SIRT1 Controls Endothelial Angiogenic Functions During Vascular Growth
Open accessAbstract
The nicotinamide adenine dinucleotide (NAD(+))-dependent histone deacetylase Sir2 regulates life-span in various species. Mammalian homologs of Sir2 are called sirtuins (SIRT1-SIRT7). In an effort to define the role of sirtuins in vascular homeostasis, we found that among the SIRT family, SIRT1 uniquely regulates angiogenesis signaling. We show that SIRT1 is highly expressed in the vasculature during blood vessel growth, where it controls the angiogenic activity of endothelial cells. Loss of SIRT1 function blocks sprouting angiogenesis and branching morphogenesis of endothelial cells with consequent down-regulation of genes involved in blood vessel development and vascular remodeling. Disruption of SIRT1 gene expression in zebrafish and mice results in defective blood vessel formation and blunts ischemia-induced neovascularization. Through gain- and loss-of-function approaches, we show that SIRT1 associates with and deacetylates the forkhead transcription factor Foxo1, an essential negative regulator of blood vessel development to restrain its anti-angiogenic activity. These findings uncover a novel and unexpected role for SIRT1 as a critical modulator of endothelial gene expression governing postnatal vascular growth.
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Sirtuin-1 plays an essential role in regulation of angiogenesis, a protective role against oxidative stress and cardiovascular disease, and higher expression levels of sirtuin-1 are associated with reducing disease.
“Sirtuin-1 plays an essential role in the regulation of angiogenesis, a protective role against oxidative stress and cardiovascular disease and higher expression levels of sirtuin-1 are associated with reducing disease (176–178).”
From A Critical Review of the Evidence That Metformin Is a Putative Anti-Aging Drug That Enhances Healthspan and Extends Lifespan (2021) · cites this paper as [177]
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Cites
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756 · see citing works
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679 · see citing works
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510 · see citing works
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239 · see citing works
Self-citationNutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160 · see citing works
Histone deacetylases (HDACs): characterization of the classical HDAC family
RUIJTER, A. J. M. D., GENNIP, A. H. V., CARON, H. N., KEMP, S., & KUILENBURG, A. B. P. V. (2003) · Biochemical Journal · doi:10.1042/bj20021321 · Cited by 3,114 · see citing works
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,653 · see citing works
In Vivo Imaging of Embryonic Vascular Development Using Transgenic Zebrafish
Lawson, N. D., & Weinstein, B. M. (2002) · Developmental Biology · doi:10.1006/dbio.2002.0711 · Cited by 2,160 · see citing works
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081 · see citing works
Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943 · see citing works
The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase
North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542 · see citing works
The Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,496 · see citing works
Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409 · see citing works
Mammalian SIRT1 Represses Forkhead Transcription Factors
Motta, M. C., Divecha, N., Lemieux, M. E., Kamel, C., Chen, D., Gu, W. J., Bultsma, Y., McBurney, M. W., & Guarente, L. (2004) · Cell · doi:10.1016/s0092-8674(04)00126-6 · Cited by 1,358 · see citing works
FOXO transcription factors at the interface between longevity and tumor suppression
Greer, E. L., & Brunet, A. (2005) · Oncogene · doi:10.1038/sj.onc.1209086 · Cited by 1,306 · see citing works
Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
Cheng, H.-L., Mostoslavsky, R., Saito, S., Manis, J. P., Gu, Y., Patel, P., Bronson, R., Appella, E., Alt, F. W., & Chua, K. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934713100 · Cited by 1,095 · see citing works
Self-citationFoxOs are lineage-restricted redundant tumor suppressors and regulate endothelial cell homeostasis
Paik, J.-H., Kollipara, R., Chu, G., Ji, H., Xiao, Y., Ding, Z., Miao, L., Tothova, Z., Horner, J. W., Carrasco, D. R., et al. (2007) · Cell · doi:10.1016/j.cell.2006.12.029 · Cited by 1,032 · see citing works
Calorie restriction, SIRT1 and metabolism: understanding longevity
Bordone, L., & Guarente, L. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1616 · Cited by 1,021 · see citing works
Signaling to Chromatin through Histone Modifications
Cheung, P., Allis, C. D., & Sassone-Corsi, P. (2000) · Cell · doi:10.1016/s0092-8674(00)00118-5 · Cited by 989 · see citing works
Human SIR2 deacetylates p53 and antagonizes PML/p53‐induced cellular senescence
Langley, E., Pearson, M., Faretta, M., Bauer, U., Frye, R. A., Minucci, S., Pelicci, P. G., & Kouzarides, T. (2002) · The EMBO Journal · doi:10.1093/emboj/21.10.2383 · Cited by 859 · see citing works
Calorie restriction–the SIR2 connection
Guarente, L., & Picard, F. (2005) · Cell · doi:10.1016/j.cell.2005.01.029 · Cited by 793 · see citing works
Endothelial cell diversity revealed by global expression profiling
Chi, J., Chang, H. Y., Haraldsen, G., Jahnsen, F. L., Troyanskaya, O. G., Chang, D. S., Wang, Z., Rockson, S. G., van de Rijn, M., Botstein, D., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1434429100 · Cited by 773 · see citing works
Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes
Kim, M. S., Kwon, H. J., Lee, Y. M., Baek, J. H., Jang, J.-E., Lee, S.-W., Moon, E.-J., Kim, H.-S., Lee, S., Chung, H. Y., et al. (2001) · Nature Medicine · doi:10.1038/86507 · Cited by 732 · see citing works
Smith, J. S., Brachmann, C. B., Celic, I., Kenna, M. A., Muhammad, S., Starai, V. J., Avalos, J. L., Escalante-Semerena, J. C., Grubmeyer, C., Wolberger, C., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.12.6658 · Cited by 718 · see citing works
Matrix Metalloproteinases Regulate Neovascularization by Acting as Pericellular Fibrinolysins
Hiraoka, N., Allen, E. D., Apel, I. J., Gyetko, M. R., & Weiss, S. J. (1998) · Cell · doi:10.1016/s0092-8674(00)81768-7 · Cited by 711 · see citing works
Hosaka, T., Biggs, W., Tieu, D. D., Boyer, A. D., Varki, N. M., Cavenee, W. K., & Arden, K. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400093101 · Cited by 684 · see citing works
The Notch target genes Hey1 and Hey2 are required for embryonic vascular developmentPreprint
Fischer, A., Schumacher, N., Maier, M., Sendtner, M., & Gessler, M. (2004) · Genes & Development · doi:10.1101/gad.291004 · Cited by 651 · see citing works
Daitoku, H., Hatta, M., Matsuzaki, H., Aratani, S., Ohshima, T., Miyagishi, M., Nakajima, T., & Fukamizu, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400593101 · Cited by 602 · see citing works
Sir2 Regulates Skeletal Muscle Differentiation as a Potential Sensor of the Redox State
Fulco, M., Schiltz, R. L., Iezzi, S., King, M. T., Zhao, P., Kashiwaya, Y., Hoffman, E. P., Veech, R. L., & Sartorelli, V. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00226-0 · Cited by 590 · see citing works
Sirtuins: Sir2-related NAD-dependent protein deacetylases.
North, B. J., & Verdin, E. M. (2004) · Genome biology · doi:10.1186/gb-2004-5-5-224 · Cited by 568 · see citing works
Frescas, D., Valenti, L. N., & Accili, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412357200 · Cited by 554 · see citing works
FOXO4 Is Acetylated upon Peroxide Stress and Deacetylated by the Longevity Protein hSir2
van der Horst, A., Tertoolen, L. G. J., Smits, L. M. M., Frye, R. A., Medema, R. H., & Burgering, B. M. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401138200 · Cited by 545 · see citing works
Involvement of Foxo transcription factors in angiogenesis and postnatal neovascularization
Potente, M., Urbich, C., Sasaki, K., Hofmann, W. K., Heeschen, C., Aicher, A., Kollipara, R., DePinho, R. A., Zeiher, A. M., & Dimmeler, S. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23126 · Cited by 531 · see citing works
Self-citationConditional Vascular Cell Adhesion Molecule 1 Deletion in Mice
Koni, P. A., Joshi, S. K., Temann, U.-A., Olson, D. L., Burkly, L. C., & Flavell, R. A. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.6.741 · Cited by 482 · see citing works
Histone Deacetylase 7 Maintains Vascular Integrity by Repressing Matrix Metalloproteinase 10
Chang, S., Young, B. D., Li, S., Qi, X., Richardson, J. A., & Olson, E. N. (2006) · Cell · doi:10.1016/j.cell.2006.05.040 · Cited by 454 · see citing works
Deroanne, C. F., Bonjean, K., Servotte, S., Devy, L., Colige, A., Clausse, N., Blacher, S., Verdin, E., Foidart, J.-M., Nusgens, B. V., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1205108 · Cited by 400 · see citing works
Lysine acetylation and the bromodomain: a new partnership for signaling
Yang, X. (2004) · BioEssays · doi:10.1002/bies.20104 · Cited by 359 · see citing works
The interaction between FOXO and SIRT1: tipping the balance towards survival
Giannakou, M. E., & Partridge, L. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.07.006 · Cited by 354 · see citing works
Suppression of FOXO1 activity by FHL2 through SIRT1‐mediated deacetylation
Yang, Y., Hou, H., Haller, E. M., Nicosia, S. V., & Bai, W. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600570 · Cited by 348 · see citing works
Abnormal Angiogenesis in Foxo1 (Fkhr)-deficient Mice
Furuyama, T., Kitayama, K., Shimoda, Y., Ogawa, M., Sone, K., Yoshida-Araki, K., Hisatsune, H., Nishikawa, S.-I., Nakayama, K., Nakayama, K., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314214200 · Cited by 341 · see citing works
Fleming, I., Fißlthaler, B., Dixit, M., & Busse, R. (2005) · Journal of Cell Science · doi:10.1242/jcs.02541 · Cited by 328 · see citing works
Daly, C., Wong, V., Burova, E., Wei, Y., Zabski, S. M., Griffiths, J., Lai, K. V., Lin, H. C., Ioffe, E., Yancopoulos, G. D., et al. (2004) · Genes & Development · doi:10.1101/gad.1189704 · Cited by 326 · see citing works
Mammalian SIRT1 limits replicative life span in response to chronic genotoxic stress
Chua, K. F., Mostoslavsky, R., Lombard, D. B., Pang, W. W., Saito, S., Franco, S., Kaushal, D., Cheng, H.-L., Fischer, M. R., Stokes, N., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.06.007 · Cited by 257 · see citing works
Self-citationRole of NAD+ in the Deacetylase Activity of the SIR2-like Proteins
Landry, J. W., Slama, J. T., & Sternglanz, R. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3854 · Cited by 254 · see citing works
Rössig, L., Li, H., Fißlthaler, B., Urbich, C., Fleming, I., Förstermann, U., Zeiher, A. M., & Dimmeler, S. (2002) · Circulation Research · doi:10.1161/01.res.0000037983.07158.b1 · Cited by 197 · see citing works
Self-citationIlli, B., Scopece, A., Nanni, S., Farsetti, A., Morgante, L., Biglioli, P., Capogrossi, M. C., & Gaetano, C. (2005) · Circulation Research · doi:10.1161/01.res.0000159181.06379.63 · Cited by 189 · see citing works
Yana, I., Sagara, H., Τακακι, S., Takatsu, K., Nakamura, K., Nakao, K., Katsuki, M., Taniguchi, S.-I., Aoki, T., Sato, H., et al. (2007) · Journal of Cell Science · doi:10.1242/jcs.000679 · Cited by 185 · see citing works
Rössig, L., Urbich, C., Brühl, T., Dernbach, E., Heeschen, C., Chavakis, E., Sasaki, K., Aicher, D., Diehl, F., Seeger, F. H., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20042097 · Cited by 163 · see citing works
Self-citationTakata, T., & Ishikawa, F. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)03020-6 · Cited by 159 · see citing works
Illi, B., Nanni, S., Scopece, A., Farsetti, A., Biglioli, P., Capogrossi, M. C., & Gaetano, C. (2003) · Circulation Research · doi:10.1161/01.res.0000080933.82105.29 · Cited by 133 · see citing works
Rosenberg, M. I., & Parkhurst, S. M. (2002) · Cell · doi:10.1016/s0092-8674(02)00732-8 · Cited by 118 · see citing works
Conserved and divergent patterns of Reelin expression in the zebrafish central nervous system
Costagli, A., Kapsimali, M., Wilson, S. W., & Mione, M. (2002) · The Journal of Comparative Neurology · doi:10.1002/cne.10292 · Cited by 83 · see citing works
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Research works printed but not linked: 1
- Smith, J.S., Brachmann, C.B., Celic, I., Kenna, M.A., Muham- mad, S., Starai, V.J., Avalos, J.L., Escalante-Semerena, J.C., Grubmeyer, C., Wolberger, C., et al. 2000. A phylogeneti- cally conserved NAD + -dependent protein deacetylase activ- ity in the Sir2 protein family. Proc. Natl. Acad. Sci. 97: 6658-6663.
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North, B. J., & Sinclair, D. A. (2012) · Circulation Research · doi:10.1161/circresaha.111.246876 · Cited by 1,585 · see citing works
Kinaan, M., Ding, H., & Triggle, C. R. (2015) · Medical Principles and Practice · doi:10.1159/000381643 · Cited by 1,515 · see citing works
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Das, A., Huang, G. X., Bonkowski, M. S., Longchamp, A., Li, C., Schultz, M. B., Kim, L.-J., Osborne, B., Joshi, S., Lu, Y., et al. (2018) · Cell · doi:10.1016/j.cell.2018.02.008 · Cited by 496 · see citing works
“In young muscle, SIRT1 is required for ischemia-induced neovascularization (Potente et al., 2007), vascular relaxation 74 Cell 173, 74–89, March 22, 2018 ª 2018 Elsevier Inc. (Mattagajasingh et al., 2007; Pearson et al., 2008; Ungvari et al., 2010), and is implicated in EC senescence (Ota et al.,…”
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AMPK and the biochemistry of exercise: implications for human health and disease
Richter, E. A., & Ruderman, N. B. (2009) · Biochemical Journal · doi:10.1042/bj20082055 · Cited by 481 · see citing works
Calorie restriction and sirtuins revisited
Guarente, L. (2013) · Genes & Development · doi:10.1101/gad.227439.113 · Cited by 464 · see citing works
Mammalian Sirt1: insights on its biological functions
Rahman, S., & Islam, R. (2011) · Cell Communication and Signaling · doi:10.1186/1478-811x-9-11 · Cited by 362 · see citing works
Zu, Y., Liu, L., Lee, M. Y. K., Xu, C., Liang, Y., Man, R. Y., Vanhoutte, P. M., & Wang, Y. (2010) · Circulation Research · doi:10.1161/circresaha.109.215483 · Cited by 303 · see citing works
Mohammed, I., Hollenberg, M. D., Ding, H., & Triggle, C. R. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.718942 · Cited by 278 · see citing works
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Chen, H.-Z., Wang, F., Gao, P., Pei, J.-F., Liu, Y., Xu, T.-T., Tang, X., Fu, W.-Y., Lu, J., Yan, Y.-F., et al. (2016) · Circulation Research · doi:10.1161/circresaha.116.308895 · Cited by 265 · see citing works
Arunachalam, G., Samuel, S. M., Marei, I., Ding, H., & Triggle, C. R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12496 · Cited by 221 · see citing works
Han, Y., & Kim, S. Y. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00906-w · Cited by 201 · see citing works
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- Authors
- Potente, M., Ghaeni, L., Baldessari, D., Mostoslavsky, R., Rossig, L., Dequiedt, F., Haendeler, J., Mione, M., Dejana, E., Alt, F. W., Zeiher, A. M., & Dimmeler, S.
- Affiliations
- Goethe University Frankfurt (DE)
- IFOM (IT)
- University of Liège (BE)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Dimmeler, Stefanie
- ORCID
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2007-10-15
- Volume
- 21
- Issue
- 20
- Pages
- 2644-2658
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC2000327
- OpenAlex
- W2099806958
- Cited by
- 608
- References
- 52
- Citations by year
- 2026: 15 · 2025: 15 · 2024: 15 · 2023: 23 · 2022: 32 · 2021: 36 · 2020: 43 · 2019: 23 · 2018: 40 · 2017: 44 · 2016: 29 · 2015: 38 · 2014: 43 · 2013: 49 · 2012: 42
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Institutional Research Information System (Università degli Studi di Trento) (submittedVersion)
- ORBi (University of Liège) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (PO1306/1-1)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- SIRT1, sirtuins, angiogenesis, endothelial cells, sprouting angiogenesis, branching morphogenesis, FOXO1, histone deacetylation, vascular remodeling, neovascularization, ischemia, vascular development, zebrafish, mice
- MeSH terms
- Forkhead Box Protein O1, Animals, Blood Vessels, Cells, Cultured, Humans, Mice, Mutant Strains, Mice, Transgenic, Morphogenesis, Zebrafish, Mice, Knockout, Gene Expression Regulation, Developmental, Neovascularization, Physiologic, RNA Interference, Sirtuins, Endothelial Cells, Mice, Forkhead Transcription Factors, Sirtuin 1
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