Kinases and Cancer
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Gene Symbol Gene Description ACVR1B Activin a Receptor, Type IB
Table S1. Kinase clones included in human kinase cDNA library for yeast two-hybrid screening Gene Symbol Gene Description ACVR1B activin A receptor, type IB ADCK2 aarF domain containing kinase 2 ADCK4 aarF domain containing kinase 4 AGK multiple substrate lipid kinase;MULK AK1 adenylate kinase 1 AK3 adenylate kinase 3 like 1 AK3L1 adenylate kinase 3 ALDH18A1 aldehyde dehydrogenase 18 family, member A1;ALDH18A1 ALK anaplastic lymphoma kinase (Ki-1) ALPK1 alpha-kinase 1 ALPK2 alpha-kinase 2 AMHR2 anti-Mullerian hormone receptor, type II ARAF v-raf murine sarcoma 3611 viral oncogene homolog 1 ARSG arylsulfatase G;ARSG AURKB aurora kinase B AURKC aurora kinase C BCKDK branched chain alpha-ketoacid dehydrogenase kinase BMPR1A bone morphogenetic protein receptor, type IA BMPR2 bone morphogenetic protein receptor, type II (serine/threonine kinase) BRAF v-raf murine sarcoma viral oncogene homolog B1 BRD3 bromodomain containing 3 BRD4 bromodomain containing 4 BTK Bruton agammaglobulinemia tyrosine kinase BUB1 BUB1 budding uninhibited by benzimidazoles 1 homolog (yeast) BUB1B BUB1 budding uninhibited by benzimidazoles 1 homolog beta (yeast) C9orf98 chromosome 9 open reading frame 98;C9orf98 CABC1 chaperone, ABC1 activity of bc1 complex like (S. pombe) CALM1 calmodulin 1 (phosphorylase kinase, delta) CALM2 calmodulin 2 (phosphorylase kinase, delta) CALM3 calmodulin 3 (phosphorylase kinase, delta) CAMK1 calcium/calmodulin-dependent protein kinase I CAMK2A calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha CAMK2B calcium/calmodulin-dependent -
Mir-338-3P Functions As a Tumor Suppressor in Gastric Cancer by Targeting PTP1B
Sun et al. Cell Death and Disease DOI 10.1038/s41419-018-0611-0 Cell Death & Disease ARTICLE Open Access miR-338-3p functions as a tumor suppressor in gastric cancer by targeting PTP1B Feng Sun1, Mengchao Yu2,JingYu2, Zhijian Liu1,XinyanZhou2,YanqingLiu2, Xiaolong Ge3,HaidongGao2, Mei Li4, Xiaohong Jiang2,SongLiu1,XiChen2 and Wenxian Guan 1 Abstract Gastric cancer (GC) is one of the most common malignant tumors and peritoneal metastasis is the primary cause for advanced GC’s mortality. Protein-tyrosine phosphatase 1B (PTP1B) functions as an oncogene and involves in carcinogenesis and cancer dissemination. However, the function and regulation of PTP1B in GC remain poorly understood. In this study, we found that PTP1B was upregulated in GC tissues and overexpression of PTP1B in vitro promoted cell migration and prevented apoptosis. Then, we predicted that PTP1B was a target of miR-338-3p and we revealed an inverse correlation between miR-338-3p levels and PTP1B protein levels in GC tissues. Next, we verified that PTP1B was inhibited by miR-338-3p via direct targeting to its 3′-untranslated regions. Moreover, overexpression of miR-338-3p in vitro attenuated GC cell migration and promoted apoptosis, and these effects could be partially reversed by reintroduction of PTP1B. Finally, we established an orthotopic xenograft model and a peritoneal dissemination model of GC to demonstrate that miR-338-3p restrained tumor growth and dissemination in vivo by targeting PTP1B. Taken together, our results highlight that PTP1B is an oncogene and is negatively regulated by miR- 1234567890():,; 1234567890():,; 338-3p in GC, which may provide new insights into novel molecular therapeutic targets for GC. -
Protein Kinase D1 Regulates Hypoxic Metabolism Through HIF-1Α and Glycolytic Enzymes Incancer Cells
ONCOLOGY REPORTS 40: 1073-1082, 2018 Protein kinase D1 regulates hypoxic metabolism through HIF-1α and glycolytic enzymes incancer cells JIAO CHEN*, BOMIAO CUI*, YAPING FAN*, XIAOYING LI, QIAN LI, YUE DU, YUN FENG and PING ZHANG State Key Laboratory of Oral Diseases, West China Hospital of Stomatology, Sichuan University, Chengdu, Sichuan 610041, P.R. China Received October 7, 2017; Accepted April 3, 2018 DOI: 10.3892/or.2018.6479 Abstract. Protein kinase D1 (PKD1), one of the protein Introduction kinase D (PKD) family members, plays a prominent role in multiple bio-behaviors of cancer cells. Low pH and hypoxia Oral cancer is a major public health issue and a social chal- are unique characteristics of the tumor microenvironment. lenge. Tongue squamous cell carcinoma (TSCC) is the most The aim of this study was to investigate the role and mecha- aggressive type of oral cancer. Environmental factors, genetics nism of PKD1 in regulating metabolism in the human tongue and immune status have been confirmed to be related to the squamous cell carcinoma (TSCC) cell line SCC25 under a tumorigenesis of tongue cancer (1). The tumor microenviron- hypoxic condition, as well as growth and apoptosis. Here, we ment, which is composed of complex components including found that hypoxia not only induced the expression of HIF-1α, stem cells, fibroblasts, immune cells and their secreted factors, but also induced the expression and activation of PKD1. is critical to the initiation, development and maintenance of Moreover, we inhibited the expression of PKD1 by shRNA tumorigenesis (1). As the ‘residence niche’ of cancer cells, the interference, and the growth of SCC25 cells under hypoxia was composition and structure of the tumor microenvironment significantly decreased, as well as the expression of HIF-1α, not only affects the bio-behavior, but also determines the while the percentage of apoptotic SCC25 cells was increased. -
A Novel Kinase Inhibitor Establishes a Predominant Role for Protein Kinase D As a Cardiac Class Iia Histone Deacetylase Kinase
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector FEBS Letters 584 (2010) 631–637 journal homepage: www.FEBSLetters.org A novel kinase inhibitor establishes a predominant role for protein kinase D as a cardiac class IIa histone deacetylase kinase Lauren Monovich a,*, Richard B. Vega a, Erik Meredith a, Karl Miranda a, Chang Rao a, Michael Capparelli a, Douglas D. Lemon b, Dillon Phan b, Keith A. Koch b, Joseph A. Chapo b, David B. Hood b, Timothy A. McKinsey b,* a Novartis Institutes for Biomedical Research, 3333 Walnut Street, Boulder, CO 80301, United States b Gilead Colorado, Inc., 3333 Walnut Street, Boulder, CO 80301, United States article info abstract Article history: Class IIa histone deacetylases (HDACs) repress genes involved in pathological cardiac hypertrophy. Received 13 November 2009 The anti-hypertrophic action of class IIa HDACs is overcome by signals that promote their phosphor- Revised 8 December 2009 ylation-dependent nuclear export. Several kinases have been shown to phosphorylate class IIa Accepted 11 December 2009 HDACs, including calcium/calmodulin-dependent protein kinase (CaMK), protein kinase D (PKD) Available online 14 December 2009 and G protein-coupled receptor kinase (GRK). However, the identity of the kinase(s) responsible Edited by Ivan Sadowski for phosphorylating class IIa HDACs during cardiac hypertrophy has remained controversial. We describe a novel and selective small molecule inhibitor of PKD, bipyridyl PKD inhibitor (BPKDi). BPKDi blocks signal-dependent phosphorylation and nuclear export of class IIa HDACs in cardio- Keywords: Kinase myocytes and concomitantly suppresses hypertrophy of these cells. -
Ponatinib Shows Potent Antitumor Activity in Small Cell Carcinoma of the Ovary Hypercalcemic Type (SCCOHT) Through Multikinase Inhibition Jessica D
Published OnlineFirst February 9, 2018; DOI: 10.1158/1078-0432.CCR-17-1928 Cancer Therapy: Preclinical Clinical Cancer Research Ponatinib Shows Potent Antitumor Activity in Small Cell Carcinoma of the Ovary Hypercalcemic Type (SCCOHT) through Multikinase Inhibition Jessica D. Lang1,William P.D. Hendricks1, Krystal A. Orlando2, Hongwei Yin1, Jeffrey Kiefer1, Pilar Ramos1, Ritin Sharma3, Patrick Pirrotte3, Elizabeth A. Raupach1,3, Chris Sereduk1, Nanyun Tang1, Winnie S. Liang1, Megan Washington1, Salvatore J. Facista1, Victoria L. Zismann1, Emily M. Cousins4, Michael B. Major4, Yemin Wang5, Anthony N. Karnezis5, Aleksandar Sekulic1,6, Ralf Hass7, Barbara C. Vanderhyden8, Praveen Nair9, Bernard E. Weissman2, David G. Huntsman5,10, and Jeffrey M. Trent1 Abstract Purpose: Small cell carcinoma of the ovary, hypercalcemic type three SWI/SNF wild-type ovarian cancer cell lines. We further (SCCOHT) is a rare, aggressive ovarian cancer in young women identified ponatinib as the most effective clinically approved that is universally driven by loss of the SWI/SNF ATPase subunits RTK inhibitor. Reexpression of SMARCA4 was shown to confer SMARCA4 and SMARCA2. A great need exists for effective targeted a 1.7-fold increase in resistance to ponatinib. Subsequent therapies for SCCOHT. proteomic assessment of ponatinib target modulation in Experimental Design: To identify underlying therapeutic vul- SCCOHT cell models confirmed inhibition of nine known nerabilities in SCCOHT, we conducted high-throughput siRNA ponatinib target kinases alongside 77 noncanonical ponatinib and drug screens. Complementary proteomics approaches pro- targets in SCCOHT. Finally, ponatinib delayed tumor dou- filed kinases inhibited by ponatinib. Ponatinib was tested for bling time 4-fold in SCCOHT-1 xenografts while reducing efficacy in two patient-derived xenograft (PDX) models and one final tumor volumes in SCCOHT PDX models by 58.6% and cell-line xenograft model of SCCOHT. -
Hyperactive and Impulsive Behaviors of LMTK1 Knockout Mice
www.nature.com/scientificreports OPEN Hyperactive and impulsive behaviors of LMTK1 knockout mice Miyuki Takahashi1,7, Arika Sugiyama1, Ran Wei1, Shizuka Kobayashi2, Kimiko Fukuda3, Hironori Nishino1, Roka Takahashi1, Koji Tsutsumi1,8, Ichiro Kita4, Kanae Ando1, Toshiya Manabe2, Hiroyuki Kamiguchi5, Mineko Tomomura6 & Shin‑ichi Hisanaga1* Lemur tail kinase 1 (LMTK1), previously called Apoptosis‑Associated Tyrosine Kinase (AATYK), remains an uncharacterized Ser/Thr protein kinase that is predominantly expressed in the brain. It is recently reported that LMTK1A, an isoform of LMTK1, binds to recycling endosomes through its palmitoylation and regulates endosomal trafcking by suppressing the activity of Rab11 small GTPase. In neurons, knockdown or knockout of LMTK1 results in longer axons, greater branching of dendrites and increased number of spines, suggesting that LMTK1 plays a role in neuronal circuit formation. However, its in vivo function remained to be investigated. Here, we examined the brain structures and behaviors of LMTK1 knockout (KO) mice. LMTK1 was expressed in most neurons throughout the brain. The overall brain structure appeared to be normal in LMTK1 KO mice, but the numbers of synapses were increased. LMTK1 KO mice had a slight impairment in memory formation and exhibited distinct psychiatric behaviors such as hyperactivity, impulsiveness and high motor coordination without social interaction defcits. Some of these abnormal behaviors represent core features of attention defcit hyperactive disorder (ADHD), suggesting the possible involvement of LMTK1 in the pathogenesis of ADHD. Abbreviations AATYK1 Apoptosis-Associated Tyrosine Kinase ADHD Attention defcit hyperactive disorder Cx Cerebral cortex Cb Cerebellum CS Conditioned stimulus ISH In situ hybridization KO Knockout LMTK Lemur tail kinase PPF Paired-pulse facilitation US Unconditioned stimulus WT Wildtype Neuronal circuit wiring is the structural and functional basis of higher brain activities such as recognition and behaviors. -
1714 Gene Comprehensive Cancer Panel Enriched for Clinically Actionable Genes with Additional Biologically Relevant Genes 400-500X Average Coverage on Tumor
xO GENE PANEL 1714 gene comprehensive cancer panel enriched for clinically actionable genes with additional biologically relevant genes 400-500x average coverage on tumor Genes A-C Genes D-F Genes G-I Genes J-L AATK ATAD2B BTG1 CDH7 CREM DACH1 EPHA1 FES G6PC3 HGF IL18RAP JADE1 LMO1 ABCA1 ATF1 BTG2 CDK1 CRHR1 DACH2 EPHA2 FEV G6PD HIF1A IL1R1 JAK1 LMO2 ABCB1 ATM BTG3 CDK10 CRK DAXX EPHA3 FGF1 GAB1 HIF1AN IL1R2 JAK2 LMO7 ABCB11 ATR BTK CDK11A CRKL DBH EPHA4 FGF10 GAB2 HIST1H1E IL1RAP JAK3 LMTK2 ABCB4 ATRX BTRC CDK11B CRLF2 DCC EPHA5 FGF11 GABPA HIST1H3B IL20RA JARID2 LMTK3 ABCC1 AURKA BUB1 CDK12 CRTC1 DCUN1D1 EPHA6 FGF12 GALNT12 HIST1H4E IL20RB JAZF1 LPHN2 ABCC2 AURKB BUB1B CDK13 CRTC2 DCUN1D2 EPHA7 FGF13 GATA1 HLA-A IL21R JMJD1C LPHN3 ABCG1 AURKC BUB3 CDK14 CRTC3 DDB2 EPHA8 FGF14 GATA2 HLA-B IL22RA1 JMJD4 LPP ABCG2 AXIN1 C11orf30 CDK15 CSF1 DDIT3 EPHB1 FGF16 GATA3 HLF IL22RA2 JMJD6 LRP1B ABI1 AXIN2 CACNA1C CDK16 CSF1R DDR1 EPHB2 FGF17 GATA5 HLTF IL23R JMJD7 LRP5 ABL1 AXL CACNA1S CDK17 CSF2RA DDR2 EPHB3 FGF18 GATA6 HMGA1 IL2RA JMJD8 LRP6 ABL2 B2M CACNB2 CDK18 CSF2RB DDX3X EPHB4 FGF19 GDNF HMGA2 IL2RB JUN LRRK2 ACE BABAM1 CADM2 CDK19 CSF3R DDX5 EPHB6 FGF2 GFI1 HMGCR IL2RG JUNB LSM1 ACSL6 BACH1 CALR CDK2 CSK DDX6 EPOR FGF20 GFI1B HNF1A IL3 JUND LTK ACTA2 BACH2 CAMTA1 CDK20 CSNK1D DEK ERBB2 FGF21 GFRA4 HNF1B IL3RA JUP LYL1 ACTC1 BAG4 CAPRIN2 CDK3 CSNK1E DHFR ERBB3 FGF22 GGCX HNRNPA3 IL4R KAT2A LYN ACVR1 BAI3 CARD10 CDK4 CTCF DHH ERBB4 FGF23 GHR HOXA10 IL5RA KAT2B LZTR1 ACVR1B BAP1 CARD11 CDK5 CTCFL DIAPH1 ERCC1 FGF3 GID4 HOXA11 IL6R KAT5 ACVR2A -
Supplementary Table 1. in Vitro Side Effect Profiling Study for LDN/OSU-0212320. Neurotransmitter Related Steroids
Supplementary Table 1. In vitro side effect profiling study for LDN/OSU-0212320. Percent Inhibition Receptor 10 µM Neurotransmitter Related Adenosine, Non-selective 7.29% Adrenergic, Alpha 1, Non-selective 24.98% Adrenergic, Alpha 2, Non-selective 27.18% Adrenergic, Beta, Non-selective -20.94% Dopamine Transporter 8.69% Dopamine, D1 (h) 8.48% Dopamine, D2s (h) 4.06% GABA A, Agonist Site -16.15% GABA A, BDZ, alpha 1 site 12.73% GABA-B 13.60% Glutamate, AMPA Site (Ionotropic) 12.06% Glutamate, Kainate Site (Ionotropic) -1.03% Glutamate, NMDA Agonist Site (Ionotropic) 0.12% Glutamate, NMDA, Glycine (Stry-insens Site) 9.84% (Ionotropic) Glycine, Strychnine-sensitive 0.99% Histamine, H1 -5.54% Histamine, H2 16.54% Histamine, H3 4.80% Melatonin, Non-selective -5.54% Muscarinic, M1 (hr) -1.88% Muscarinic, M2 (h) 0.82% Muscarinic, Non-selective, Central 29.04% Muscarinic, Non-selective, Peripheral 0.29% Nicotinic, Neuronal (-BnTx insensitive) 7.85% Norepinephrine Transporter 2.87% Opioid, Non-selective -0.09% Opioid, Orphanin, ORL1 (h) 11.55% Serotonin Transporter -3.02% Serotonin, Non-selective 26.33% Sigma, Non-Selective 10.19% Steroids Estrogen 11.16% 1 Percent Inhibition Receptor 10 µM Testosterone (cytosolic) (h) 12.50% Ion Channels Calcium Channel, Type L (Dihydropyridine Site) 43.18% Calcium Channel, Type N 4.15% Potassium Channel, ATP-Sensitive -4.05% Potassium Channel, Ca2+ Act., VI 17.80% Potassium Channel, I(Kr) (hERG) (h) -6.44% Sodium, Site 2 -0.39% Second Messengers Nitric Oxide, NOS (Neuronal-Binding) -17.09% Prostaglandins Leukotriene, -
GAK and PRKCD Are Positive Regulators of PRKN-Independent
bioRxiv preprint doi: https://doi.org/10.1101/2020.11.05.369496; this version posted November 5, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. 1 GAK and PRKCD are positive regulators of PRKN-independent 2 mitophagy 3 Michael J. Munson1,2*, Benan J. Mathai1,2, Laura Trachsel1,2, Matthew Yoke Wui Ng1,2, Laura 4 Rodriguez de la Ballina1,2, Sebastian W. Schultz2,3, Yahyah Aman4, Alf H. Lystad1,2, Sakshi 5 Singh1,2, Sachin Singh 2,3, Jørgen Wesche2,3, Evandro F. Fang4, Anne Simonsen1,2* 6 1Division of Biochemistry, Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo 7 2Centre for Cancer Cell Reprogramming, Institute of Clinical Medicine, Faculty of Medicine, University of Oslo, N-0316, Oslo, Norway. 8 3Department of Molecular Cell Biology, The Norwegian Radium Hospital Montebello, N-0379, Oslo, Norway 9 4Department of Clinical Molecular Biology, University of Oslo and Akershus University Hospital, 1478 Lørenskog, Norway 10 11 Keywords: GAK, Cyclin G Associated Kinase, PRKCD, Protein Kinase C Delta, Mitophagy, DFP, 12 DMOG, PRKN 13 14 *Corresponding Authors: 15 [email protected] 16 [email protected] 17 bioRxiv preprint doi: https://doi.org/10.1101/2020.11.05.369496; this version posted November 5, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. -
The Apoptosis Associated Tyrosine Kinase Gene Is Frequently Hypermethylated in Human Cancer and Is Regulated by Epigenetic Mechanisms
www.impactjournals.com/Genes&Cancer Genes & Cancer, Vol. 5 (9-10), September 2014 The apoptosis associated tyrosine kinase gene is frequently hypermethylated in human cancer and is regulated by epigenetic mechanisms Tanja Haag1, Christina E. Herkt1, Sara K. Walesch1, Antje M. Richter1 and Reinhard H. Dammann1 1 Institute for Genetics; Justus-Liebig-University; Universities of Giessen and Marburg Lung Center, Member of the German Center for Lung Research; Giessen, Germany Correspondence to: Reinhard H. Dammann, email: [email protected] Keywords: AATK/ epigenetic regulation / DNA methylation/ human cancer/ tumor suppressor/ CTCF Received: July 30, 2014 Accepted: August 18, 2014 Published: August 19, 2014 This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. ABSTRACT: Epigenetic gene inactivation through promoter hypermethylation is an important aberration involved in the silencing of tumor-associated genes in cancer. Here we identified the apoptosis associated tyrosine kinase (AATK) as an epigenetically downregulated tumor related gene. We analyzed the epigenetic regulation of AATK in several human cancer cell lines and normal tissues by methylation and expression analysis. Hypermethylation of AATK was also analyzed in 25 primary lung tumors, 30 breast cancers and 24 matching breast tissues. In normal tissues the AATK CpG island promoter was unmethylated and AATK was expressed. Hypermethylation of AATK occurred frequently in 13 out of 14 (93%) human cancer cell lines. Methylation was reversed by 5-aza-2’-deoxycytidine treatment leading to re-expression of AATK in cancer cell lines. -
Circptk2 Suppresses the Progression of Gastric Cancer by Targeting Mir-196A-3P/AATK Axis
CircPTK2 Suppresses the Progression of Gastric Cancer by Targeting miR-196a-3p/AATK Axis Ling Gao The First Aliated Hospital of Soochow University Tingting Xia The First Aliated Hospital of Soochow University Mingde Qin Soochow University Xiaofeng Xue The First Aliated Hospital of Soochow University Linhua Jiang The First Aliated Hospital of Soochow University Xinguo Zhu ( [email protected] ) The First Aliated Hospital of Soochow University https://orcid.org/0000-0001-9686-6797 Primary research Keywords: Gastric cancer, circPTK2, miR-196a-3p, AATK Posted Date: June 8th, 2021 DOI: https://doi.org/10.21203/rs.3.rs-569952/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/20 Abstract Background Gastric cancer is a type of malignant tumor with high morbidity and mortality. It has been shown that circular RNAs (circRNAs) exert critical functions in gastric cancer progression via working as microRNA (miRNA) sponges to regulate gene expression. However, the role and potential molecular mechanism of circRNAs in gastric cancer remain largely unknown. Methods CircPTK2 (hsa_circ_0005273) was identied by bioinformatics analysis and validated by RT-qPCR assay. Bioinformatics prediction, dual-luciferase reporter and RNA pull down assays were used to determine the interaction between circPTK2, miR-196a-3p, AATK. Results The level of circPTK2 was markedly downregulated in gastric cancer tissues. Upregulation of circPTK2 suppressed the proliferation, migration and invasion of gastric cancer cells, while downregulation of circPTK2 exhibited opposite effects. Mechanically, circPTK2 could competitively bind to miR-196a-3p and prevent miR-196a-3p to reduce the expression of AATK. -
Deficiency of Antioxidative Paraoxonase 2 (Pon2) Leads to Increased Number of Phenotypic LT-Hscs and Disturbed Erythropoiesis
Hindawi Oxidative Medicine and Cellular Longevity Volume 2021, Article ID 3917028, 18 pages https://doi.org/10.1155/2021/3917028 Research Article Deficiency of Antioxidative Paraoxonase 2 (Pon2) Leads to Increased Number of Phenotypic LT-HSCs and Disturbed Erythropoiesis Lisa Spiecker ,1 Ines Witte ,1 Julia Mehlig ,1 Viral Shah ,2,3 Markus Meyerhöfer,2,3 Patricia S. Haehnel ,2,3 Victoria Petermann ,1 Andrea Schüler,2 Piyush More ,1 Nina Cabezas-Wallscheid ,4 Sven Horke ,1 Andrea Pautz ,1 Andreas Daiber ,5 Daniel Sasca ,2,3 Thomas Kindler ,2,3 and Hartmut Kleinert 1 1Department of Pharmacology, Johannes Gutenberg University Medical Center, Mainz, Germany 2Department of Hematology, Medical Oncology and Pneumology, University Medical Center, Mainz, Germany 3University Cancer Center of Mainz, Germany 4Max Planck Institute of Immunobiology and Epigenetics, 79108 Freiburg, Germany 5Department of Cardiology, Cardiology I, Johannes Gutenberg University Medical Center Mainz, Germany Correspondence should be addressed to Daniel Sasca; [email protected], Thomas Kindler; [email protected], and Hartmut Kleinert; [email protected] Received 29 June 2020; Revised 26 April 2021; Accepted 27 May 2021; Published 25 June 2021 Academic Editor: Liren Qian Copyright © 2021 Lisa Spiecker et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The publication of this article was funded by Max Planck. Background. Long-term hematopoietic stem cells (LT-HSCs) reside in bone marrow niches with tightly controlled reactive oxygen species (ROS) levels. ROS increase results into LT-HSC differentiation and stem cell exhaustion.