Cargando…

Ponatinib Activates an Inflammatory Response in Endothelial Cells via ERK5 SUMOylation

Ponatinib is a multi-targeted third generation tyrosine kinase inhibitor (TKI) used in the treatment of chronic myeloid leukemia (CML) patients harboring the Abelson (Abl)-breakpoint cluster region (Bcr) T315I mutation. In spite of having superb clinical efficacy, ponatinib triggers severe vascular...

Descripción completa

Detalles Bibliográficos
Autores principales:	Paez-Mayorga, Jesus, Chen, Andrew L., Kotla, Sivareddy, Tao, Yunting, Abe, Rei J., He, Emma D., Danysh, Brian P., Hofmann, Marie-Claude C., Le, Nhat-Tu
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Frontiers Media S.A. 2018
Materias:	Cardiovascular Medicine
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6135907/ https://www.ncbi.nlm.nih.gov/pubmed/30238007 http://dx.doi.org/10.3389/fcvm.2018.00125

Ejemplares similares

Ionizing Radiation Induces Endothelial Inflammation and Apoptosis via p90RSK-Mediated ERK5 S496 Phosphorylation
por: Vu, Hang Thi, et al.
Publicado: (2018)

p90RSK-MAGI1 Module Controls Endothelial Permeability by Post-translational Modifications of MAGI1 and Hippo Pathway
por: Abe, Rei J., et al.
Publicado: (2020)

Corrigendum: p90RSK-MAGI1 Module Controls Endothelial Permeability by Post-translational Modifications of MAGI1 and Hippo Pathway
por: Abe, Rei J., et al.
Publicado: (2021)

Senescence-Associated Secretory Phenotype as a Hinge Between Cardiovascular Diseases and Cancer
por: Banerjee, Priyanka, et al.
Publicado: (2021)

Reactive Oxygen Species, SUMOylation, and Endothelial Inflammation
por: Le, Nhat-Tu, et al.
Publicado: (2012)

Endothelial activation and fibrotic changes are impeded by laminar flow-induced CHK1-SENP2 activity through mechanisms distinct from endothelial-to-mesenchymal cell transition
por: Nguyen, Minh T. H., et al.
Publicado: (2023)

Metabolic regulation of endothelial senescence
por: Le, Nhat-Tu
Publicado: (2023)

Possible molecular mechanisms underlying the development of atherosclerosis in cancer survivors
por: Banerjee, Priyanka, et al.
Publicado: (2023)

The BCR-ABL1 Inhibitors Imatinib and Ponatinib Decrease Plasma Cholesterol and Atherosclerosis, and Nilotinib and Ponatinib Activate Coagulation in a Translational Mouse Model
por: Pouwer, Marianne G., et al.
Publicado: (2018)

p53 SUMOylation Mediates AOPP-Induced Endothelial Senescence and Apoptosis Evasion
por: Chen, Yanjia, et al.
Publicado: (2022)

MAGI1 inhibits interferon signaling to promote influenza A infection
por: Wang, Yin, et al.
Publicado: (2022)

PKCζ mediates disturbed flow-induced endothelial apoptosis via p53 SUMOylation
por: Heo, Kyung-Sun, et al.
Publicado: (2011)

Withdrawal: Reactive oxygen species (ROS) mediate p300-dependent STAT1 protein interaction with peroxisome proliferator-activated receptor (PPAR)-γ in CD36 protein expression and foam cell formation
por: Kotla, Sivareddy, et al.
Publicado: (2022)

SUMOylation as a Therapeutic Target for Myocardial Infarction
por: Zhao, Wei, et al.
Publicado: (2021)

Radiation therapy induces immunosenescence mediated by p90RSK
por: Imanishi, Masaki, et al.
Publicado: (2022)

Developing a Reliable Mouse Model for Cancer Therapy-Induced Cardiovascular Toxicity in Cancer Patients and Survivors
por: Ko, Kyung Ae, et al.
Publicado: (2018)

The significance of ERK5 catalytic-independent functions in disease pathways
por: Le, Nhat-Tu
Publicado: (2023)

Ponatinib‐induced ichthyosiform eruption
por: Kluger, Nicolas, et al.
Publicado: (2021)

ROS via BTK-p300-STAT1-PPARγ signaling activation mediates cholesterol crystals-induced CD36 expression and foam cell formation
por: Kotla, Sivareddy, et al.
Publicado: (2016)

Corrigendum to “ROS via BTK-p300-STAT1-PPARγ signaling activation mediates cholesterol crystals-induced CD36 expression and foam cell formation” [Redox Biol. 11 (2017) 350–364/513]
por: Kotla, Sivareddy, et al.
Publicado: (2022)

Eruptive melanocytic nevi associated with ponatinib
por: Devred, Inès, et al.
Publicado: (2018)

Ponatinib-Induced Cerebrovascular Accident (CVA)
por: Azad, Farhan, et al.
Publicado: (2022)

Reengineering Ponatinib to Minimize Cardiovascular Toxicity
por: Hnatiuk, Anna P., et al.
Publicado: (2022)

SUMOylation Is Required for ERK5 Nuclear Translocation and ERK5-Mediated Cancer Cell Proliferation
por: Erazo, Tatiana, et al.
Publicado: (2020)

Premature senescence and cardiovascular disease following cancer treatments: mechanistic insights
por: Jain, Ashita, et al.
Publicado: (2023)

Shp2 SUMOylation promotes ERK activation and hepatocellular carcinoma development
por: Deng, Rong, et al.
Publicado: (2015)

Cyclic AMP Response Element Binding Protein Mediates Pathological Retinal Neovascularization via Modulating DLL4-NOTCH1 Signaling
por: Singh, Nikhlesh K., et al.
Publicado: (2015)

PLCβ3 mediates cortactin interaction with WAVE2 in MCP1-induced actin polymerization and cell migration
por: Janjanam, Jagadeesh, et al.
Publicado: (2015)

Correction: Heterodimers of the transcriptional factors NFATc3 and FosB mediate tissue factor expression for 15(S)-hydroxyeicosatetraenoic acid-induced monocyte trafficking
por: Kotla, Sivareddy, et al.
Publicado: (2022)

Effects of Ketoconazole on the Pharmacokinetics of Ponatinib in Healthy Subjects
por: Narasimhan, Narayana I, et al.
Publicado: (2013)

Effects of food on the pharmacokinetics of ponatinib in healthy subjects
por: Narasimhan, NI, et al.
Publicado: (2013)

Ponatinib Combined With Rapamycin Causes Regression of Murine Venous Malformation
por: Li, Xian, et al.
Publicado: (2019)

SUMOylation of nuclear actin
por: Hofmann, Wilma A., et al.
Publicado: (2009)

Resistant mutations in CML and Ph(+)ALL – role of ponatinib
por: Miller, Geoffrey D, et al.
Publicado: (2014)

Ponatinib and other CML Tyrosine Kinase Inhibitors in Thrombosis
por: Zeng, Peng, et al.
Publicado: (2020)

A20/TNFAIP3 Increases ENOS Expression in an ERK5/KLF2-Dependent Manner to Support Endothelial Cell Health in the Face of Inflammation
por: Angolano, Cleide, et al.
Publicado: (2021)

SUMOylation of Grb2 enhances the ERK activity by increasing its binding with Sos1
por: Qu, Yingying, et al.
Publicado: (2014)

Disturbed flow: p53 SUMOylation in the turnover of endothelial cells
por: Takabe, Wakako, et al.
Publicado: (2011)

FGFR1 SUMOylation coordinates endothelial angiogenic signaling in angiogenesis
por: Zhu, Xiaolong, et al.
Publicado: (2022)

PML, SUMOylation, and Senescence
por: Ivanschitz, Lisa, et al.
Publicado: (2013)

Cannot write session to /tmp/vufind_sessions/sess_cvvmpn9365vs167d42j5hhagm0