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Journal articles on the topic 'Apoptosis signal-regulating kinase 1'

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Published: 10 December 2022

Last updated: 28 January 2023

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1

Kim, Albert H., Gus Khursigara, Xuan Sun, Thomas F. Franke, and Moses V. Chao. "Akt Phosphorylates and Negatively Regulates Apoptosis Signal-Regulating Kinase 1." Molecular and Cellular Biology 21, no. 3 (February 1, 2001): 893–901. http://dx.doi.org/10.1128/mcb.21.3.893-901.2001.

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ABSTRACT The Akt family of serine/threonine-directed kinases promotes cellular survival in part by phosphorylating and inhibiting death-inducing proteins. Here we describe a novel functional interaction between Akt and apoptosis signal-regulating kinase 1 (ASK1), a mitogen-activated protein kinase kinase kinase. Akt decreased ASK1 kinase activity stimulated by both oxidative stress and overexpression in 293 cells by phosphorylating a consensus Akt site at serine 83 of ASK1. Activation of the phosphoinositide 3-kinase (PI3-K)/Akt pathway also inhibited the serum deprivation-induced activity of endogenous ASK1 in L929 cells. An association between Akt and ASK1 was detected in cells by coimmunoprecipitation. Phosphorylation by Akt inhibited ASK1-mediated c-Jun N-terminal kinase and activating transcription factor 2 activities in intact cells. Finally, activation of the PI3-K/Akt pathway reduced apoptosis induced by ASK1 in a manner dependent on phosphorylation of serine 83 of ASK1. These results provide the first direct link between Akt and the family of stress-activated kinases.

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2

Wilson, Kathryn S., Hanna Buist, Kornelija Suveizdyte, John T. Liles, Grant R. Budas, Colin Hughes, Margaret R. MacLean, et al. "Apoptosis signal-regulating kinase 1 inhibition in in vivo and in vitro models of pulmonary hypertension." Pulmonary Circulation 10, no. 2 (April 2020): 204589402092281. http://dx.doi.org/10.1177/2045894020922810.

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Pulmonary arterial hypertension, group 1 of the pulmonary hypertension disease family, involves pulmonary vascular remodelling, right ventricular dysfunction and cardiac failure. Oxidative stress, through activation of mitogen-activated protein kinases is implicated in these changes. Inhibition of apoptosis signal-regulating kinase 1, an apical mitogen-activated protein kinase, prevented pulmonary arterial hypertension developing in rodent models. Here, we investigate apoptosis signal-regulating kinase 1 in pulmonary arterial hypertension by examining the impact that its inhibition has on the molecular and cellular signalling in established disease. Apoptosis signal-regulating kinase 1 inhibition was investigated in in vivo pulmonary arterial hypertension and in vitro pulmonary hypertension models. In the in vivo model, male Sprague Dawley rats received a single subcutaneous injection of Sugen SU5416 (20 mg/kg) prior to two weeks of hypobaric hypoxia (380 mmHg) followed by three weeks normoxia (Sugen/hypoxic), then animals were either maintained for three weeks on control chow or one containing apoptosis signal-regulating kinase 1 inhibitor (100 mg/kg/day). Cardiovascular measurements were carried out. In the in vitro model, primary cultures of rat pulmonary artery fibroblasts and rat pulmonary artery smooth muscle cells were maintained in hypoxia (5% O2) and investigated for proliferation, migration and molecular signalling in the presence or absence of apoptosis signal-regulating kinase 1 inhibitor. Sugen/hypoxic animals displayed significant pulmonary arterial hypertension compared to normoxic controls at eight weeks. Apoptosis signal-regulating kinase 1 inhibitor decreased right ventricular systolic pressure to control levels and reduced muscularised vessels in lung tissue. Apoptosis signal-regulating kinase 1 inhibition was found to prevent hypoxia-induced proliferation, migration and cytokine release in rat pulmonary artery fibroblasts and also prevented rat pulmonary artery fibroblast-induced rat pulmonary artery smooth muscle cell migration and proliferation. Apoptosis signal-regulating kinase 1 inhibition reversed pulmonary arterial hypertension in the Sugen/hypoxic rat model. These effects may be a result of intrinsic changes in the signalling of adventitial fibroblast.

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3

Tobiume, Kei. "Characterization of Mouse Apoptosis Signal-regulating Kinase 1." JOURNAL OF THE STOMATOLOGICAL SOCIETY,JAPAN 65, no. 1 (1998): 42–52. http://dx.doi.org/10.5357/koubyou.65.42.

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4

Hattori, Kazuki, and Hidenori Ichijo. "Apoptosis signal-regulating kinase 1 in regulated necrosis." Cell Cycle 17, no. 1 (January 2, 2018): 5–6. http://dx.doi.org/10.1080/15384101.2017.1397330.

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5

Weijman, Johannes F., Abhishek Kumar, Sam A. Jamieson, Chontelle M. King, Tom T. Caradoc-Davies, Elizabeth C. Ledgerwood, James M. Murphy, and Peter D. Mace. "Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1." Proceedings of the National Academy of Sciences 114, no. 11 (February 27, 2017): E2096—E2105. http://dx.doi.org/10.1073/pnas.1620813114.

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Apoptosis signal-regulating kinases (ASK1–3) are apical kinases of the p38 and JNK MAP kinase pathways. They are activated by diverse stress stimuli, including reactive oxygen species, cytokines, and osmotic stress; however, a molecular understanding of how ASK proteins are controlled remains obscure. Here, we report a biochemical analysis of the ASK1 kinase domain in conjunction with its N-terminal thioredoxin-binding domain, along with a central regulatory region that links the two. We show that in solution the central regulatory region mediates a compact arrangement of the kinase and thioredoxin-binding domains and the central regulatory region actively primes MKK6, a key ASK1 substrate, for phosphorylation. The crystal structure of the central regulatory region reveals an unusually compact tetratricopeptide repeat (TPR) region capped by a cryptic pleckstrin homology domain. Biochemical assays show that both a conserved surface on the pleckstrin homology domain and an intact TPR region are required for ASK1 activity. We propose a model in which the central regulatory region promotes ASK1 activity via its pleckstrin homology domain but also facilitates ASK1 autoinhibition by bringing the thioredoxin-binding and kinase domains into close proximity. Such an architecture provides a mechanism for control of ASK-type kinases by diverse activators and inhibitors and demonstrates an unexpected level of autoregulatory scaffolding in mammalian stress-activated MAP kinase signaling.

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6

Nishida, Kazuhiko, and Kinya Otsu. "The Role of Apoptosis Signal-Regulating Kinase 1 in Cardiomyocyte Apoptosis." Antioxidants & Redox Signaling 8, no. 9-10 (September 2006): 1729–36. http://dx.doi.org/10.1089/ars.2006.8.1729.

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7

Fujisawa, Takao. "Therapeutic application of apoptosis signal-regulating kinase 1 inhibitors." Advances in Biological Regulation 66 (December 2017): 85–90. http://dx.doi.org/10.1016/j.jbior.2017.10.004.

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8

Kawarazaki, Yosuke, Hidenori Ichijo, and Isao Naguro. "Apoptosis signal-regulating kinase 1 as a therapeutic target." Expert Opinion on Therapeutic Targets 18, no. 6 (March 24, 2014): 651–64. http://dx.doi.org/10.1517/14728222.2014.896903.

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9

Mizuguchi, Junichiro, Eiko Takada, and Masae Furuhata. "Apoptosis signal-regulating kinase (ASK)-1 mediates apoptosis in B cells (34.6)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 34.6. http://dx.doi.org/10.4049/jimmunol.182.supp.34.6.

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Abstract Engagement of membrane immunoglobulin (mIg) on B cells results in reduction of the mitochondrial membrane potential (ƒ¢ƒμm) and apoptosis, which plays a crucial role in the regulation of immune responses. In this study, we show that the apoptosis signal-regulating kinase 1 (ASK1)-JNK1 signaling pathway participates in mIg-induced apoptosis in normal B cells as well as WEHI-231 B lymphoma cells. Stimulation of WEHI-231 cells with anti-IgM induces phosphorylation and subsequent activation of ASK1, leading to JNK activation. Anti-IgM stimulation produces superoxide anions (O2-), accompanied by loss of ƒ¢ƒμm and an increase in cells with sub-G1 DNA content. Anti-IgM-induced O2- production, loss of ƒ¢ƒμm, and increase in the sub-G1 fraction were all reduced substantially in WEHI-231 cells overexpressing a dominant-negative form of ASK1, compared with control vector alone. The mIg-mediated O2- production, loss of ƒ¢ƒμm, and increase in the sub-G1 fraction were partially abrogated by the reactive oxygen species scavenger N-acetyl-L-cysteine (NAC). Similarly to WEHI-231 B lymphoma cells, the mIg-mediated apoptotic features were moderately compromised in mouse ASK1-deficient B cells. Taken together, these results suggest that mIg engagement induces JNK activation through ASK1 activation, resulting in production of O2- that leads to loss of ƒ¢ƒμm and finally to apoptosis.

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10

Zou, Xianghong, Tateki Tsutsui, Dipankar Ray, James F. Blomquist, Hidenori Ichijo, David S. Ucker, and Hiroaki Kiyokawa. "The Cell Cycle-Regulatory CDC25A Phosphatase Inhibits Apoptosis Signal-Regulating Kinase 1." Molecular and Cellular Biology 21, no. 14 (July 15, 2001): 4818–28. http://dx.doi.org/10.1128/mcb.21.14.4818-4828.2001.

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ABSTRACT CDC25A phosphatase promotes cell cycle progression by activating G1 cyclin-dependent kinases and has been postulated to be an oncogene because of its ability to cooperate with RAS to transform rodent fibroblasts. In this study, we have identified apoptosis signal-regulating kinase 1 (ASK1) as a CDC25A-interacting protein by yeast two-hybrid screening. ASK1 activates the p38 mitogen-activated protein kinase (MAPK) and c-Jun NH2-terminal protein kinase–stress-activated protein kinase (JNK/SAPK) pathways upon various cellular stresses. Coimmunoprecipitation studies demonstrated that CDC25A physically associates with ASK1 in mammalian cells, and immunocytochemistry with confocal laser-scanning microscopy showed that these two proteins colocalize in the cytoplasm. The carboxyl terminus of CDC25A binds to a domain of ASK1 adjacent to its kinase domain and inhibits the kinase activity of ASK1, independent of and without effect on the phosphatase activity of CDC25A. This inhibitory action of CDC25A on ASK1 activity involves diminished homo-oligomerization of ASK1. Increased cellular expression of wild-type or phosphatase-inactive CDC25A from inducible transgenes suppresses oxidant-dependent activation of ASK1, p38, and JNK1 and reduces specific sensitivity to cell death triggered by oxidative stress, but not other apoptotic stimuli. Thus, increased expression of CDC25A, frequently observed in human cancers, could contribute to reduced cellular responsiveness to oxidative stress under mitogenic or oncogenic conditions, while it promotes cell cycle progression. These observations propose a mechanism of oncogenic transformation by the dual function of CDC25A on cell cycle progression and stress responses.

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11

Sirotkin, Alexander V., Andrej Benco, Jan Kotwica, Saleh H. Alwasel, and Abdel H. Harrath. "Apoptosis signal-regulating kinase (ASK-1) controls ovarian cell functions." Reproduction, Fertility and Development 31, no. 11 (2019): 1657. http://dx.doi.org/10.1071/rd19055.

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The involvement of the apoptosis signal-regulating kinase 1 (ASK1)-related signalling pathway in the control of reproduction is unknown. This study aimed to investigate the role of ASK-1 in the control of basic ovarian functions (proliferation, apoptosis and hormone release) and its response to ovarian hormonal regulators (leptin and FSH). We compared the accumulation of ASK-1, proliferation marker proliferating cell nuclear antigen (PCNA), apoptosis marker Bax and apoptosis and proliferation regulating transcription factor p53 and the release of progesterone (P4), oxytocin (OT), insulin-like growth factor I (IGF-I) and prostaglandins F (PGF) and E (PGE) using cultured porcine ovarian granulosa cells transfected with ASK-1 cDNA and cultured with leptin or FSH. This study is the first to demonstrate that ASK-1 does not affect cell apoptosis and viability in ovarian cells, but promotes cell proliferation, suppresses p53, alters the release of ovarian hormones (P4, OT, IGF-I, PGF and PGE) and defines their response to the upstream hormonal regulators leptin and FSH. Therefore, ASK-1 can be considered a new and important regulator of multiple ovarian functions.

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12

Hwang, Jae Ryoung, Chunlian Zhang, and Cam Patterson. "C-terminus of heat shock protein 70– interacting protein facilitates degradation of apoptosis signal-regulating kinase 1 and inhibits apoptosis signal-regulating kinase 1– dependent apoptosis." Cell Stress & Chaperones 10, no. 2 (2005): 147. http://dx.doi.org/10.1379/csc-90r.1.

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13

Kherrouche, Zoulika, Alexandre Blais, Elisabeth Ferreira, Yvan De Launoit, and Didier Monté. "ASK-1 (apoptosis signal-regulating kinase 1) is a direct E2F target gene." Biochemical Journal 396, no. 3 (May 29, 2006): 547–56. http://dx.doi.org/10.1042/bj20051981.

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In the present study, we show that E2Fs (E2 promoter-binding factors) regulate the expression of ASK-1 (apoptosis signal-regulating kinase 1), which encodes a mitogen-activated protein kinase kinase kinase, also known as MAP3K5. Its mRNA expression is cell-cycle-regulated in human T98G cells released from serum starvation. Moreover, overexpression and RNA interference experiments support the requirement of endogenous E2F/DP (E2F dimerization partner) activity for ASK-1 expression. Characterization of the human ASK-1 promoter demonstrates that the −95/+11 region is critical for E2F-mediated up-regulation. Chromatin immunoprecipitation assays show that E2F1–E2F4 are bound in vivo to the ASK-1 promoter in cycling cells, probably through a non-consensus E2F-binding site located 12 bp upstream of the transcription start site. Mutation of this site completely abolishes the ASK-1 promoter response to E2Fs as well as the E2F1 binding in electrophoretic mobility-shift experiments. Our results indicate that E2Fs modulate the expression of ASK-1 and suggest that some of the cellular functions of ASK-1 may be under the control of E2F transcription factors. Moreover, the up-regulation of ASK-1 may also favour the p53-independent E2F1 apoptotic activity.

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14

Immanuel, Camille N., Bin Teng, Brittany Dong, Elizabeth M. Gordon, Joseph A. Kennedy, Charlean Luellen, Andreas Schwingshackl, Stephania A. Cormier, Elizabeth A. Fitzpatrick, and Christopher M. Waters. "Apoptosis signal-regulating kinase-1 promotes inflammasome priming in macrophages." American Journal of Physiology-Lung Cellular and Molecular Physiology 316, no. 3 (March 1, 2019): L418—L427. http://dx.doi.org/10.1152/ajplung.00199.2018.

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We previously showed that mice deficient in apoptosis signal-regulating kinase-1 (ASK1) were partially protected against ventilator-induced lung injury. Because ASK1 can promote both cell death and inflammation, we hypothesized that ASK1 activation regulates inflammasome-mediated inflammation. Mice deficient in ASK1 expression (ASK1−/−) exhibited significantly less inflammation and lung injury (as measured by neutrophil infiltration, IL-6, and IL-1β) in response to treatment with inhaled lipopolysaccharide (LPS) compared with wild-type (WT) mice. To determine whether this proinflammatory response was mediated by ASK1, we investigated inflammasome-mediated responses to LPS in primary macrophages and bone marrow-derived macrophages (BMDMs) from WT and ASK1−/− mice, as well as the mouse alveolar macrophage cell line MH-S. Cells were treated with LPS alone for priming or LPS followed by ATP for activation. When macrophages were stimulated with LPS followed by ATP to activate the inflammasome, we found a significant increase in secreted IL-1β from WT cells compared with ASK1-deficient cells. LPS priming stimulated an increase in NOD-like receptor 3 (NLRP3) and pro-IL-1β in WT BMDMs, but expression of NLRP3 was significantly decreased in ASK1−/− BMDMs. Subsequent ATP treatment stimulated an increase in cleaved caspase-1 and IL-1β in WT BMDMs compared with ASK1−/− BMDMs. Similarly, treatment of MH-S cells with LPS + ATP caused an increase in both cleaved caspase-1 and IL-1β that was diminished by the ASK-1 inhibitor NQDI1. These results demonstrate, for the first time, that ASK1 promotes inflammasome priming.

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15

Shan, Xiaoyin, Hongmei Wang, and Kenneth B. Margulies. "Apoptosis Signal-Regulating Kinase 1 Attenuates Atrial Natriuretic Peptide Secretion†." Biochemistry 47, no. 38 (September 23, 2008): 10041–48. http://dx.doi.org/10.1021/bi800972z.

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16

Cho, Sayeon, Hyung-Mun Ko, Jeong-Min Kim, Jung-A. Lee, Jae-Eun Park, Mi-Sun Jang, Sung Goo Park, Do Hee Lee, Seong-Eon Ryu, and Byoung-Chul Park. "Positive Regulation of Apoptosis Signal-regulating Kinase 1 by hD53L1." Journal of Biological Chemistry 279, no. 16 (February 4, 2004): 16050–56. http://dx.doi.org/10.1074/jbc.m305758200.

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17

Shan, Xiaoyin, Hongmei Wang, and Kenneth B. Margulies. "Apoptosis Signal-Regulating Kinase 1 Attenuates Atrial Natriuretic Peptide Secretion." Journal of Cardiac Failure 14, no. 6 (August 2008): S40. http://dx.doi.org/10.1016/j.cardfail.2008.06.285.

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18

Takeda, Kohsuke, Takuya Noguchi, Isao Naguro, and Hidenori Ichijo. "Apoptosis Signal-Regulating Kinase 1 in Stress and Immune Response." Annual Review of Pharmacology and Toxicology 48, no. 1 (February 2008): 199–225. http://dx.doi.org/10.1146/annurev.pharmtox.48.113006.094606.

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19

Kutuzov, Mikhail A., Alexandra V. Andreeva, and Tatyana A. Voyno‐Yasenetskaya. "Regulation of apoptosis signal‐regulating kinase 1 degradation by Gα13." FASEB Journal 21, no. 13 (June 26, 2007): 3727–36. http://dx.doi.org/10.1096/fj.06-8029com.

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20

Park, Hee-Sae, Ssang-Goo Cho, Chang Kyun Kim, Hyun Sub Hwang, Kyung Tae Noh, Mi-Sung Kim, Sung-Ho Huh, et al. "Heat Shock Protein Hsp72 Is a Negative Regulator of Apoptosis Signal-Regulating Kinase 1." Molecular and Cellular Biology 22, no. 22 (November 15, 2002): 7721–30. http://dx.doi.org/10.1128/mcb.22.22.7721-7730.2002.

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ABSTRACT Heat shock protein 72 (Hsp72) is thought to protect cells against cellular stress. The protective role of Hsp72 was investigated by determining the effect of this protein on the stress-activated protein kinase signaling pathways. Prior exposure of NIH 3T3 cells to mild heat shock (43°C for 20 min) resulted in inhibition of H2O2-induced activation of apoptosis signal-regulating kinase 1 (ASK1). Overexpression of Hsp72 also inhibited H2O2-induced activation of ASK1 as well as that of downstream kinases in the p38 mitogen-activated protein kinase (MAPK) signaling cascade. Recombinant Hsp72 bound directly to ASK1 and inhibited ASK1 activity in vitro. Furthermore, coimmunoprecipitation analysis revealed a physical interaction between endogenous Hsp72 and ASK1 in NIH 3T3 cells exposed to mild heat shock. Hsp72 blocked both the homo-oligomerization of ASK1 and ASK1-dependent apoptosis. Hsp72 antisense oligonucleotides prevented the inhibitory effects of mild heat shock on H2O2-induced ASK1 activation and apoptosis. These observations suggest that Hsp72 functions as an endogenous inhibitor of ASK1.

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21

Mochida, Yoshiyuki. "Functional Analysis of Apoptosis Signal-regulating Kinase 1(ASK-1)-Binding Proteins." JOURNAL OF THE STOMATOLOGICAL SOCIETY,JAPAN 67, no. 2 (2000): 182–92. http://dx.doi.org/10.5357/koubyou.67.182.

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22

Hsu, M. J., C. Y. Hsu, B. C. Chen, M. C. Chen, G. Ou, and C. H. Lin. "Apoptosis Signal-Regulating Kinase 1 in Amyloid Peptide-Induced Cerebral Endothelial Cell Apoptosis." Journal of Neuroscience 27, no. 21 (May 23, 2007): 5719–29. http://dx.doi.org/10.1523/jneurosci.1874-06.2007.

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23

Takizawa, Takenori, Chizuru Tatematsu, and Yoshinobu Nakanishi. "Double-stranded RNA-activated protein kinase interacts with apoptosis signal-regulating kinase 1." European Journal of Biochemistry 269, no. 24 (December 2002): 6126–32. http://dx.doi.org/10.1046/j.1432-1033.2002.03325.x.

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24

Saito, Jun-ichi, Shinnosuke Toriumi, Kenjiro Awano, Hidenori Ichijo, Keiichi Sasaki, Takayasu Kobayashi, and Shinri Tamura. "Regulation of apoptosis signal-regulating kinase 1 by protein phosphatase 2Cϵ." Biochemical Journal 405, no. 3 (July 13, 2007): 591–96. http://dx.doi.org/10.1042/bj20070231.

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ASK1 (apoptosis signal-regulating kinase 1), a MKKK (mitogen-activated protein kinase kinase kinase), is activated in response to cytotoxic stresses, such as H2O2 and TNFα (tumour necrosis factor α). ASK1 induction initiates a signalling cascade leading to apoptosis. After exposure of cells to H2O2, ASK1 is transiently activated by autophosphorylation at Thr845. The protein then associates with PP5 (protein serine/threonine phosphatase 5), which inactivates ASK1 by dephosphorylation of Thr845. Although this feedback regulation mechanism has been elucidated, it remains unclear how ASK1 is maintained in the dephosphorylated state under non-stressed conditions. In the present study, we have examined the possible role of PP2Cϵ (protein phosphatase 2Cϵ), a member of PP2C family, in the regulation of ASK1 signalling. Following expression in HEK-293 cells (human embryonic kidney cells), wild-type PP2Cϵ inhibited ASK1-induced activation of an AP-1 (activator protein 1) reporter gene. Conversely, a dominant-negative PP2Cϵ mutant enhanced AP-1 activity. Exogenous PP2Cϵ associated with exogenous ASK1 in HEK-293 cells under non-stressed conditions, inactivating ASK1 by decreasing Thr845 phosphorylation. The association of endogenous PP2Cϵ and ASK1 was also observed in mouse brain extracts. PP2Cϵ directly dephosphorylated ASK1 at Thr845in vitro. In contrast with PP5, PP2Cϵ transiently dissociated from ASK1 within cells upon H2O2 treatment. These results suggest that PP2Cϵ maintains ASK1 in an inactive state by dephosphorylation in quiescent cells, supporting the possibility that PP2Cϵ and PP5 play different roles in H2O2-induced regulation of ASK1 activity.

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25

Luo, Youguang, Siqi Gao, Ziwei Hao, Yang Yang, Songbo Xie, Dengwen Li, Min Liu, and Jun Zhou. "Apoptosis signal-regulating kinase 1 exhibits oncogenic activity in pancreatic cancer." Oncotarget 7, no. 46 (September 17, 2016): 75155–64. http://dx.doi.org/10.18632/oncotarget.12090.

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26

Xin, Zhili, Martin K. Himmelbauer, J. Howard Jones, Istvan Enyedy, Rab Gilfillan, Thomas Hesson, Kristopher King, et al. "Discovery of CNS-Penetrant Apoptosis Signal-Regulating Kinase 1 (ASK1) Inhibitors." ACS Medicinal Chemistry Letters 11, no. 4 (February 12, 2020): 485–90. http://dx.doi.org/10.1021/acsmedchemlett.9b00611.

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27

Choi, Jong-Ryoul, Hyejung Heo, Yoo Lang, Ki Soon Shin, and Shin Jung Kang. "Apoptosis signal-regulating kinase 1 regulates the expression of caspase-11." FEBS Letters 583, no. 18 (August 18, 2009): 3016–20. http://dx.doi.org/10.1016/j.febslet.2009.08.014.

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28

Jiang, C., L. Wen, C. Yin, W. Xu, C. Ding, B. Shi, X. Zhang, and W. Xie. "Apoptosis Signal-Regulating Kinase 1 Suppresses the Malignancy of Hepatocellular Carcinoma." Journal of Hepatology 64, no. 2 (2016): S559. http://dx.doi.org/10.1016/s0168-8278(16)01008-4.

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29

Dasgupta, Piyali, Vicki Betts, Shipra Rastogi, Bharat Joshi, Mark Morris, Brenda Brennan, Dalia Ordonez-Ercan, and Srikumar Chellappan. "Direct Binding of Apoptosis Signal-regulating Kinase 1 to Retinoblastoma Protein." Journal of Biological Chemistry 279, no. 37 (June 21, 2004): 38762–69. http://dx.doi.org/10.1074/jbc.m312273200.

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30

Zhang, Qian-Shi, Gregory J. Eaton, Carol Diallo, and Theresa A. Freeman. "Stress-Induced Activation of Apoptosis Signal-Regulating Kinase 1 Promotes Osteoarthritis." Journal of Cellular Physiology 231, no. 4 (September 29, 2015): 944–53. http://dx.doi.org/10.1002/jcp.25186.

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31

Anderson, P. "Kinase cascades regulating entry into apoptosis." Microbiology and Molecular Biology Reviews 61, no. 1 (March 1997): 33–46. http://dx.doi.org/10.1128/mmbr.61.1.33-46.1997.

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All cells are constantly exposed to conflicting environment cues that signal cell survival or cell death. Survival signals are delivered by autocrine or paracrine factors that actively suppress a default death pathway. In addition to survival factor withdrawal, cell death can be triggered by environmental stresses such as heat, UV light, and hyperosmolarity or by dedicated death receptors (e.g., FAS/APO-1 and tumor necrosis factor [TNF] receptors) that are counterparts of growth factor or survival receptors at the cell surface. One of the ways that cells integrate conflicting exogenous stimuli is by phosphorylation (or dephosphorylation) of cellular constituents by interacting cascades of serine/threonine and tyrosine protein kinases (and phosphatases). Survival factors (e.g., growth factors and mitogens) activate receptor tyrosine kinases and selected mitogen-activated, cyclin-dependent, lipid-activated, nucleic acid-dependent, and cyclic AMP-dependent kinases to promote cell survival and proliferation, whereas environmental stress (or death factors such as FAS/APO-1 ligand and TNF-alpha) activates different members of these kinase families to inhibit cell growth and, under some circumstances, promote apoptotic cell death. Because individual kinase cascades can interact with one another, they are able to integrate conflicting exogenous stimuli and provide a link between cell surface receptors and the biochemical pathways leading to cell proliferation or cell death.

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32

Kuo, Chen-Tzu, Bing-Chang Chen, Chung-Chi Yu, Chih-Ming Weng, Ming-Jen Hsu, Chien-Chih Chen, Mei-Chieh Chen, et al. "Apoptosis signal-regulating kinase 1 mediates denbinobin-induced apoptosis in human lung adenocarcinoma cells." Journal of Biomedical Science 16, no. 1 (2009): 43. http://dx.doi.org/10.1186/1423-0127-16-43.

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33

Jung, Haiyoung, Hyun-A. Seong, and Hyunjung Ha. "Murine Protein Serine/Threonine Kinase 38 Activates Apoptosis Signal-regulating Kinase 1 via Thr838Phosphorylation." Journal of Biological Chemistry 283, no. 50 (October 23, 2008): 34541–53. http://dx.doi.org/10.1074/jbc.m807219200.

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34

Yamaguchi, O., Y. Higuchi, S. Hirotani, K. Kashiwase, H. Nakayama, S. Hikoso, T. Takeda, et al. "Targeted deletion of apoptosis signal-regulating kinase 1 attenuates left ventricular remodeling." Proceedings of the National Academy of Sciences 100, no. 26 (December 9, 2003): 15883–88. http://dx.doi.org/10.1073/pnas.2136717100.

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35

Taniike, Masayuki, Osamu Yamaguchi, Ikuko Tsujimoto, Shungo Hikoso, Toshihiro Takeda, Atsuko Nakai, Shigemiki Omiya, et al. "Apoptosis Signal-Regulating Kinase 1/p38 Signaling Pathway Negatively Regulates Physiological Hypertrophy." Circulation 117, no. 4 (January 29, 2008): 545–52. http://dx.doi.org/10.1161/circulationaha.107.710434.

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36

Lee, Kang-Woo, Xin Zhao, Joo-Young Im, Hilary Grosso, Won Hee Jang, Teresa W. Chan, Patricia K. Sonsalla, et al. "Apoptosis Signal-Regulating Kinase 1 Mediates MPTP Toxicity and Regulates Glial Activation." PLoS ONE 7, no. 1 (January 10, 2012): e29935. http://dx.doi.org/10.1371/journal.pone.0029935.

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Sumbayev, Vadim V. "S-nitrosylation of thioredoxin mediates activation of apoptosis signal-regulating kinase 1." Archives of Biochemistry and Biophysics 415, no. 1 (July 2003): 133–36. http://dx.doi.org/10.1016/s0003-9861(03)00199-1.

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Nygaard, Gyrid, Julie A. Di Paolo, Deepa Hammaker, David L. Boyle, Grant Budas, Gregory T. Notte, Igor Mikaelian, Vivian Barry, and Gary S. Firestein. "Regulation and function of apoptosis signal-regulating kinase 1 in rheumatoid arthritis." Biochemical Pharmacology 151 (May 2018): 282–90. http://dx.doi.org/10.1016/j.bcp.2018.01.041.

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Izumi, Yasukatsu, Shokei Kim-Mitsuyama, Minoru Yoshiyama, Takashi Omura, Masayuki Shiota, Atsushi Matsuzawa, Tokihito Yukimura, et al. "Important Role of Apoptosis Signal-Regulating Kinase 1 in Ischemia-Induced Angiogenesis." Arteriosclerosis, Thrombosis, and Vascular Biology 25, no. 9 (September 2005): 1877–83. http://dx.doi.org/10.1161/01.atv.0000174801.76234.bd.

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Tesch, Greg H., Frank Y. Ma, and David J. Nikolic‐Paterson. "Targeting apoptosis signal‐regulating kinase 1 in acute and chronic kidney disease." Anatomical Record 303, no. 10 (January 23, 2020): 2553–60. http://dx.doi.org/10.1002/ar.24373.

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Tobiume, Kei, Toshihiko Inage, Kohsuke Takeda, Shoji Enomoto, Kohei Miyazono, and Hidenori Ichijo. "Molecular Cloning and Characterization of the Mouse Apoptosis Signal-Regulating Kinase 1." Biochemical and Biophysical Research Communications 239, no. 3 (October 1997): 905–10. http://dx.doi.org/10.1006/bbrc.1997.7580.

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Cho, Y.-C., J. E. Park, B. C. Park, J.-H. Kim, D. G. Jeong, S. G. Park, and S. Cho. "Cell cycle-dependent Cdc25C phosphatase determines cell survival by regulating apoptosis signal-regulating kinase 1." Cell Death & Differentiation 22, no. 10 (January 30, 2015): 1605–17. http://dx.doi.org/10.1038/cdd.2015.2.

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Harada, Chikako, Kazuaki Nakamura, Kazuhiko Namekata, Akinori Okumura, Yoshinori Mitamura, Yoko Iizuka, Kenji Kashiwagi, et al. "Role of Apoptosis Signal-Regulating Kinase 1 in Stress-Induced Neural Cell Apoptosis in Vivo." American Journal of Pathology 168, no. 1 (January 2006): 261–69. http://dx.doi.org/10.2353/ajpath.2006.050765.

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Ying, Wei-Zhong, Pei-Xuan Wang, and Paul W. Sanders. "Pivotal Role of Apoptosis Signal-Regulating Kinase 1 in Monoclonal Free Light Chain–Mediated Apoptosis." American Journal of Pathology 180, no. 1 (January 2012): 41–47. http://dx.doi.org/10.1016/j.ajpath.2011.09.017.

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Watanabe, Tetsuya, Kinya Otsu, Toshihiro Takeda, Osamu Yamaguchi, Shungo Hikoso, Kazunori Kashiwase, Yoshiharu Higuchi, et al. "Apoptosis signal-regulating kinase 1 is involved not only in apoptosis but also in non-apoptotic cardiomyocyte death." Biochemical and Biophysical Research Communications 333, no. 2 (July 2005): 562–67. http://dx.doi.org/10.1016/j.bbrc.2005.05.151.

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Watanabe, Tetsuya, Kinya Otsu, and Masatsugu Hori. "Apoptosis Signal-regulating Kinase 1 is Involved Not Only in Apoptosis But Also in Non-apoptotic Cardiomyocyte Death." Journal of Cardiac Failure 11, no. 9 (December 2005): S289. http://dx.doi.org/10.1016/j.cardfail.2005.08.209.

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Savira, Feby, Andrew R. Kompa, Ruth Magaye, Xin Xiong, Li Huang, Beat M. Jucker, Robert N. Willette, Darren J. Kelly, and Bing H. Wang. "Apoptosis signal-regulating kinase 1 inhibition reverses deleterious indoxyl sulfate-mediated endothelial effects." Life Sciences 272 (May 2021): 119267. http://dx.doi.org/10.1016/j.lfs.2021.119267.

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Patel, Pravin, Noor F. Shaik, Yuhang Zhou, Kalyan Golla, Steven E. McKenzie, and Ulhas P. Naik. "Apoptosis signal‐regulating kinase 1 regulates immune‐mediated thrombocytopenia, thrombosis, and systemic shock." Journal of Thrombosis and Haemostasis 18, no. 11 (September 9, 2020): 3013–28. http://dx.doi.org/10.1111/jth.15049.

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Sayama, Koji, Yasushi Hanakawa, Yuji Shirakata, Kenshi Yamasaki, Yasuhiro Sawada, Lin Sun, Kiyofumi Yamanishi, Hidenori Ichijo, and Koji Hashimoto. "Apoptosis Signal-regulating Kinase 1 (ASK1) Is an Intracellular Inducer of Keratinocyte Differentiation." Journal of Biological Chemistry 276, no. 2 (October 11, 2000): 999–1004. http://dx.doi.org/10.1074/jbc.m003425200.

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Takenaka, Satoshi, Takao Fujisawa, and Hidenori Ichijo. "Apoptosis signal-regulating kinase 1 (ASK1) as a therapeutic target for neurological diseases." Expert Opinion on Therapeutic Targets 24, no. 11 (September 30, 2020): 1061–64. http://dx.doi.org/10.1080/14728222.2020.1821648.

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