Timothy Garrington, Gary L. Johnson, and Erwin W. Gelfand. "MEKK2-MEK5-BMK1/ERK5-MEF2C activation: A new pathway regulating c-jun gene expression in stimulated mast cells." Journal of Allergy and Clinical Immunology 109, no. 1 (January 2002): S323. http://dx.doi.org/10.1016/s0091-6749(02)82133-9.

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24

Luo, Fengbao, Jian Shi, Qianqian Shi, Xianlin Xu, Ying Xia, and Xiaozhou He. "Mitogen-Activated Protein Kinases and Hypoxic/Ischemic Nephropathy." Cellular Physiology and Biochemistry 39, no. 3 (2016): 1051–67. http://dx.doi.org/10.1159/000447812.

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Tissue hypoxia/ischemia is a pathological feature of many human disorders including stroke, myocardial infarction, hypoxic/ischemic nephropathy, as well as cancer. In the kidney, the combination of limited oxygen supply to the tissues and high oxygen demand is considered the main reason for the susceptibility of the kidney to hypoxic/ischemic injury. In recent years, increasing evidence has indicated that a reduction in renal oxygen tension/blood supply plays an important role in acute kidney injury, chronic kidney disease, and renal tumorigenesis. However, the underlying signaling mechanisms, whereby hypoxia alters cellular behaviors, remain poorly understood. Mitogen-activated protein kinases (MAPKs) are key signal-transducing enzymes activated by a wide range of extracellular stimuli, including hypoxia/ischemia. There are four major family members of MAPKs: the extracellular signal-regulated kinases-1 and -2 (ERK1/2), the c-Jun N-terminal kinases (JNK), p38 MAPKs, and extracellular signal-regulated kinase-5 (ERK5/BMK1). Recent studies, including ours, suggest that these MAPKs are differentially involved in renal responses to hypoxic/ischemic stress. This review will discuss their changes in hypoxic/ischemic pathophysiology with acute kidney injury, chronic kidney diseases and renal carcinoma.

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25

Vassalli, Giuseppe, Giuseppina Milano, and Tiziano Moccetti. "Role of Mitogen-Activated Protein Kinases in Myocardial Ischemia-Reperfusion Injury during Heart Transplantation." Journal of Transplantation 2012 (2012): 1–16. http://dx.doi.org/10.1155/2012/928954.

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In solid organ transplantation, ischemia/reperfusion (IR) injury during organ procurement, storage and reperfusion is an unavoidable detrimental event for the graft, as it amplifies graft inflammation and rejection. Intracellular mitogen-activated protein kinase (MAPK) signaling pathways regulate inflammation and cell survival during IR injury. The four best-characterized MAPK subfamilies are the c-Jun NH2-terminal kinase (JNK), extracellular signal- regulated kinase-1/2 (ERK1/2), p38 MAPK, and big MAPK-1 (BMK1/ERK5). Here, we review the role of MAPK activation during myocardial IR injury as it occurs during heart transplantation. Most of our current knowledge regarding MAPK activation and cardioprotection comes from studies of preconditioning and postconditioning in nontransplanted hearts. JNK and p38 MAPK activation contributes to myocardial IR injury after prolonged hypothermic storage. p38 MAPK inhibition improves cardiac function after cold storage, rewarming and reperfusion. Small-molecule p38 MAPK inhibitors have been tested clinically in patients with chronic inflammatory diseases, but not in transplanted patients, so far. Organ transplantation offers the opportunity of starting a preconditioning treatment before organ procurement or during cold storage, thus modulating early events in IR injury. Future studies will need to evaluate combined strategies including p38 MAPK and/or JNK inhibition, ERK1/2 activation, pre- or postconditioning protocols, new storage solutions, and gentle reperfusion.

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26

Rovida, Elisabetta, Elena Spinelli, Sara Sdelci, Valentina Barbetti, Andrea Morandi, Serena Giuntoli, and Persio Dello Sbarba. "ERK5/BMK1 Is Indispensable for Optimal Colony-Stimulating Factor 1 (CSF-1)-Induced Proliferation in Macrophages in a Src-Dependent Fashion." Journal of Immunology 180, no. 6 (March 5, 2008): 4166–72. http://dx.doi.org/10.4049/jimmunol.180.6.4166.

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27

Xing, Feiyue, Yong Jiang, Jing Liu, Kesen Zhao, Yongyan Mo, Zhifeng Liu, and Yaoying Zeng. "Downregulation of human endothelial nitric oxide synthase promoter activity by p38 mitogen-activated protein kinase activation." Biochemistry and Cell Biology 84, no. 5 (October 2006): 780–89. http://dx.doi.org/10.1139/o06-092.

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Human endothelial nitric oxide synthase (eNOS) plays a crucial role in maintaining blood pressure homeostasis and vascular integrity. eNOS gene expression may be upregulated by a signaling pathway, including PI-3Kγ → Jak2 → MEK1 → ERK1/2 → PP2A. It remains unclear whether other mitogen-activated protein kinase (MAPK) family members, such as JNK, p38 kinase, and ERK5/BMK1, also modulate eNOS gene expression. Our purpose, therefore, is to shed light on the effect of the p38 MAPK signaling pathway on the regulation of eNOS promoter activity. The results showed that a red fluorescent protein reporter gene vector containing the full length of the human eNOS promoter was first successfully constructed, expressing efficiently in ECV304 cells with the characteristics of real time observation. The wild-types of p38α, p38β, p38γ, and p38δ signal molecules all markedly downregulated promoter activity, which could be reversed by their negative mutants, including p38α (AF), p38β (AF), p38γ (AF), and p38δ (AF). Promoter activity was also significantly downregulated by MKK6b (E), an active mutant of an upstream kinase of p38 MAPK. The reduction in promoter activity by p38 MAPK could be blocked by treatment with a p38 MAPK specific inhibitor, SB203580. Moreover, the activation of endogenous p38 MAPK induced by lipopolysaccharide resulted in a prominent reduction in promoter activity. These findings strongly suggest that the activation of the p38 MAPK signaling pathway may be implicated in the downregulation of human eNOS promoter activity.

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28

Yoshizumi, Masanori, Yoji Kyotani, Jing Zhao, Kosuke Nagayama, Satoyasu Ito, Yuichi Tsuji, and Kentaro Ozawa. "The Role of Big Mitogen-Activated Protein Kinase 1 (BMK1) / Extracellular Signal-Regulated Kinase 5 (ERK5) in the Pathogenesis and Progression of Atherosclerosis." Journal of Pharmacological Sciences 120, no. 4 (2012): 259–63. http://dx.doi.org/10.1254/jphs.12r11cp.

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29

IZAWA, Yuki, Masanori YOSHIZUMI, Keisuke ISHIZAWA, Yoshiko FUJITA, Shuji KONDO, Shoji KAGAMI, Kazuyoshi KAWAZOE, Koichiro TSUCHIYA, Shuhei TOMITA, and Toshiaki TAMAKI. "Big Mitogen-Activated Protein Kinase 1 (BMK1)/Extracellular Signal Regulated Kinase 5 (ERK5) Is Involved in Platelet-Derived Growth Factor (PDGF)-Induced Vascular Smooth Muscle Cell Migration." Hypertension Research 30, no. 11 (2007): 1107–17. http://dx.doi.org/10.1291/hypres.30.1107.

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