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The transcription factor EPAS-1/hypoxia-inducible factor 2α plays an important role in vascular remodeling
Open accessAbstract
We have studied the role of the basic helix–loop–helix–PAS transcription factor EPAS-1/hypoxia-inducible factor 2α in vascular development by gene targeting. In ICR/129 Sv outbred background, more than half of the mutants displayed varying degrees of vascular disorganization, typically in the yolk sac, and died in utero between embryonic day (E)9.5 and E13.5. In mutant embryos directly derived from EPAS-1 −/− embryonic stem cells (hence in 129 Sv background), all embryos developed severe vascular defects both in the yolk sac and embryo proper and died between E9.5 and E12.5. Normal blood vessels were formed by vasculogenesis but they either fused improperly or failed to assemble into larger vessels later during development. Our results suggest that EPAS-1 plays an important role at postvasculogenesis stages and is required for the remodeling of the primary vascular network into a mature hierarchy pattern.
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“Vascularization is severely impaired in HIF1A -/- (Carmeliet et al., 1998;Ryan et al., 1998) and HIF2A -/- (Peng et al., 2000) mice.”
From Therapeutic targeting of hypoxia and hypoxia-inducible factors in cancer (2016) · cites this paper as Peng et al., 2000
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Borton, A. H., Benson, B. L., Neilson, L. E., Saunders, A., Alaiti, M. A., Huang, A. Y.-C., Jain, M. K., Proweller, A., & Ramírez‐Bergeron, D. L. (2018) · Journal of the American Heart Association · doi:10.1161/jaha.118.009205 · Cited by 2
Retinal and Choroidal Vasculature
Grant, M. B., & Lutty, G. A. (2012) · Elsevier eBooks · doi:10.1016/b978-1-4557-0737-9.00018-7 · Cited by 7
Cardiac Vasculature: Development and Pathology
Watanabe, M., Wikenheiser, J. C., Ramírez‐Bergeron, D. L., Flores, S., Dangol, A., Karunamuni, G. H., Thomas, A. S., Montano, M. M., & Ashwath, R. C. (2011) · InTech eBooks · doi:10.5772/27391 · Cited by 2
“The specific deletion of HIF-2a in endothelial cells has resulted in variable results ranging from no effect on vasculature to yolk sac vascular defects (Compernolle et al., 2002; Duan et al., 2005; Peng, 2000; Scortegagna et al., 2003a; Scortegagna et al., 2003b; Tian et al., 1998).”
BackgroundNatural Products as Inhibitors of Hypoxia-Inducible Factor-1
Nagle, D. G., & Zhou, Y. (2011) · CRC Press eBooks · doi:10.1201/b11196-8 · Cited by 1
Modulation of Innate Immunity by Hypoxia
Riboldi, E., & Sica, A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-801968-9.00004-0 · Cited by 3
Kurtz, A., Wenger, R. H., & Eckardt, K. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-381462-3.00092-6 · Cited by 2
Contribution of the Unfolded Protein Response to VEGF Expression
Pereira, E. R. (2012) · doi:10.21007/etd.cghs.2012.0243
“Both, HIF1 and HIF2 knockout animals are embryonic lethal due to lack of functional vasculature [119, 120].”
BackgroundUPR Activation in Cancer Cells: A Double-Edged Sword
Pereira, E. R., Preston, A. M., & Hendershot, L. M. (2012) · Springer eBooks · doi:10.1007/978-94-007-4351-9_17 · Cited by 1
Hypoxia-Inducible Factors and Adenosine Signaling in Vascular Growth
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“A HIF-2α null mouse, in 129 SV/ICR background, exhibited severe vascular defects that died by E12.5 [ 60 ].”
BackgroundTranscriptional Regulation of Angiogenesis
Oettgen, P. (2007) · Humana Press eBooks · doi:10.1007/978-1-59259-934-9_2 · Cited by 1
“Targeted disruption of the EPAS gene has been evaluated by two different groups, resulting in two different phenotypes (18, 19 ).”
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Hypoxia-induced alternative splicing in human diseases: the pledge, the turn, and the prestige
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“As HIF-2α has an important role in vascular remodeling and preserves microvascular integrity (Peng et al., 2000; Jiang et al., 2019), the strong expression of HIF-2α in glomerular cells of the unclipped kidney exposed to systemic hypertension might reflect activation of the endothelium and microvascular injury.”
BackgroundDuan, L., Jiang, Y., Shi, Y., & Fong, G. (2023) · Biology Open · doi:10.1242/bio.059684 · Cited by 2
“Oxygen sensing and hypoxia responses are ubiquitous processes in different types of cells, and are mediated by prolyl hydroxylase domain proteins (PHDs, also known as Egg LayingNine or EGLN) and hypoxia inducible factor (HIF)-α proteins (Bruick and McKnight, 2001; Carmeliet et al., 1998; Epstein et al., 2001; Ivan et…”
BackgroundSelf-citationHypoxia-Inducible Factor: Pattern of the Effects and Their Dualism
Maistrenko, A., Kopach, O., & Skibo, G. G. (2015) · Neurophysiology · doi:10.1007/s11062-015-9530-1 · Cited by 1
Functional analysis of the von Hippel-Lindau tumour suppressor and its role in tumourigenesis
Barry, R. E. (2004) · edoc (University of Basel) · doi:10.5451/unibas-003376459
Interferons and Uterine Receptivity
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Qu, X., Ding, T., Li, X., Li, G., Bao, Q., Lai, D., Ma, Y., Li, X., & Yi, G. (2026) · Animal Genetics · doi:10.1002/age.70205
Curcumin: Promising Modulator of Hypoxia Signaling in Cancer
Singh, T., Sharma, D., Adhikari, S., Kaur, G., Kaur, J., Ramniwas, S., Rani, I., Aggarwal, D., Kuniyil, S., Mathkor, D. M., et al. (2026) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70799
Wilk, B. M., Gajapathy, M., Brown, D. M., Duncan, V. E., & Worthey, E. A. (2026) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-026-04228-2
Roles Of HIF and 2-Oxoglutarate Dependent Enzymes in Controlling Gene Expression In Hypoxia
Frost, J., Frost, M., Batie, M., Jiang, H., & Rocha, S. (2020) · doi:10.20944/preprints202011.0651.v1
Sex Differences of the Brain Structural Adaptation to Hypoxic EnvironmentPreprint
Fan, C., Zhao, C., Zhao, Y., Yin, W., Lin, J., & Zhang, J. (2019) · Research Square · doi:10.21203/rs.2.13727/v1
“10 an important role in vascular remodeling [51].”
BackgroundV-ATPase regulation of Hypoxia Inducible transcription Factors
Miles, A. L. (2018) · doi:10.17863/cam.30585
“(Peng et al., 2000; Ryan et al., 1998).”
Protein Kinase A and Protein Kinase C Connections: What Could Angiogenesis Tell Us?
Veleirinho, B., Coelho, D. S., Polli, V. A. B., de Oliveira, S. K., Ribeiro‐do‐Valle, R. M., Maraschin, M., & Dias, P. F. (2015) · InTech eBooks · doi:10.5772/60401
EPAS1 (Endothelial PAS Domain Protein 1)
Mohlin, S., Hamidian, A., Bexell, D., Påhlman, S., & Wigerup, C. (2014) · Atlas of Genetics and Cytogenetics in Oncology and Haematology · doi:10.4267/2042/54007
“HIF2A deficient embryos from an ICR/129Sv background die in utero and display severe post-vasculogenic defects (Peng et al., 2000), while HIF2A deficient mice on 129/Sv x Swiss background display lowered VEGF levels (Compernolle et al.”
BackgroundHaarmann‐Stemmann, T., & Abel, J. (2011) · Wiley eBooks · doi:10.1002/9781118140574.ch8 · Cited by 1
Javerzat, S., Franco, M., Herbert, J. J., Platonova, N., Peille, A.-L., Pantesco, V., Vos, J. D., Assou, S., Bicknell, R., Bikfalvi, A., et al. (2010) · PLoS ONE · doi:10.1371/annotation/110bdc8c-b16e-4043-816c-a3f8105ca061
Transcriptional Networks and Endothelial Lineage
Oettgen, P. (2005) · doi:10.3109/9780203025956-18
HIF-2a: A Regulator of Autonomous Growth in Ovarian Carcinoma
Omar, T. (2012) · doi:10.20381/ruor-6014
“The absence of HIF-2α in mice causes embryonic and perinatal lethality, as well as developmental abnormalities and severe vascular defects (Peng et al., 2000; Tian et al., 1998).”
BackgroundGene expression in the right ventricle during development of pulmonary hypertension
Drake, J. I. (2011) · doi:10.25772/c9h1-we71
“187 Figure 30: qRT-PCR of genes in the normal RV, failing RV, and carvediloltreated RV ................................................................................................................ 194 Figure 31: Glycolysis and gluconeogenesis pathway in the carvedilol-treated failing RV.............................…”
BackgroundInfluentialOxygen-Dependent Regulation of Erythropoiesis
Haase, V. H. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-857-7_23
Molecular Mechanisms of Post-Ischemic Angiogenesis in the Brain
Beck, H. (2010) · Springer eBooks · doi:10.1007/978-90-481-9495-7_6
Metadata
- Authors
- Peng, J., Zhang, L., Drysdale, L., & Fong, G.-H.
- Affiliations
- Western University (CA)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2000-07-04
- Volume
- 97
- Issue
- 15
- Pages
- 8386-8391
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC26957
- OpenAlex
- W2124053736
- Cited by
- 460
- References
- 0
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 9 · 2023: 13 · 2022: 8 · 2021: 11 · 2020: 10 · 2019: 14 · 2018: 7 · 2017: 9 · 2016: 9 · 2015: 22 · 2014: 19 · 2013: 19 · 2012: 19
- FWCI
- 7.00
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Keywords
- HIF-2α, vascular remodeling, vascular development, vasculogenesis, yolk sac vasculature, embryonic lethality, gene targeting, transcription factors
- MeSH terms
- Endothelial PAS Domain-Containing Protein 1, Animals, Cell Line, Female, Hemorrhage, Male, Mice, Inbred ICR, Trans-Activators, Helix-Loop-Helix Motifs, Mice, Knockout, Neovascularization, Physiologic, Mice, Basic Helix-Loop-Helix Transcription Factors, Basic Helix-Loop-Helix Proteins
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