Cited by 235Cancer, Hypoxia, and MetabolismEar and Head TumorsAngiogenesis and VEGF in Cancer

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Failure to prolyl hydroxylate hypoxia‐inducible factor α phenocopies VHL inactivation in vivo

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Kim, William Y, Safran, Michal, Buckley, Marshall RM, Ebert, Benjamin L, Glickman, Jonathan, Bosenberg, Marcus, Regan, Meredith, Kaelin, William G·2006·The EMBO Journal

DOI 10.1038/sj.emboj.7601300PMC PMC1589988

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Abstract

Many functions have been assigned to the von Hippel-Lindau tumor suppressor gene product (pVHL), including targeting the alpha subunits of the heterodimeric transcription factor HIF (hypoxia-inducible factor) for destruction. The binding of pVHL to HIFalpha requires that HIFalpha be hydroxylated on one of two prolyl residues. We introduced HIF1alpha and HIF2alpha variants that cannot be hydroxylated on these sites into the ubiquitously expressed ROSA26 locus along with a Lox-stop-Lox cassette that renders their expression Cre-dependent. Expression of the HIF2alpha variant in the skin and liver induced changes that were highly similar to those seen when pVHL is lost in these organs. Dual expression of the HIF1alpha and HIF2alpha variants in liver, however, more closely phenocopied the changes seen after pVHL inactivation than did the HIF2alpha variant alone. Moreover, gene expression profiling confirmed that the genes regulated by HIF1alpha and HIF2alpha in the liver are overlapping but non-identical. Therefore, the pathological changes caused by pVHL inactivation in skin and liver are due largely to dysregulation of HIF target genes.

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Gene set enrichment analysis: A knowledge-based approach for interpreting genome-wide expression profiles
Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625
Molecular classification of cancer: class discovery and class prediction by gene expression monitoring
Golub, T. R., Slonim, D. K., Tamayo, P., Huard, C., Gaasenbeek, M., Mesirov, J. P., Coller, H., Loh, M. L., Downing, J. R., Caligiuri, M. A., et al. (1999) · Science · doi:10.1126/science.286.5439.531 · Cited by 11,516
A comparison of normalization methods for high density oligonucleotide array data based on variance and bias
Bolstad, B. M., Irizarry, R. A., Åstrand, M., & Speed, T. P. (2003) · Bioinformatics · doi:10.1093/bioinformatics/19.2.185 · Cited by 8,328
Targeting HIF-1 for cancer therapy
Semenza, G. L. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1187 · Cited by 6,717
Generalized lacZ expression with the ROSA26 Cre reporter strain
Soriano, P. (1999) · Nature Genetics · doi:10.1038/5007 · Cited by 5,237
The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180
Cre reporter strains produced by targeted insertion of EYFP and ECFP into the ROSA26 locus
Srinivas, S., Watanabe, T., Lin, C.-S., William, C. M., Tanabe, Y., Jessell, T. M., & Costantini, F. (2001) · BMC Developmental Biology · doi:10.1186/1471-213x-1-4 · Cited by 3,121
Cellular and developmental control of O 2 homeostasis by hypoxia-inducible factor 1α
Iyer, N. V., Kotch, L. E., Agani, F., Leung, S. W., Laughner, E., Wenger, R. H., Gassmann, M., Gearhart, J. D., Lawler, A. M., Yu, A. Y., et al. (1998) · Genes & Development · doi:10.1101/gad.12.2.149 · Cited by 2,476
Oxygen sensing by HIF hydroxylases
Schofield, C. J., & Ratcliffe, P. J. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1366 · Cited by 2,068
Analysis of lung tumor initiation and progression using conditional expression of oncogenic K-rasPreprint
Jackson, E. L., Willis, N. A., Mercer, K. L., Bronson, R. T., Crowley, D. G., Montoya, R., Jacks, T., & Tuveson, D. A. (2001) · Genes & Development · doi:10.1101/gad.943001 · Cited by 1,927
Differential Roles of Hypoxia-Inducible Factor 1α (HIF-1α) and HIF-2α in Hypoxic Gene Regulation
Hu, C.-J., Wang, L.-Y., Chodosh, L. A., Keith, B., & Simon, M. C. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.24.9361-9374.2003 · Cited by 1,386
Leakage-Resistant Blood Vessels in Mice Transgenically Overexpressing Angiopoietin-1
Thurston, G., Suri, C., Smith, K., McClain, J., Sato, T. T., Yancopoulos, G. D., & McDonald, D. M. (1999) · Science · doi:10.1126/science.286.5449.2511 · Cited by 1,350
Dual Roles for Glucokinase in Glucose Homeostasis as Determined by Liver and Pancreatic β Cell-specific Gene Knock-outs Using Cre Recombinase
Postic, C., Shiota, M., Niswender, K. D., Jetton, T. L., Chen, Y., Moates, J. M., Shelton, K. D., Lindner, J., Cherrington, A. D., & Magnuson, M. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.1.305 · Cited by 1,302
Regulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1alpha.
Ravi, R. K., Mookerjee, B., Bhujwalla, Z. M., Sutter, T. R., Artemov, D., Zeng, Q., Dillehay, L. E., Madan, A., Semenza, G. L., & Bedi, A. (2000) · PubMed Central · Cited by 1,099
Hypoxia Inducible Factor-α Binding and Ubiquitylation by the von Hippel-Lindau Tumor Suppressor Protein
Cockman, M. E., Masson, N., Mole, D. R., Jaakkola, P., Chang, G.-W., Clifford, S. C., Maher, E. R., Pugh, C. W., Ratcliffe, P. J., & Maxwell, P. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002740200 · Cited by 1,053
Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation
Masson, N., Willam, C., Maxwell, P. H., Pugh, C. W., & Ratcliffe, P. J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.18.5197 · Cited by 1,014 · cited 1×
“Earlier studies showed that these variants are relatively stable compared to their wild-type counterparts and retain the ability to transcriptionally acti- vate HIF target genes (Masson et al, 2001; Hu et al, 2003; Kondo et al, 2003).”
Background
Regulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1α
Ravi, R., Mookerjee, B., Bhujwalla, Z. M., Sutter, C. H., Artemov, D., Zeng, Q., Dillehay, L. E., Madan, A., Semenza, G. L., & Bedi, A. (2000) · Genes & Development · doi:10.1101/gad.14.1.34 · Cited by 967
Role of VHL Gene Mutation in Human Cancer
Kim, W. Y., & Kaelin, W. G. (2004) · Journal of Clinical Oncology · doi:10.1200/jco.2004.05.061 · Cited by 953
Contrasting properties of hypoxia-inducible factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-associated renal cell carcinoma
Raval, R. R., Lau, K. W., Tran, M. G. B., Sowter, H. M., Mandriota, S. J., Li, J.-L., Pugh, C. W., Maxwell, P. H., Harris, A. L., & Ratcliffe, P. J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5675-5686.2005 · Cited by 940
Negative regulation of hypoxia-inducible genes by the von Hippel-Lindau protein.
Iliopoulos, O., Levy, A. P., Jiang, C., Kaelin, W. G., & Goldberg, M. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.10595 · Cited by 896
Molecular basis of the VHL hereditary cancer syndrome
Kaelin, W. G. (2002) · Nature Reviews Cancer · doi:10.1038/nrc885 · Cited by 865
Self-citation
Disruption of overlapping transcripts in the ROSA βgeo 26 gene trap strain leads to widespread expression of β-galactosidase in mouse embryos and hematopoietic cells
Zambrowicz, B., Imamoto, A., Fiering, S., Herzenberg, L. A., Kerr, W. G., & Soriano, P. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3789 · Cited by 850
Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein
Kondo, K., Klco, J., Nakamura, E., Lechpammer, M., & Kaelin, W. G. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00043-0 · Cited by 761
Self-citation
Loss of HIF-2α and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice
Compernolle, V., Brusselmans, K., Acker, T., Hoet, P., Tjwa, M., Beck, H., Plaisance, S., Dor, Y., Keshet, E., Lupu, F., et al. (2002) · Nature Medicine · doi:10.1038/nm721 · Cited by 732
Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α-degradative pathway
Isaacs, J. S., Jung, Y.-J., Mimnaugh, E. G., Martinez, A., Cuttitta, F., & Neckers, L. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204733200 · Cited by 663
The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development
Tian, H., Hammer, R. E., Matsumoto, A. M., Russell, D. W., & McKnight, S. L. (1998) · Genes & Development · doi:10.1101/gad.12.21.3320 · Cited by 647
Inhibition of HIF2α Is Sufficient to Suppress pVHL-Defective Tumor Growth
Kondo, K., Kim, W. Y., Lechpammer, M., & Kaelin, W. G. (2003) · PLoS Biology · doi:10.1371/journal.pbio.0000083 · Cited by 611
Self-citation
Post-transcriptional regulation of vascular endothelial growth factor mRNA by the product of the VHL tumor suppressor gene.
Gnarra, J. R., Zhou, S., Merrill, M. J., WAGNER, J. R., Krumm, A., Papavassiliou, E. D., Oldfield, E. H., Klausner, R. D., & Linehan, W. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.10589 · Cited by 531
Disruption of oxygen homeostasis underlies congenital Chuvash polycythemia
Ang, S. O., Chen, H., Hirota, K., Gordeuk, V. R., Jelinek, J., Guan, Y., Liu, E., Sergueeva, A. I., Miasnikova, G. Y., Mole, D., et al. (2002) · Nature Genetics · doi:10.1038/ng1019 · Cited by 510
HIF activation identifies early lesions in VHL kidneys
Mandriota, S. J., Turner, K. J., Davies, D. R., Murray, P. G., Morgan, N. V., Sowter, H. M., Wykoff, C. C., Maher, E. R., Harris, A. L., Ratcliffe, P. J., et al. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00071-5 · Cited by 483
The transcription factor EPAS-1/hypoxia-inducible factor 2α plays an important role in vascular remodeling
Peng, J., Zhang, L., Drysdale, L., & Fong, G.-H. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.140087397 · Cited by 460 · cited 1×
“HIF2a / mice also exhibit embryonic or early postnatal lethality but as a consequence of catechola- mine deficiency or lung maturation defects (Tian et al, 1998; Peng et al, 2000; Compernolle et al, 2002).”
Background
The contribution of VHL substrate binding and HIF1-α to the phenotype of VHL loss in renal cell carcinoma
Maranchie, J. K., Vasselli, J. R., Riss, J., Bonifacino, J. S., Linehan, W. M., & Klausner, R. D. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00044-2 · Cited by 440
Vascular tumors in livers with targeted inactivation of the von Hippel–Lindau tumor suppressor
Haase, V. H., Glickman, J. N., Socolovsky, M., & Jaenisch, R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1583 · Cited by 430
von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF.
Hoffman, M. A. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.10.1019 · Cited by 382
Defective placental vasculogenesis causes embryonic lethality in VHL-deficient mice
Gnarra, J. R., Ward, J. M., Porter, F. D., WAGNER, J. R., Devor, D. E., Grinberg, A., Emmert‐Buck, M. R., Westphal, H., Klausner, R. D., & Linehan, W. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.17.9102 · Cited by 366
Signalling hypoxia by HIF hydroxylases
Schofield, C. J., & Ratcliffe, P. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.111 · Cited by 343
Differential Gene Up-Regulation by Hypoxia-Inducible Factor-1α and Hypoxia-Inducible Factor-2α in HEK293T Cells
Wang, V., Davis, D. A., Haque, M., Huang, E. L., & Yarchoan, R. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4130 · Cited by 317
Angiogenesis Is Induced in a Rabbit Model of Hindlimb Ischemia by Naked DNA Encoding an HIF-1α/VP16 Hybrid Transcription Factor
Vincent, K. A., Shyu, K., Luo, Y., Magner, M., Tio, R. A., Jiang, C., Goldberg, M. A., Akita, G. Y., Gregory, R. J., & Isner, J. M. (2000) · Circulation · doi:10.1161/01.cir.102.18.2255 · Cited by 314
Reversion of deregulated expression of vascular endothelial growth factor in human renal carcinoma cells by von Hippel-Lindau tumor suppressor protein.
Siemeister, G., Weindel, K., Mohrs, K., Barleon, B., Martiny‐Baron, G., & Marmé, D. (1996) · PubMed · Cited by 308
Induction of hypervascularity without leakage or inflammation in transgenic mice overexpressing hypoxia-inducible factor-1αPreprint
Elson, D. A., Thurston, G., Huang, E. L., Ginzinger, D. G., McDonald, D. M., Johnson, R. S., & Arbeit, J. M. (2001) · Genes & Development · doi:10.1101/gad.914801 · Cited by 297
Activation of EGFP expression by Cre-mediated excision in a new ROSA26 reporter mouse strain
Mao, X., Fujiwara, Y., Chapdelaine-Williams, A. M., Yang, H., & Orkin, S. H. (2001) · Blood · doi:10.1182/blood.v97.1.324 · Cited by 291
Congenital disorder of oxygen sensing: association of the homozygous Chuvash polycythemia VHL mutation with thrombosis and vascular abnormalities but not tumors
Gordeuk, V. R., Sergueeva, A. I., Miasnikova, G. Y., Okhotin, D., Voloshin, Y., Choyke, P. L., Butman, J. A., Jedlickova, K., Prchal, J. T., & Polyakova, L. A. (2004) · Blood · doi:10.1182/blood-2003-07-2535 · Cited by 273
Identification of novel hypoxia dependent and independent target genes of the von Hippel-Lindau (VHL) tumour suppressor by mRNA differential expression profiling
Wykoff, C. C., Pugh, C. W., Maxwell, P. H., Harris, A. L., & Ratcliffe, P. J. (2000) · Oncogene · doi:10.1038/sj.onc.1204012 · Cited by 267
Inhibition of hypoxia-inducible factor is sufficient for growth suppression of VHL−/− tumors
Zimmer, M., Doucette, D., Siddiqui, N., & Iliopoulos, O. (2004) · Molecular Cancer Research · doi:10.1158/1541-7786.89.2.2 · Cited by 244
Erratum: Loss of HIF-2α and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice
Compernolle, V., Brusselmans, K., Acker, T., Hoet, P., Tjwa, M., Beck, H., Plaisance, S., Dor, Y., Keshet, E., Lupu, F., et al. (2002) · Nature Medicine · doi:10.1038/nm1102-1329b · Cited by 237
VEGF/VPF overexpression in skin of transgenic mice induces angiogenesis, vascular hyperpermeability and accelerated tumor development
Larcher, F., Murillas, R., Bolontrade, M. F., Conti, C. J., & Jorcano, J. L. (1998) · Oncogene · doi:10.1038/sj.onc.1201928 · Cited by 231
The von Hippel–Lindau protein, HIF hydroxylation, and oxygen sensing
Kaelin, W. G. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.165 · Cited by 217
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Identification of cyclin D1 and other novel targets for the von Hippel-Lindau tumor suppressor gene by expression array analysis and investigation of cyclin D1 genotype as a modifier in von Hippel-Lindau disease
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Inactivation of the Arylhydrocarbon Receptor Nuclear Translocator (Arnt) Suppresses von Hippel-Lindau Disease-Associated Vascular Tumors in Mice
Rankin, E. B., Higgins, D. F., Walisser, J. A., Johnson, R. S., Bradfield, C. A., & Haase, V. H. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.3163-3172.2005 · Cited by 140
Mutations in the VHL gene in sporadic apparently congenital polycythemia
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Gene expression profiling in a renal cell carcinoma cell line: dissecting VHL and hypoxia-dependent pathways.
Jiang, Y., Zhang, W., Kondo, K., Klco, J. M., Martin, T. B. S., Dufault, M. R., Madden, S. F., Kaelin, W. G., & Nacht, M. (2003) · PubMed · Cited by 125
Targeted Replacement of Hypoxia-Inducible Factor-1α by a Hypoxia-Inducible Factor-2α Knock-in Allele Promotes Tumor Growth
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Authors: Kim, W. Y., Safran, M., Buckley, M. R., Ebert, B. L., Glickman, J., Bosenberg, M., Regan, M., & Kaelin, W. G.
Affiliations: Brigham and Women's Hospital (US)
Broad Institute (US)
University of Vermont (US)
Harvard University (US)
Corresponding author: Kaelin, William G
ORCID: Kim, William Y
Safran, Michal
Ebert, Benjamin L
Glickman, Jonathan
Bosenberg, Marcus
Regan, Meredith
Kaelin, William G
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2006-09-14
Volume: 25
Issue: 19
Pages: 4650-4662
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/sj.emboj.7601300
PMC: PMC1589988
OpenAlex: W2097654747
Cited by: 235
References: 58
Citations by year: 2026: 3 · 2025: 5 · 2024: 13 · 2023: 11 · 2022: 9 · 2021: 11 · 2020: 10 · 2019: 12 · 2018: 13 · 2017: 6 · 2016: 10 · 2015: 10 · 2014: 25 · 2013: 14 · 2012: 12
FWCI: 6.01
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Howard Hughes Medical Institute
National Institutes of Health
National Cancer Institute (T32CA009172)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
Health Sciences › Medicine › Oncology › Ear and Head Tumors
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
Keywords: von Hippel-Lindau tumor suppressor, hypoxia-inducible factor alpha, HIF-1α, HIF-2α, prolyl hydroxylation, phenocopy, Rosa26 locus, Cre-loxP system, liver, skin, HIF target genes, gene expression profiling, tumor suppressor inactivation
MeSH terms: Epidermal Cells, Endothelial PAS Domain-Containing Protein 1, Animals, Blood Vessels, Body Weight, Epidermis, Gene Expression Regulation, HeLa Cells, Humans, Hydroxylation, Liver, Mice, Inbred BALB C, Mice, Mutant Strains, Organ Size, Phenotype, Proline, Recombination, Genetic, Hepatocytes, Cell Proliferation, Mice, Basic Helix-Loop-Helix Proteins, Basic Helix-Loop-Helix Transcription Factors, Von Hippel-Lindau Tumor Suppressor Protein, Hypoxia-Inducible Factor 1, alpha Subunit

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Failure to prolyl hydroxylate hypoxia‐inducible factor α phenocopies VHL inactivation in vivo

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