Cited by 251Cancer, Hypoxia, and MetabolismAngiogenesis and VEGF in CancerErythropoietin and Anemia Treatment

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HIF-1 in cancer therapy: two decade long story of a transcription factor

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Soni, Sourabh, Padwad, Yogendra S.·2017·Acta Oncologica

DOI 10.1080/0284186x.2017.1301680

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Abstract

Background: Oxygen (O2) homeostasis is an indispensable requirement of eukaryotes. O2 concentration in cellular milieu is defined as normoxia (∼21% O2), physoxia (∼1–13% O2) or hypoxia (∼0.1–1% O2). Hypoxia, a striking micro-environmental feature in tumorigenesis, is countered by tumor cells via induction of O2 governed transcription factor, hypoxia inducible factor-1 (HIF-1). Post discovery, HIF-1 has emerged as a promising anticancer therapeutic target during the last two decades. Recent reports have highlighted that enhanced levels of HIF-1 correlate with tumor metastasis leading to poor patient prognosis.Material and methods: A systematic search in PubMed and SciFinder for the literature on HIF-1 biology and therapeutic importance in cancer was carried out.Results: This review highlights the initial description as well as the recent insights into HIF-1 biology and regulation. We have focused on emerging data regarding varied classes of HIF-1 target genes affecting various levels of crosstalk among tumorigenic pathways. We have emphasized on the fact that HIF-1 acts as a networking hub coordinating activities of multiple signaling molecules influencing tumorigenesis. Emerging evidences indicate role of many HIF-induced proteomic and genomic alterations in malignant progression by mediating a myriad of genes stimulating angiogenesis, anaerobic metabolism and survival of cancer cells in O2-deficient microenvironment.Conclusions: Better understanding of the crucial role of HIF-1 in carcinogenesis could offer promising new avenues to researchers and aid in elucidating various open issues regarding the use of HIF-1 as an anticancer therapeutic target. In spite of large efforts in this field, many questions still remain unanswered. Hence, future investigations are necessary to devise, assess and refine methods for translating previous research efforts into novel clinical practices in cancer treatment.

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4 retracted

RETRACTED: Hypoxia-inducible factors are required for chemotherapy resistance of breast cancer stem cells
Samanta, D., Gilkes, D. M., Chaturvedi, P., Xiang, L., & Semenza, G. L. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421438111 · Cited by 460
Retracted
RETRACTED: Acriflavine inhibits HIF-1 dimerization, tumor growth, and vascularization
Lee, K., Zhang, H., Qian, D. Z., Rey, S., Liu, J. O., & Semenza, G. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909353106 · Cited by 451 · cited 1×
“In vivo investigations revealed that targeting HIF-1 function significantly inhibits tumor vascularization [79].”
Background
Retracted
RETRACTED ARTICLE: HIF-1-dependent expression of angiopoietin-like 4 and L1CAM mediates vascular metastasis of hypoxic breast cancer cells to the lungs
Zhang, H., Wong, C. C. L., Wei, H., Gilkes, D. M., Korangath, P., Chaturvedi, P., Schito, L., Chen, J., Krishnamachary, B., Winnard, P. T., et al. (2012) · Oncogene · doi:10.1038/onc.2011.365 · Cited by 326
Retracted
RETRACTED: Hypoxia induced E-cadherin involving regulators of Hippo pathway due to HIF-1α stabilization/nuclear translocation in bone metastasis from breast carcinoma
Maroni, P., Matteucci, E., Drago, L., Banfi, G., Bendinelli, P., & Desiderio, M. A. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.10.004 · Cited by 32
Retracted
Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension.
Wang, G. L., Jiang, B. H., Rue, E. A., & Semenza, G. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5510 · Cited by 6,212 · cited 1×
“HIF-1a, a basic-helix-loop-helix (bHLH)-PER (Period)ARNT-SIM (single minded) (PAS) superfamily member is the O2-labile subunit and is ubiquitously expressed in hypoxia [10].”
Background
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 · cited 1×
“[19] first demonstrated a central role of pVHL in HIF-1a regulation in 1999, and during the next decade mechanistic specifications of pVHL-HIF pathway and regulation of proteasomal degradation and polyubiquitylation were elucidated.”
Background
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735 · cited 1×
“Under normal O2 tension, the PHDs become active and cause prolyl hydroxylation in HIF-1, leading to a recognition indicator for pVHL binding, ubiquitylation and subsequent degradation of HIF-1a [33].”
Background
Succinate is an inflammatory signal that induces IL-1β through HIF-1α
Tannahill, G. M., Curtis, A. M., Adamik, J., Palsson-McDermott, E. M., McGettrick, A. F., Goel, G., Frezza, C., Bernard, N. J., Kelly, B., Foley, N. H., et al. (2013) · Nature · doi:10.1038/nature11986 · Cited by 4,176 · cited 1×
“HIF-1 serves as an important moderator of the Warburg effect, the tumor-related metabolic switch, which helps cancer cells to create energy largely by disintegration of glucose in a non-oxidative manner rather than typical oxidative phosphorylation [64].”
Background
C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333 · cited 1×
“are hydroxylated by prolyl-4-hydroxylases (PHDs) [15].”
A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation
Semenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617

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Background
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Background
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Background
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Background
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Background
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Background
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BackgroundMethodInfluential
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Influential
Investigation of cytotoxic and apoptotic effects of disodium pentaborate decahydrate on ovarian cancer cells and assessment of gene profiling
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Background

Authors: Soni, S., & Padwad, Y. S.
Affiliations: Institute of Himalayan Bioresource Technology (IN)
Corresponding author: Padwad, Yogendra S.
ORCID: Soni, Sourabh
Padwad, Yogendra S.
Venue: Acta Oncologica
Publisher: MJS Publishing, Medical Journals Sweden AB
Published: 2017-03-30
Volume: 56
Issue: 4
Pages: 503-515
ISSN: 0284-186X (ISSN-L)
1651-226X
DOI: 10.1080/0284186x.2017.1301680
OpenAlex: W2599085091
Cited by: 251
References: 122
Citations by year: 2026: 6 · 2025: 16 · 2024: 16 · 2023: 35 · 2022: 34 · 2021: 38 · 2020: 41 · 2019: 43 · 2018: 20 · 2017: 1
FWCI: 2.92
Type: journal article
Language: en
Open access: diamond
doi.org
Locations: Acta Oncologica (publishedVersion)
PubMed (publishedVersion)
Funders: Council of Scientific and Industrial Research
Council for Scientific and Industrial Research (MLP0039)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
Keywords: HIF-1, tumor hypoxia, oxygen homeostasis, transcription factor regulation, HIF-1 target genes, tumor angiogenesis, anaerobic metabolism, metastasis, carcinogenesis, cancer therapy targets, tumor microenvironment
MeSH terms: Animals, Humans, Neoplasms, Cell Hypoxia, Hypoxia-Inducible Factor 1, alpha Subunit

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HIF-1 in cancer therapy: two decade long story of a transcription factor

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