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Article ; Online: Tailored chromatin modulation to promote tissue regeneration.

Martinez-Redondo, Paloma / Izpisua Belmonte, Juan Carlos

Seminars in cell & developmental biology

2019 Volume 97, Page(s) 3–15

Abstract: Epigenetic regulation of gene expression is fundamental in the maintenance of cellular identity and the regulation of cellular plasticity during tissue repair. In fact, epigenetic modulation is associated with the processes of cellular de-differentiation, ...

Abstract	Epigenetic regulation of gene expression is fundamental in the maintenance of cellular identity and the regulation of cellular plasticity during tissue repair. In fact, epigenetic modulation is associated with the processes of cellular de-differentiation, proliferation, and re-differentiation that takes place during tissue regeneration. In here we explore the epigenetic events that coordinate tissue repair in lower vertebrates with high regenerative capacity, and in mammalian adult stem cells, which are responsible for the homeostasis maintenance of most of our tissues. Finally we summarize promising CRISPR-based editing technologies developed during the last years, which look as promising tools to not only study but also promote specific events during tissue regeneration.
MeSH term(s)	Chromatin/metabolism ; Epigenesis, Genetic/genetics ; Humans ; Regeneration/drug effects
Chemical Substances	Chromatin
Language	English
Publishing date	2019-05-02
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1312473-0
ISSN	1096-3634 ; 1084-9521
ISSN (online)	1096-3634
ISSN	1084-9521
DOI	10.1016/j.semcdb.2019.04.015
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Article: The diversity of histone versus nonhistone sirtuin substrates.

Martínez-Redondo, Paloma / Vaquero, Alejandro

Genes & cancer

2013 Volume 4, Issue 3-4, Page(s) 148–163

Abstract: The members of the Sir2 family, or sirtuins, are major regulators of the response to different types of stress. The members of the family have adapted to increasing complexities throughout evolution and have become diversified by increasing their number, ...

Abstract	The members of the Sir2 family, or sirtuins, are major regulators of the response to different types of stress. The members of the family have adapted to increasing complexities throughout evolution and have become diversified by increasing their number, specificity, and localization and acquiring novel functions. Sirtuins have been consistently implicated in the cross-talk between the genomic information and environment from the prokaryotes onward. Evidence suggests that in the transition to eukaryotes, histones became one of the basic and most conserved targets of the family, to the extent that in yeast and mammals, sirtuins were originally described as NAD(+)-dependent histone deacetylases and classified as class III histone deacetylases. A growing number of studies have determined that sirtuins also target a wide range of nonhistone proteins. Many of these targets are also directly or indirectly related to chromatin regulation. The number of targets has grown considerably in the last decade but has provoked an ill-founded discussion that neglects the importance of histones as sirtuin targets. In this review, we summarize our knowledge regarding the range of sirtuin targets described to date and discuss the different functional implications of histone and nonhistone targets throughout evolution.
Language	English
Publishing date	2013-01-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	2538519-7
ISSN	1947-6027 ; 1947-6019
ISSN (online)	1947-6027
ISSN	1947-6019
DOI	10.1177/1947601913483767
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Article ; Online: Methods to study the role of sirtuins in genome stability.

Martínez-Redondo, Paloma / Vaquero, Alejandro

Methods in molecular biology (Clifton, N.J.)

2013 Volume 1077, Page(s) 273–283

Abstract: One of the most important roles of Sirtuins is to ensure the maintenance of genome integrity under stress conditions. In this chapter, we provide a methodology to study this role of Sirtuins at two different levels: detection of genomic instability (with ...

Abstract	One of the most important roles of Sirtuins is to ensure the maintenance of genome integrity under stress conditions. In this chapter, we provide a methodology to study this role of Sirtuins at two different levels: detection of genomic instability (with the Neutral Comet Assay) and study of Sirtuin dynamics in chromatin under stress conditions (by isolating insoluble chromatin fractions).
MeSH term(s)	Animals ; Blotting, Western ; Cells, Cultured ; Chromatin/genetics ; Comet Assay/methods ; DNA Damage/genetics ; DNA Damage/radiation effects ; Fibroblasts/cytology ; Fibroblasts/metabolism ; Fibroblasts/radiation effects ; Genomic Instability ; Mice ; Mice, Knockout ; Sirtuins/physiology
Chemical Substances	Chromatin ; Sirtuins (EC 3.5.1.-)
Language	English
Publishing date	2013
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-62703-637-5_18
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Article ; Online: Elixir of Life: Thwarting Aging With Regenerative Reprogramming.

Beyret, Ergin / Martinez Redondo, Paloma / Platero Luengo, Aida / Izpisua Belmonte, Juan Carlos

Circulation research

2017 Volume 122, Issue 1, Page(s) 128–141

Abstract: All living beings undergo systemic physiological decline after ontogeny, characterized as aging. Modern medicine has increased the life expectancy, yet this has created an aged society that has more predisposition to degenerative disorders. Therefore, ... ...

Abstract	All living beings undergo systemic physiological decline after ontogeny, characterized as aging. Modern medicine has increased the life expectancy, yet this has created an aged society that has more predisposition to degenerative disorders. Therefore, novel interventions that aim to extend the healthspan in parallel to the life span are needed. Regeneration ability of living beings maintains their biological integrity and thus is the major leverage against aging. However, mammalian regeneration capacity is low and further declines during aging. Therefore, modalities that reinforce regeneration can antagonize aging. Recent advances in the field of regenerative medicine have shown that aging is not an irreversible process. Conversion of somatic cells to embryonic-like pluripotent cells demonstrated that the differentiated state and age of a cell is not fixed. Identification of the pluripotency-inducing factors subsequently ignited the idea that cellular features can be reprogrammed by defined factors that specify the desired outcome. The last decade consequently has witnessed a plethora of studies that modify cellular features including the hallmarks of aging in addition to cellular function and identity in a variety of cell types in vitro. Recently, some of these reprogramming strategies have been directly used in animal models in pursuit of rejuvenation and cell replacement. Here, we review these in vivo reprogramming efforts and discuss their potential use to extend the longevity by complementing or augmenting the regenerative capacity.
MeSH term(s)	Aging/genetics ; Aging/pathology ; Aging/physiology ; Animals ; Cellular Reprogramming/physiology ; Cellular Senescence/physiology ; Epigenesis, Genetic/physiology ; Humans ; Regeneration/physiology ; Regenerative Medicine/methods ; Regenerative Medicine/trends ; Rejuvenation/physiology
Language	English
Publishing date	2017-12-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.117.311866
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Article ; Online: A big step for SIRT7, one giant leap for Sirtuins… in cancer.

Martínez-Redondo, Paloma / Santos-Barriopedro, Irene / Vaquero, Alejandro

Cancer cell

2012 Volume 21, Issue 6, Page(s) 719–721

Abstract: Recently reporting in Nature, Barber et al. demonstrated that SIRT7 maintains critical features that define cancer cells by removing the acetylation mark on lysine 18 of histone H3. Interestingly, hypoacetylation of H3K18 has been described as a general ... ...

Abstract	Recently reporting in Nature, Barber et al. demonstrated that SIRT7 maintains critical features that define cancer cells by removing the acetylation mark on lysine 18 of histone H3. Interestingly, hypoacetylation of H3K18 has been described as a general marker of tumor prognosis and oncoviral transformation.
Language	English
Publishing date	2012-06-12
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	2078448-X
ISSN	1878-3686 ; 1535-6108
ISSN (online)	1878-3686
ISSN	1535-6108
DOI	10.1016/j.ccr.2012.05.028
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Zs.A 5650: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: In vivo partial reprogramming of myofibers promotes muscle regeneration by remodeling the stem cell niche.

Wang, Chao / Rabadan Ros, Ruben / Martinez-Redondo, Paloma / Ma, Zaijun / Shi, Lei / Xue, Yuan / Guillen-Guillen, Isabel / Huang, Ling / Hishida, Tomoaki / Liao, Hsin-Kai / Nuñez Delicado, Estrella / Rodriguez Esteban, Concepcion / Guillen-Garcia, Pedro / Reddy, Pradeep / Izpisua Belmonte, Juan Carlos

Nature communications

2021 Volume 12, Issue 1, Page(s) 3094

Abstract: Short-term, systemic expression of the Yamanaka reprogramming factors (Oct-3/4, Sox2, Klf4 and c-Myc [OSKM]) has been shown to rejuvenate aging cells and promote tissue regeneration in vivo. However, the mechanisms by which OSKM promotes tissue ... ...

Abstract	Short-term, systemic expression of the Yamanaka reprogramming factors (Oct-3/4, Sox2, Klf4 and c-Myc [OSKM]) has been shown to rejuvenate aging cells and promote tissue regeneration in vivo. However, the mechanisms by which OSKM promotes tissue regeneration are unknown. In this work, we focus on a specific tissue and demonstrate that local expression of OSKM, specifically in myofibers, induces the activation of muscle stem cells or satellite cells (SCs), which accelerates muscle regeneration in young mice. In contrast, expressing OSKM directly in SCs does not improve muscle regeneration. Mechanistically, expressing OSKM in myofibers regulates the expression of genes important for the SC microenvironment, including upregulation of p21, which in turn downregulates Wnt4. This is critical because Wnt4 is secreted by myofibers to maintain SC quiescence. Thus, short-term induction of the Yamanaka factors in myofibers may promote tissue regeneration by modifying the stem cell niche.
MeSH term(s)	Animals ; Cell Differentiation/genetics ; Cells, Cultured ; Cellular Reprogramming/genetics ; Female ; Gene Expression ; Kruppel-Like Transcription Factors/genetics ; Mice, Transgenic ; Myofibrils/metabolism ; Myofibrils/physiology ; Octamer Transcription Factor-3/genetics ; Proto-Oncogene Proteins c-myc/genetics ; Regeneration/genetics ; SOXB1 Transcription Factors/genetics ; Satellite Cells, Skeletal Muscle/cytology ; Satellite Cells, Skeletal Muscle/metabolism ; Stem Cell Niche ; Wnt4 Protein/genetics
Chemical Substances	GKLF protein ; Kruppel-Like Transcription Factors ; Octamer Transcription Factor-3 ; Proto-Oncogene Proteins c-myc ; SOXB1 Transcription Factors ; Wnt4 Protein
Language	English
Publishing date	2021-05-25
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-23353-z
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Article ; Online: Integration of CpG-free DNA induces de novo methylation of CpG islands in pluripotent stem cells.

Takahashi, Yuta / Wu, Jun / Suzuki, Keiichiro / Martinez-Redondo, Paloma / Li, Mo / Liao, Hsin-Kai / Wu, Min-Zu / Hernández-Benítez, Reyna / Hishida, Tomoaki / Shokhirev, Maxim Nikolaievich / Esteban, Concepcion Rodriguez / Sancho-Martinez, Ignacio / Belmonte, Juan Carlos Izpisua

Science (New York, N.Y.)

2017 Volume 356, Issue 6337, Page(s) 503–508

Abstract: CpG islands (CGIs) are primarily promoter-associated genomic regions and are mostly unmethylated within highly methylated mammalian genomes. The mechanisms by which CGIs are protected from de novo methylation remain elusive. Here we show that insertion ... ...

Abstract	CpG islands (CGIs) are primarily promoter-associated genomic regions and are mostly unmethylated within highly methylated mammalian genomes. The mechanisms by which CGIs are protected from de novo methylation remain elusive. Here we show that insertion of CpG-free DNA into targeted CGIs induces de novo methylation of the entire CGI in human pluripotent stem cells (PSCs). The methylation status is stably maintained even after CpG-free DNA removal, extensive passaging, and differentiation. By targeting the DNA mismatch repair gene
Language	English
Publishing date	2017--05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.aag3260
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Zs.A 27: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: SIRT7 promotes genome integrity and modulates non-homologous end joining DNA repair.

Vazquez, Berta N / Thackray, Joshua K / Simonet, Nicolas G / Kane-Goldsmith, Noriko / Martinez-Redondo, Paloma / Nguyen, Trang / Bunting, Samuel / Vaquero, Alejandro / Tischfield, Jay A / Serrano, Lourdes

The EMBO journal

2016 Volume 35, Issue 14, Page(s) 1488–1503

Abstract: Sirtuins, a family of protein deacetylases, promote cellular homeostasis by mediating communication between cells and environment. The enzymatic activity of the mammalian sirtuin SIRT7 targets acetylated lysine in the N-terminal tail of histone H3 ( ... ...

Abstract	Sirtuins, a family of protein deacetylases, promote cellular homeostasis by mediating communication between cells and environment. The enzymatic activity of the mammalian sirtuin SIRT7 targets acetylated lysine in the N-terminal tail of histone H3 (H3K18Ac), thus modulating chromatin structure and transcriptional competency. SIRT7 deletion is associated with reduced lifespan in mice through unknown mechanisms. Here, we show that SirT7-knockout mice suffer from partial embryonic lethality and a progeroid-like phenotype. Consistently, SIRT7-deficient cells display increased replication stress and impaired DNA repair. SIRT7 is recruited in a PARP1-dependent manner to sites of DNA damage, where it modulates H3K18Ac levels. H3K18Ac in turn affects recruitment of the damage response factor 53BP1 to DNA double-strand breaks (DSBs), thereby influencing the efficiency of non-homologous end joining (NHEJ). These results reveal a direct role for SIRT7 in DSB repair and establish a functional link between SIRT7-mediated H3K18 deacetylation and the maintenance of genome integrity.
MeSH term(s)	Animals ; DNA/metabolism ; DNA Damage ; DNA End-Joining Repair ; Mice, Inbred C57BL ; Mice, Knockout ; Sirtuins/metabolism
Chemical Substances	Sirt7 protein, mouse ; DNA (9007-49-2) ; Sirtuins (EC 3.5.1.-)
Language	English
Publishing date	2016-05-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.201593499
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Article ; Online: Loss of SIRT2 leads to axonal degeneration and locomotor disability associated with redox and energy imbalance.

Fourcade, Stéphane / Morató, Laia / Parameswaran, Janani / Ruiz, Montserrat / Ruiz-Cortés, Tatiana / Jové, Mariona / Naudí, Alba / Martínez-Redondo, Paloma / Dierssen, Mara / Ferrer, Isidre / Villarroya, Francesc / Pamplona, Reinald / Vaquero, Alejandro / Portero-Otín, Manel / Pujol, Aurora

Aging cell

2017 Volume 16, Issue 6, Page(s) 1404–1413

Abstract: Sirtuin 2 (SIRT2) is a member of a family of ... ...

Abstract	Sirtuin 2 (SIRT2) is a member of a family of NAD
MeSH term(s)	Aging/metabolism ; Aging/pathology ; Animals ; Axons/metabolism ; Axons/pathology ; Cognition/physiology ; DNA, Mitochondrial/genetics ; DNA, Mitochondrial/metabolism ; Energy Metabolism ; Locomotion/physiology ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Oxidation-Reduction ; Sirtuin 2/deficiency ; Sirtuin 2/metabolism
Chemical Substances	DNA, Mitochondrial ; Sirt2 protein, mouse (EC 3.5.1.-) ; Sirtuin 2 (EC 3.5.1.-)
Language	English
Publishing date	2017-10-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2113083-8
ISSN	1474-9726 ; 1474-9718
ISSN (online)	1474-9726
ISSN	1474-9718
DOI	10.1111/acel.12682
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Article ; Online: Activation-induced cytidine deaminase targets SUV4-20-mediated histone H4K20 trimethylation to class-switch recombination sites.

Rodríguez-Cortez, Virginia C / Martínez-Redondo, Paloma / Català-Moll, Francesc / Rodríguez-Ubreva, Javier / Garcia-Gomez, Antonio / Poorani-Subramani, Ganesh / Ciudad, Laura / Hernando, Henar / Pérez-García, Arantxa / Company, Carlos / Urquiza, José M / Ramiro, Almudena R / Di Noia, Javier M / Vaquero, Alejandro / Ballestar, Esteban

Scientific reports

2017 Volume 7, Issue 1, Page(s) 7594

Abstract: Activation-induced cytidine deaminase (AID) triggers antibody diversification in B cells by catalysing deamination and subsequently mutating immunoglobulin (Ig) genes. Association of AID with RNA Pol II and occurrence of epigenetic changes during Ig gene ...

Abstract	Activation-induced cytidine deaminase (AID) triggers antibody diversification in B cells by catalysing deamination and subsequently mutating immunoglobulin (Ig) genes. Association of AID with RNA Pol II and occurrence of epigenetic changes during Ig gene diversification suggest participation of AID in epigenetic regulation. AID is mutated in hyper-IgM type 2 (HIGM2) syndrome. Here, we investigated the potential role of AID in the acquisition of epigenetic changes. We discovered that AID binding to the IgH locus promotes an increase in H4K20me3. In 293F cells, we demonstrate interaction between co-transfected AID and the three SUV4-20 histone H4K20 methyltransferases, and that SUV4-20H1.2, bound to the IgH switch (S) mu site, is replaced by SUV4-20H2 upon AID binding. Analysis of HIGM2 mutants shows that the AID truncated form W68X is impaired to interact with SUV4-20H1.2 and SUV4-20H2 and is unable to bind and target H4K20me3 to the Smu site. We finally show in mouse primary B cells undergoing class-switch recombination (CSR) that AID deficiency associates with decreased H4K20me3 levels at the Smu site. Our results provide a novel link between SUV4-20 enzymes and CSR and offer a new aspect of the interplay between AID and histone modifications in setting the epigenetic status of CSR sites.
MeSH term(s)	Animals ; B-Lymphocytes/drug effects ; B-Lymphocytes/immunology ; B-Lymphocytes/pathology ; Binding Sites ; Cell Line, Tumor ; Cytidine Deaminase/genetics ; Cytidine Deaminase/immunology ; Epigenesis, Genetic/immunology ; Gene Expression Regulation ; HEK293 Cells ; HeLa Cells ; Histone-Lysine N-Methyltransferase/genetics ; Histone-Lysine N-Methyltransferase/immunology ; Histones/genetics ; Histones/immunology ; Humans ; Hyper-IgM Immunodeficiency Syndrome/genetics ; Hyper-IgM Immunodeficiency Syndrome/immunology ; Hyper-IgM Immunodeficiency Syndrome/pathology ; Immunoglobulin Class Switching/genetics ; Immunoglobulin G/genetics ; Lipopolysaccharides/pharmacology ; Lymphocyte Activation/drug effects ; Mice ; Mice, Inbred C57BL ; Models, Biological ; Mutation ; Protein Binding ; RNA Polymerase II/genetics ; RNA Polymerase II/immunology ; Signal Transduction
Chemical Substances	Histones ; Immunoglobulin G ; Lipopolysaccharides ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; KMT5C protein, human (EC 2.1.1.43) ; RNA Polymerase II (EC 2.7.7.-) ; AICDA (activation-induced cytidine deaminase) (EC 3.5.4.-) ; Cytidine Deaminase (EC 3.5.4.5)
Language	English
Publishing date	2017-08-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-017-07380-9
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