Relevant bibliographies by topics / HMGA2

Academic literature on the topic 'HMGA2'

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Published: 4 June 2021
Last updated: 6 July 2024

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Journal articles on the topic "HMGA2"

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Ismail, A. A., S. Wagner, H. Murua Escobar, S. Willenbrock, K. A. Sterenczak, M. T. Samy, A. M. Abd El-Aal, I. Nolte, and P. Wefstaedt. "Effects of High-Mobility Group A Protein Application on Canine Adipose-Derived Mesenchymal Stem CellsIn Vitro." Veterinary Medicine International 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/752083.

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Multipotency and self-renewal are considered as most important features of stem cells to persist throughout life in tissues. In this context, the role of HMGA proteins to influence proliferation of adipose-derived mesenchymal stem cell (ASCs) while maintaining their multipotent and self-renewal capacities has not yet been investigated. Therefore, extracellular HMGA1 and HMGA2 application alone (10–200 ng/mL) and in combination with each other (100, 200 ng/mL each) was investigated with regard to proliferative effects on canine ASCs (cASCs) after 48 hours of cultivation. Furthermore, mRNA expression of multipotency marker genes in unstimulated and HMGA2-stimulated cASCs (50, 100 ng/mL) was analyzed by RT-qPCR. HMGA1 significantly reduced cASCs proliferation in concentrations of 10–200 ng/mL culture medium. A combination of HMGA1 and HMGA2 protein (100 and 200 ng/mL each) caused the same effects, whereas no significant effect on cASCs proliferation was shown after HMGA2 protein application alone. RT-qPCR results showed that expression levels of marker genes including KLF4, SOX2, OCT4, HMGA2, and cMYC mRNAs were on the same level in both HMGA2-protein-stimulated and -unstimulated cASCs. Extracellular HMGA protein application might be valuable to control proliferation of cASCs in context with their employment in regenerative approaches without affecting their self-renewal and multipotency abilities.
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Palumbo Júnior, Antonio, Vanessa Paiva Leite de Sousa, Francesco Esposito, Marco De Martino, Floriana Forzati, Fábio Carvalho de Barros Moreira, Tatiana de Almeida Simão, et al. "Overexpression of HMGA1 Figures as a Potential Prognostic Factor in Endometrioid Endometrial Carcinoma (EEC)." Genes 10, no. 5 (May 15, 2019): 372. http://dx.doi.org/10.3390/genes10050372.

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Endometrioid endometrial carcinomas (EEC) are the most common malignant gynecologic tumors. Despite the increase in EEC molecular knowledge, the identification of new biomarkers involved in disease’s development and/or progression would represent an improvement in its course. High-mobility group A protein (HMGA) family members are frequently overexpressed in a wide range of malignancies, correlating with a poor prognosis. Thus, the aim of this study was to analyze HMGA1 and HMGA2 expression pattern and their potential role as EEC biomarkers. HMGA1 and HMGA2 expression was initially evaluated in a series of 46 EEC tumors (stages IA to IV), and the findings were then validated in The Cancer Genome Atlas (TCGA) EEC cohort, comprising 381 EEC tumors (stages IA to IV). Our results reveal that HMGA1 and HMGA2 mRNA and protein are overexpressed in ECC, but only HMGA1 expression is associated with increased histological grade and tumor size. Moreover, HMGA1 but not HMGA2 overexpression was identified as a negative prognostic factor to EEC patients. Finally, a positive correlation between expression of HMGA1 pseudogenes—HMGA1-P6 and HMGA1-P7—and HMGA1 itself was detected, suggesting HMGA1 pseudogenes may play a role in HMGA1 expression regulation in EEC. Thus, these results indicate that HMGA1 overexpression possesses a potential role as a prognostic biomarker for EEC.
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Li, Liping, Wenyan Lu, Alison R. Moliterno, Lingling Xian, Joseph Kim, Ophelia Rogers, Jerry L. Spivak, and Linda Resar. "High Mobility Group A1 Chromatin Regulators: Key Epigenetic Switches and Therapeutic Targets Required for Leukemic Transformation in JAK2 Mutant MPN." Blood 134, Supplement_1 (November 13, 2019): 1680. http://dx.doi.org/10.1182/blood-2019-130262.

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Introduction: Myeloproliferative neoplasms (MPN) are clonal hematopoietic stem cell (HSC) disorders characterized by hyperactive JAK/STAT signaling and increased risk of transformation to myelofibrosis (MF) and acute myeloid leukemia (AML). However, mechanisms driving progression remain elusive and therapies are ineffective after leukemia develops. The High Mobility Group A1/2 (HMGA1/2) genes encode oncogenic chromatin remodeling proteins which are overexpressed in aggressive solid tumors where they portend adverse outcomes. HMGA1/2 genes are also up-regulated in hematologic malignancies and MPN with disease progression. In murine models, Hmga1/2 overexpression drives clonal expansion and deregulated proliferation while Hmga1 overexpression is sufficient for lymphoid leukemic transformation. We therefore sought to: 1) test the hypothesis that HMGA1/2 proteins are rational therapeutic targets required for leukemic transformation in MPN, 2) elucidate mechanisms mediated by HMGA1/2 during disease progression, and, 3) identify therapeutic approaches to disrupt HMGA function and intercept the transition from chronic disease to aggressive leukemia. Methods: We compared HMGA1/2 in JAK2V617F mutant AML cell lines from MPN patients (DAMI, SET-2), CD34+ cells from PV patients during chronic and transformation phases, and JAK2V617F murine models of PV (transgenic JAK2V617F) and PV-AML (transgenic JAK2V617F/MPLSV). To elucidate HMGA1/2 function, we silenced HMGA1 or HMGA2 via short hairpin RNA in human MPN-AML cells and generated murine models of PV-AML with heterozygous Hmga1 or Hmga2 deficiency. To dissect molecular mechanisms underlying HMGA, we compared RNA-Seq from MPN-AML cell lines after gene silencing. Finally, to identify therapies to target HMGA pathways, we integrated the RNA-Seq data with the Broad Connectivity Map (cMAP). Results: There is a marked up-regulation in HMGA1/2 in CD34+ cells from PV patients after transformation to AML and in leukemic blasts from our PV-AML mouse model. Conversely, silencing HMGA1 or HMGA2 in human MPN-AML cell lines (DAMI, SET-2) dramatically halts proliferation, disrupts clonogenicity, and prevents leukemia development in mice. Further, heterozygous Hmga1 deficiency prolongs survival in the transgenic PV-AML murine model with fulminant leukemia and early mortality, although Hmga2 deficiency has no effect. RNA-Seq analyses from human MPN-AML cell lines revealed that HMGA1 up-regulates transcriptional networks involved in cell cycle progressions (E2F targets, mitotic spindle, G2M checkpoint, MYC targets) while repressing immune pathways (inflammation, interferon gamma) and oxidative phosphorylation. HMGA2 up-regulates similar pathways, but represses TNFalpha signaling. cMAP identified inhibitors of histone deacetylation and cell cycle progression as potential agents to target HMGA1 pathways; DNA synthesis inhibitors were predicted to target HMGA2 pathways. Cytotoxicity assays demonstrate that epigenetic therapy with HDAC inhibitors synergizes with Ruxolitinib in JAK2 mutant MPN cells after transformation to leukemia. Conclusions: HMGA1/2 genes are overexpressed in MPN with highest levels after leukemic transformation. Further, silencing HMGA1/2 disrupts leukemogenic phenotypes in vitro and prevents the development of leukemia in mice. In addition, heterozygous deficiency of Hmga1 prolongs survival in a fulminant MPN-AML model. Mechanistically, RNA-Seq analyses revealed that HMGA amplifies transcriptional networks involved cell cycle progression, which can be targeted with epigenetic therapies. Our findings further underscore the key role for HMGA as an epigenetic switch required for leukemic transformation in MPN and opens the door to novel therapeutic approaches to intercept the transition from chronic indolent disease to aggressive leukemia. Disclosures No relevant conflicts of interest to declare.
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Parisi, Silvia, Silvia Piscitelli, Fabiana Passaro, and Tommaso Russo. "HMGA Proteins in Stemness and Differentiation of Embryonic and Adult Stem Cells." International Journal of Molecular Sciences 21, no. 1 (January 6, 2020): 362. http://dx.doi.org/10.3390/ijms21010362.

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HMGA1 and HMGA2 are chromatin architectural proteins that do not have transcriptional activity per se, but are able to modify chromatin structure by interacting with the transcriptional machinery and thus negatively or positively regulate the transcription of several genes. They have been extensively studied in cancer where they are often found to be overexpressed but their functions under physiologic conditions have still not been completely addressed. Hmga1 and Hmga2 are expressed during the early stages of mouse development, whereas they are not detectable in most adult tissues. Hmga overexpression or knockout studies in mouse have pointed to a key function in the development of the embryo and of various tissues. HMGA proteins are expressed in embryonic stem cells and in some adult stem cells and numerous experimental data have indicated that they play a fundamental role in the maintenance of stemness and in the regulation of differentiation. In this review, we discuss available experimental data on HMGA1 and HMGA2 functions in governing embryonic and adult stem cell fate. Moreover, based on the available evidence, we will aim to outline how HMGA expression is regulated in different contexts and how these two proteins contribute to the regulation of gene expression and chromatin architecture in stem cells.
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Vignali, Robert, and Silvia Marracci. "HMGA Genes and Proteins in Development and Evolution." International Journal of Molecular Sciences 21, no. 2 (January 19, 2020): 654. http://dx.doi.org/10.3390/ijms21020654.

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HMGA (high mobility group A) (HMGA1 and HMGA2) are small non-histone proteins that can bind DNA and modify chromatin state, thus modulating the accessibility of regulatory factors to the DNA and contributing to the overall panorama of gene expression tuning. In general, they are abundantly expressed during embryogenesis, but are downregulated in the adult differentiated tissues. In the present review, we summarize some aspects of their role during development, also dealing with relevant studies that have shed light on their functioning in cell biology and with emerging possible involvement of HMGA1 and HMGA2 in evolutionary biology.
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Meireles Da Costa, Nathalia, Luis Felipe Ribeiro Pinto, Luiz Eurico Nasciutti, and Antonio Palumbo Jr. "The Prominent Role of HMGA Proteins in the Early Management of Gastrointestinal Cancers." BioMed Research International 2019 (October 13, 2019): 1–7. http://dx.doi.org/10.1155/2019/2059516.

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GI tumors represent a heterogeneous group of neoplasms concerning their natural history and molecular alterations harbored. Nevertheless, these tumors share very high incidence and mortality rates worldwide and patients’ poor prognosis. Therefore, the identification of specific biomarkers could increase the development of personalized medicine, in order to improve GI cancer management. In this sense, HMGA family members (HMGA1 and HMGA2) comprise an important group of genes involved in the genesis and progression of malignant tumors. Additionally, it has also been reported that HMGA1 and HMGA2 display an important role in the detection and progression of GI tumors. In this way, HMGA family members could be used as reliable biomarkers able to efficiently track not only the tumor per se but also the main risk conditions related with their development of GI cancers in the future. Finally, it shall be a promising option to revert the current scenario, once HMGA genes and proteins could represent a convergence point in the complex landscape of GI tumors.
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Tessari, Michela A., Monica Gostissa, Sandro Altamura, Riccardo Sgarra, Alessandra Rustighi, Clio Salvagno, Giuseppina Caretti, et al. "Transcriptional Activation of the Cyclin A Gene by the Architectural Transcription Factor HMGA2." Molecular and Cellular Biology 23, no. 24 (December 15, 2003): 9104–16. http://dx.doi.org/10.1128/mcb.23.24.9104-9116.2003.

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ABSTRACT The HMGA2 protein belongs to the HMGA family of architectural transcription factors, which play an important role in chromatin organization. HMGA proteins are overexpressed in several experimental and human tumors and have been implicated in the process of neoplastic transformation. Hmga2 knockout results in the pygmy phenotype in mice and in a decreased growth rate of embryonic fibroblasts, thus indicating a role for HMGA2 in cell proliferation. Here we show that HMGA2 associates with the E1A-regulated transcriptional repressor p120E4F, interfering with p120E4F binding to the cyclin A promoter. Ectopic expression of HMGA2 results in the activation of the cyclin A promoter and induction of the endogenous cyclin A gene. In addition, chromatin immunoprecipitation experiments show that HMGA2 associates with the cyclin A promoter only when the gene is transcriptionally activated. These data identify the cyclin A gene as a cellular target for HMGA2 and, for the first time, suggest a mechanism for HMGA2-dependent cell cycle regulation.
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Resar, Linda, Donna Marie Williams, Zhizhuang Joe Zhao, Ophelia Rogers, Lingling Xian, Jerry L. Spivak, and Alison R. Moliterno. "High Mobility Group A1/2 Chromatin Remodeling Proteins Associate with Polycythemia Vera Transformation to Acute Leukemia in Humans and a JAK2 V617F Transgenic Mouse Model." Blood 128, no. 22 (December 2, 2016): 1958. http://dx.doi.org/10.1182/blood.v128.22.1958.1958.

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Abstract Introduction: The MPN are clonal hematopoietic stem cell (HSC) disorders characterized by an overproduction of blood cells and an increased risk of transformation to an aggressive phase with myelofibrosis (MF) and/or acute myeloid leukemia (AML). Polycythemia vera (PV) is the most common clinical subtype, and while PV starts as an indolent process, nearly 25% of patients will progress to MF and/or AML. PV is caused by acquired mutations of JAK2, yet JAK2 mutations alone do not account for MF or AML transformation. Mutations in genes encoding epigenetic regulators are associated with MPN transformation, but the mechanism of action is not understood. HMGA1/2 chromatin binding proteins are potent oncogenes that drive tumor progression by activating oncogenic and stem cell transcriptional networks. Both HMGA1/2 are overexpressed in acute leukemia and have been shown to be drivers of clonal expansion in myeloid disease in humans and in murine myeloproliferative disease models. We hypothesized that HMGA proteins could be critical drivers of transformation in PV and therefore tested the association of HMGA1/2 expression to transformation in human and murine PV. Methods: We examined the HSC genomic context and clonal evolution in 49 JAK2V617F-positive PV patients using standard and SNP-array karyotyping and a targeted resequencing panel of 163 genes associated with myeloid cancers. We examined HSC clonal burden by examining JAK2V617F HSC genotypes on a single cell basis. We measured HMGA1 and HMGA2 expression in a JAK2V617F positive human cell line, in isolated CD34+ HSCs from PV patients during chronic and transformation phases, in JAK2V617F transgenic murine models of PV (tgJAK2V617F) and PV-AML (tgJAK2V617F/MPLSV; Blood 2015;126:484) using a real-time quantitative RT-PCR (qRT-PCR) assay. Results: Both HMGA1 and HMGA2 mRNA were up-regulated in all JAK2V617F-positive contexts. In primary human PV CD34+ HSCs, HMGA1 and HMGA2 were found to be increased by 7 and 100 fold, respectively, compared to controls. Moreover, there was a dramatic up-regulation in both HMGA1/2 in patients who transformed from PV to MF or AML compared to chronic phase PV, whether analyzed cross-sectionally (Figure) or prospectively in selected patients. In addition to disease phase, over-expression of HMGA1/2 correlated with clonal dominance of JAK2V617F-homozygous stem cells, and additional mutations of epigenetic regulators including EZH2 and SETBP1. Similarly, when assessed in unfractionated bone marrow or in tumor samples in the two transgenic mouse models for PV and PV-AML, Hmga1/2 were overexpressed compared to wild-type littermates, with highest levels in the PV-AML transgenic mouse model. Conclusion: HMGA1 and HMGA2 are overexpressed in PV, and higher levels associate with disease progression to MF and AML, both in human PV and in transgenic murine models of PV. These data suggest HMGA proteins are critical drivers of PV transformation and that the mechanism of HMGA1/2 overexpression is a consequence of aberrant JAK/STAT signaling and epigenetic dysregulation. Our findings indicate that HMGA1/2 overexpression may function as a necessary molecular switch for PV leukemic transformation. Therefore, HMGA proteins and their transcriptional pathways offer novel therapeutic targets aimed at the prevention of PV progression to MF and AML. Disclosures No relevant conflicts of interest to declare.
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Moliterno, Alison R., Donna Marie Williams, Liping Li, Lingling Xian, Li Luo, Amy S. Duffield, Ophelia Rogers, Jerry L. Spivak, and Linda Resar. "The High Mobility Group A1 Chromatin Regulator Is Required for Pathologic Megakaryocyte Development and Progression to Myelofibrosis in JAK2V617F Murine Models." Blood 134, Supplement_1 (November 13, 2019): 472. http://dx.doi.org/10.1182/blood-2019-131432.

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Introduction: JAK2V617F-positive myeloproliferative neoplasms (MPN) are clonal hematopoietic stem cell (HSC) disorders characterized by unregulated JAK2/STAT signaling and increased risk of transformation to myelofibrosis (MF). Pathologic JAK2/STAT signaling of the thrombopoietin/thrombopoietin receptor pathway in HSC, progenitors, and megakaryocytes drives megakaryocytic proliferation, megakaryocytic hypertrophy, thrombocytosis, HSC niche damage, osteosclerosis, myelofibrosis, and extramedullary hematopoiesis (EMH). The High Mobility Group A1/2 (HMGA1/2) genes encode oncogenic chromatin remodeling proteins that foster aberrant STAT3 signaling in diverse contexts. In murine models, Hmga1/2 overexpression drives clonal expansion and deregulated proliferation. In patients with MPN, HMGA1/2 genes are overexpressed with disease progression to MF. We therefore sought to: 1) elucidate mechanisms mediated by HMGA1/2 in JAK2V617F-associated MF transformation and 2) test the hypothesis that HMGA proteins are rational therapeutic targets for MF progression. Methods: We used a JAK2V617F transgenic murine model (VF) in which 13 copies of the human JAK2V617F cDNA are driven by the Vav promoter (Blood 2008; 111:5109-5117). To elucidate the function of Hmga1 or Hmga2 in the JAK2V617F context, we crossed VF mice onto a background deficient for Hmga1 or Hmga2 to generate VF/Hmga1+/- and VF/Hmga2+/- progeny. We also generated a tissue specific model whereby Hmga1 was deleted in HSC via Vav-cre (Vav-cre Hmga1+/-) and crossed these mice onto the VF model (VF/Vav-cre Hmga1+/-). Serial blood counts, histology of marrow and spleen, and immunohistochemistry with CD61 antibodies were compared in each model at 8, 16, and/or 40 weeks of age. We also performed flow cytometric analysis of HSC and progenitor populations in mice with these genotypes. Results: The VF mice develop an MPN phenotype by 8 weeks with marked thrombocytosis and erythrocytosis. By 33 weeks, VF mice progress to MF characterized by anemia, splenomegaly due to extramedullary hematopoiesis (EMH), marked megakaryocytic hyperplasia, megakaryocytic hypertrophy, increased platelet size, and osteosclerosis with reticulin fibrosis (Figure A and B). ). The VF mouse also develops an expansion of megakaryocyte-erythroid progenitors (MEP) compared to wildtype mice (P<0.01). Neither mice with Hmga1deficiency (Hmga1+/- or Hmga1-/-) nor Hmga2+/- mice develop thrombocytopenia or other blood count abnormalities at one year of age, and preliminary data suggests that the MEP compartment is normal in Hmga1+/- and Hmga1-/- mice. However, VF/Hmga1+/- mice had reduction of both megakaryocyte hypertrophy and hyperplasia, bone marrow fibrosis, and osteosclerosis compared to VF mice at corresponding age ranges (Figure A). Further, there was mitigation of thrombocytosis, reduction in platelet size, and decreased spleen weight in VF/Hmga1+/- mice compared to VF mice at corresponding age ranges (Figure B). Importantly, VF/Hmga1+/- mice fail to develop anemia which occurs after 33 weeks in the VF model (VF hemoglobin 12.9 g/dl, VF/Hmga1+/- hemoglobin 15.1 g/dl, P<.05). In VF/Hmga1-/- mice, there was no expansion in MEP. The MPN progression to MF was prevented by both global or HSC-specific heterozygous Hmga1 deficiency, demonstrating that the effects of Hmga1 are specific to the hematopoietic cell context rather than the bone marrow microenvironment. In addition, similar degrees of mitigation were observed in VF mice with heterozygous or homozygous Hmga1 deficiency. In contrast, Hmga2 deficiency failed to prevent progression in the VF model. Unexpectedly, Hmga2 deficiency exacerbated megakaryocyte hypertrophy and reticulin fibrosis in VF mice. Conclusions: In a JAK2V617F murine model, heterozygous deficiency of Hmga1 prevents MPN progression to MF, interrupting both the development of megakaryocytic hyperplasia and fibrosis, which are hallmarks of murine and human JAK2V617F disease. While Hmga1 is not required for megakaryocyte or platelet development under steady state conditions, it is critical to the amplification of aberrant signaling in MF associated VF. Further, our findings underscore a key role for HMGA1 as a mediator of aberrant JAK2/STAT3 signaling and a therapeutic target to quell myeloproliferation and prevent MF progression. Disclosures Duffield: Boston Biomedical/Sumitomo Dainippon Pharma Co., Ltd.: Consultancy, Membership on an entity's Board of Directors or advisory committees; MedImmune: Consultancy.
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Huang, Shaoyue, Zhen Hong, Leguo Zhang, Jian Guo, Yanhua Li, and Kuo Li. "HMGA2 Promotes Brain Injury in Rats with Cerebral Infarction by Activating TLR4/NF-κB Signaling Pathway." Mediators of Inflammation 2022 (August 4, 2022): 1–8. http://dx.doi.org/10.1155/2022/1376959.

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Cerebral infarction is a common disease with a higher disability and fatality rates. The incidence rates of cerebral infarction or cerebral ischemic stroke gradually increase with aging and cerebrovascular disease progression. This study is aimed at evaluating the effects of HMGA2 on cerebral infarction-induced brain tissue damage and its underlying mechanisms. Adult Sprague Dawley rats were pretreated with sh-HMGA2 before cerebral infarction operation. The effect of HMGA2 on the arrangement, distribution, and morphological structure of neurons and the cell apoptosis ratio in brain tissue were detected via hematoxylin and eosin staining, brain-water content, TTC staining, and TUNEL staining. The results from ELISA assay, qPCR, and western blot indicated that downregulation of HMGA2 mitigated inflammatory stress via regulating the expression of TLR4/NF-κB. In addition, results showed that suppressed HMGA2 attenuated the neurological dysfunction of brain injury rats and markedly reduced infarct volume. HMGA2 might be able to alleviate the damage associated with cerebral infarction-induced inflammatory response and cell apoptosis. Moreover, downregulation of HMGA2 had a protective effect on the brain damage derived from cerebral infarction by mediating the TLR4/NF-κB pathway. In conclusion, the current study demonstrated that downregulation of HMGB2 decreased the infarct size, inflammatory responses, and apoptosis in cerebral injury and further had neuroprotective effects against cerebral infarction-induced brain damage. Finally, these results indicated that the downregulation of the TLR4/NF-κB pathway after ischemia by HMGB2 inhibition is a potential mechanism of the neuroprotective effect of cerebral injury.
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Dissertations / Theses on the topic "HMGA2"

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Kahli, Malik. "Implication des protéines HMGA et HMGA2 dans les changements du programme de réplication au cours de la sénescence cellulaire." Thesis, Montpellier 2, 2011. http://www.theses.fr/2011MON20059/document.

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La sénescence, considérée comme étant un arrêt irréversible du cycle cellulaire, se caractérise par des changements drastiques de l'expression génique et de l'organisation de la structure de la chromatine. En effet, il se forme des foyers denses d'hétérochromatine au sein du noyau (SAHF) et ces modifications s'accompagnent d'un déclin progressif de la capacité à dupliquer le génome. Au cours de ma thèse, j'ai voulu savoir si ces modifications de la chromatine induite par les SAHF pouvaient influer sur le programme de réplication et changer la distribution des origines de réplication sur le génome au cours du processus d'entrée en sénescence réplicative des cellules. Nous avons donc, dans un premier temps, comparé par peignage moléculaire de l'ADN réplicatif la distribution des origines de réplication de cellules primaires prolifératives et sénescentes. Nous avons également cartographié l'ensemble de leurs origines de réplication sur la totalité du génome en purifiant les brins naissants aux origines de réplication que nous avons couplé à une analyse de séquençage à haut débit.Les protéines HMGA1 et HMGA2 étant des éléments précurseurs essentiels à la mise en place des SAHF, nous avons créé des lignées cellulaires qui, en sur-exprimant de façon inductibles ces protéines, induit une sénescence prématurée. Nous avons réalisé le même type d'analyses sur ces cellules afin de mettre en évidence le rôle de ces protéines dans les modifications du programme de réplication que nous avons observé au cours de l'entrée en sénescence de ces différents types cellulaires
Senescence, considered as an irreversible cell cycle arrest, is characterized by dramatic changes in genes expression and chromatin organisation forming dense heterochromatic foci (SAHF). These changes are concomitant to a progressive decline of the capactity to replicate the genome. My PhD topic was to investigate whether the chromatin changes induced by SAHF formation could influence the replication program and modify the origin distribution along the genome at replicative senescence. We first compared the origin distribution of proliferative and pre-senescent primary fibroblasts by DNA molecular combing. Then, we mapped the origins positions in whole human genome by using the nascent strand purification assay coupled to deep sequencing.As HMGA1 and HMGA2 proteins are essential to induce SAHF formation, we designed inducible cell lines wich overexpress these proteins, triggering premature senescence. We made the same type of experiments in these cell lines in order to investigate the implication of these proteins on the changes of the replication program we observed during senescence
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Saada-Bouzid, Esma. "Étude génomique et fonctionnelle de la dérégulation du gène HMGA2 dans les tumeurs adipocytaires." Thesis, Nice, 2015. http://www.theses.fr/2015NICE4000/document.

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Les tumeurs adipocytaires (TA) bénignes sont majoritairement constituées par les lipomes, alors que les TA malignes sont principalement des Tumeurs Lipomateuses Atypiques (TLA)/ liposarcome (LPS) bien différenciés (LBD) et les LPS dédifférenciés (LDD). Le gène HMGA2 (High Mobility Group A2) est remanié dans certains lipomes et amplifié dans les TLA/LBD et LDD. Ainsi, nous avons émis l’hypothèse que HMGA2 jouait un rôle fondamental dans la genèse des TA bénignes et malignes. En faveur de cette hypothèse, nous avons observé une surexpression constante de HMGA2 dans les TLA/LBD et LDD avec amplification de HMGA2 et les lipomes avec remaniement de HMGA2. Dans un cas de lipomatose, hypertrophie pathologique du tissu adipeux sans anomalie du gène HMGA2, une surexpression de HMGA2 était associée à une inhibition de l’expression de plusieurs microARN let-7. En revanche, nos travaux ne sont pas en faveur d’un rôle prépondérant des microARN let7 dans la surexpression de HMGA2 dans les TA. Nous nous sommes également intéressés aux gènes partenaires de fusion avec HMGA2 dans les lipomes et avons notamment identifié une nouvelle fusion impliquant PPAP2B (Phosphatidic Acid Phosphatase type 2B) localisé en 1p32. Nous avons aussi confirmé le rôle du gène NFIB (9p22) dans les lipomes. Enfin, nous avons établi des corrélations pronostiques dans une grande série de 116 TLA/LBD et LDD : l’amplification de HMGA2 était associée à l’histotype TLA/LBD et à une survie longue alors que les amplifications de CDK4 et JUN sont associées au type LDD et une survie courte. Ainsi, nos données confortent l’hypothèse d’un rôle précoce et majeur de HMGA2 dans la genèse des TA bien différenciées
Benign adipocytic tumors (AT) are mainly represented by lipomas whereas most malignant AT are Atypical Lipomatous Tumors/Well-differentiated liposarcomas (ALT/WDLPS) and dedifferentiated liposarcomas (DDLPS). HMGA2 gene (High Mobility Group A2) is rearranged in some lipomas and amplified in ALT/WDLPS and DDLPS. Thus, we hypothesized that HMGA2 played a fundamental role in benign and malignant AT genesis. In favor of this hypothesis, we observed a constant overexpression of HMGA2 in amplified ALT/WDLPS and DDLPS, and in rearranged lipomas. In a case of lipomatosis, that is a pathological proliferation of the adipocytic tissu without rearrrangement of HMGA2, the overexpression of HMGA2 was asssociated with an inhibition of the expression of several let-7 microRNAs. However, we did not find a leading role of let-7 microRNAs in the deregulation of HMGA2 expression in AT. We also studied partner fusion genes of HMGA2 in lipomas and have specifically identified a new fusion involving PPAP2B (Phosphatidic Acid Phosphatase type 2B) which is located in 1p32. We also confirmed the role of NFIB gene (9p22) in lipomas. Finally, we have established prognostic correlations in a series of 116 ALT/WDLPS and DDLPS: HMGA2 amplification was associated with ALT/WDLPS histotype and a longer survival whereas respective CDK4 and JUN amplification were associated with DDLPS and shorter survival. Thus, our data support the hypothesis of an early and major role of HMGA2 in the genesis well differentiated AT
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Wei, Linxuan, Xiaolin Liu, Wenjing Zhang, Yuyan Wei, Yingwei Li, Qing Zhang, Ruifen Dong, et al. "Overexpression and oncogenic function of HMGA2 in endometrial serous carcinogenesis." E-CENTURY PUBLISHING CORP, 2016. http://hdl.handle.net/10150/614759.

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The high-mobility group A protein 2 (HMGA2) is a non-histone chromatin factor highly expressed in fetal tissue and malignant tumors but rarely detected within normal adult tissues. The clinical implications and biological functions of HMGA2 in endometrial carcinoma are largely unknown. Here we report that HMGA2 expression was barely detected in benign endometrium samples (2 of 28 samples). However, HMGA2 expression increased significantly from precancerous lesion endometrial glandular dysplasia (7 of 17, 41.2%), to serous endometrial intraepithelial carcinoma (5 of 8, 62.5%) and to full blown endometrial serous carcinoma (39 of 59, 66.1%). Functional characterization of HMGA2 revealed that the gene has both tumor growth promotion and metastasis. In addition, HMGA2 induced epithelial-mesenchymal transition (EMT) through modulation vimentin and β-catenin. Furthermore, HMGA2 overexpression started from endometrial serous precancers, non-invasive cancers, as well as in full blown carcinomas in a p53 knockout mouse model we recently established in our laboratory. Our findings suggest that HMGA2 may serve as a useful diagnostic marker in the assessment of endometrial serous cancer and its precursor lesions.
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Hawsawi, Ohuod. "Role of High Mobility Group A2 (HMGA2) in Prostate Cancer." DigitalCommons@Robert W. Woodruff Library, Atlanta University Center, 2019. http://digitalcommons.auctr.edu/cauetds/184.

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High mobility group A2 (HMGA2) is a non-histone protein highly expressed during the development but is low or absent in most adult tissues. Epithelial-mesenchymal transition (EMT) plays a critical role in prostate cancer progression and metastasis. HMGA2 has been shown to promote EMT in separate studies. Interestingly, wild-type HMGA2 and truncated (lacking the 3’UTR) HMGA2 isoforms are overexpressed in many cancers. However, there are no studies on the role of each isoform in prostate cancer progression. We hypothesized that wild-type and truncated HMGA2 promotes prostate cancer progression by different mechanisms. We analyzed the expression of HMGA2 in the prostate panel by western blot analysis and the localization in prostate tissue microarray by immunohistochemistry. We stably overexpressed wild-type and truncated HMGA2 cDNA in LNCaP cells and measured the expression and the localization of HMGA2 as well as EMT markers. We also performed the migration and cell viability assays. We analyzed phospho-ERK in cells overexpressing HMGA2 as well as inhibition with U0126 (MAPK inhibitor). To explore the role of truncated HMGA2, we measured the reactive oxygen species (ROS) concentration by DCFDA dye, as well as analyzing Jun-D as a putative downstream effector of HMGA2. Additionally, we knocked down Jun-D and performed the migration and cell viability assays. We treated ARCaP-M mesenchymal cells with camalexin, a 3-thizol-2-yl-indole (a natural product, as a candidate to target HMGA2) in vitro and in vivo in nude mice. Our results showed an increase in nuclear HMGA2 expression with prostate cancer progression as compared to normal tissue. LNCaP cells overexpressing wild-type but not truncated HMGA2 displayed nuclear localization and induced EMT via the ERK1/2 pathway, and this effect could be reversed by treating the cells with U0126. Conversely, truncated HMGA2 displayed cytoplasmic expression and increased prostate cancer migration via increasing Jun-D expression and ROS; this could be antagonized by Jun-D knockdown. Finally, treating ARCaP-M aggressive prostate cancer cells with camalexin reduce its expression in vitro and in vivo. In conclusion, both wild-type and truncated HMGA2 induce prostate cancer progression by different mechanisms which may be targeted by camalexin.
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Annewanter, Franka Maria [Verfasser]. "Expression von TRAIL-Rezeptoren und HMGA2 im duktalen Pankreasadenokarzinom / Franka Maria Annewanter." Kiel : Universitätsbibliothek Kiel, 2014. http://d-nb.info/1064306101/34.

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Natarajan, Suchitra. "Roles of high mobility group AT-hook protein 2 (HMGA2) in human cancers." Elsevier, 2013. http://hdl.handle.net/1993/31092.

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High Mobility Group AT-hook protein 2 (HMGA2) is a non-histone chromatin binding protein expressed in stem cells, cancer cells but not in normal human somatic cells. The presence of HMGA2 in cancer correlates with advanced neoplastic disease and poor prognosis. HMGA2 plays important roles in Base Excision Repair (BER) and at replication forks. HMGA2 is present at mammalian metaphase telomeres and its loss induces chromosomal aberrations. However, the functional role of HMGA2 at telomeres remains elusive. We hypothesized a protective role of HMGA2 that guards telomeres and modulates DNA damage repair signaling pathways. Employing different HMGA2+ human tumor cell models, we investigated the HMGA2-mediated functions that contribute to chemoresistance in glioblastoma (GB). This study presents a novel interaction of HMGA2 with telomeric protein TRF2 (Telomere Repeat-Binding Factor 2). This interaction retains TRF2 at telomeres, thus capping the telomeres and reducing telomere-dysfunction induced foci despite induced telomere stress. Loss of HMGA2 coincides with increased phosphorylation of TRF2, decreased TRF2 retention at telomeres and increased formation of telomeric aggregates, anaphase bridges and micronuclei. These findings provide new evidence for a unique role of HMGA2 at telomeres as a novel contributor of telomeric integrity. We show that upon DNA damage, HMGA2 causes increased and sustained phosphorylation of Ataxia Telangiectasia and Rad3-related kinase (ATR) and checkpoint kinase 1 (CHK1). Prolonged presence of pCHK1Ser296 coincides with prolonged G2/M block and increased tumor cell survival. The relationship between (ATR)-CHK1 DNA damage response pathway and HMGA2 identifies a novel mechanism by which HMGA2 can alter DNA repair function in cancer cells. We identified HMGA2 as a novel factor contributing to temozolomide (TMZ) resistance in GB. HMGA2 knockdown sensitizes the GB cells to TMZ. We propose a specific combination of FDA-approved drugs, TMZ and Dovitinib (DOV), to increase GB cell death. We show that DOV downregulates key BER proteins, attenuates pSTAT3-coordinated Lin28A and HMGA2 expression. Our results suggest that a sequential therapeutic strategy of pretreating GB cells with DOV followed by a sequence of TMZ and DOV diminishes TMZ resistance and enhances the ability of TMZ to induce GB cell death. Overall, we identified HMGA2 as a multifunctional survival factor in human cancer cells and showed that targeting HMGA2 is a valid strategy to combat HMGA2+ cancer cells.
February 2016
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Saada-Bouzid, Esma. "Étude génomique et fonctionnelle de la dérégulation du gène HMGA2 dans les tumeurs adipocytaires." Electronic Thesis or Diss., Nice, 2015. http://www.theses.fr/2015NICE4000.

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Les tumeurs adipocytaires (TA) bénignes sont majoritairement constituées par les lipomes, alors que les TA malignes sont principalement des Tumeurs Lipomateuses Atypiques (TLA)/ liposarcome (LPS) bien différenciés (LBD) et les LPS dédifférenciés (LDD). Le gène HMGA2 (High Mobility Group A2) est remanié dans certains lipomes et amplifié dans les TLA/LBD et LDD. Ainsi, nous avons émis l’hypothèse que HMGA2 jouait un rôle fondamental dans la genèse des TA bénignes et malignes. En faveur de cette hypothèse, nous avons observé une surexpression constante de HMGA2 dans les TLA/LBD et LDD avec amplification de HMGA2 et les lipomes avec remaniement de HMGA2. Dans un cas de lipomatose, hypertrophie pathologique du tissu adipeux sans anomalie du gène HMGA2, une surexpression de HMGA2 était associée à une inhibition de l’expression de plusieurs microARN let-7. En revanche, nos travaux ne sont pas en faveur d’un rôle prépondérant des microARN let7 dans la surexpression de HMGA2 dans les TA. Nous nous sommes également intéressés aux gènes partenaires de fusion avec HMGA2 dans les lipomes et avons notamment identifié une nouvelle fusion impliquant PPAP2B (Phosphatidic Acid Phosphatase type 2B) localisé en 1p32. Nous avons aussi confirmé le rôle du gène NFIB (9p22) dans les lipomes. Enfin, nous avons établi des corrélations pronostiques dans une grande série de 116 TLA/LBD et LDD : l’amplification de HMGA2 était associée à l’histotype TLA/LBD et à une survie longue alors que les amplifications de CDK4 et JUN sont associées au type LDD et une survie courte. Ainsi, nos données confortent l’hypothèse d’un rôle précoce et majeur de HMGA2 dans la genèse des TA bien différenciées
Benign adipocytic tumors (AT) are mainly represented by lipomas whereas most malignant AT are Atypical Lipomatous Tumors/Well-differentiated liposarcomas (ALT/WDLPS) and dedifferentiated liposarcomas (DDLPS). HMGA2 gene (High Mobility Group A2) is rearranged in some lipomas and amplified in ALT/WDLPS and DDLPS. Thus, we hypothesized that HMGA2 played a fundamental role in benign and malignant AT genesis. In favor of this hypothesis, we observed a constant overexpression of HMGA2 in amplified ALT/WDLPS and DDLPS, and in rearranged lipomas. In a case of lipomatosis, that is a pathological proliferation of the adipocytic tissu without rearrrangement of HMGA2, the overexpression of HMGA2 was asssociated with an inhibition of the expression of several let-7 microRNAs. However, we did not find a leading role of let-7 microRNAs in the deregulation of HMGA2 expression in AT. We also studied partner fusion genes of HMGA2 in lipomas and have specifically identified a new fusion involving PPAP2B (Phosphatidic Acid Phosphatase type 2B) which is located in 1p32. We also confirmed the role of NFIB gene (9p22) in lipomas. Finally, we have established prognostic correlations in a series of 116 ALT/WDLPS and DDLPS: HMGA2 amplification was associated with ALT/WDLPS histotype and a longer survival whereas respective CDK4 and JUN amplification were associated with DDLPS and shorter survival. Thus, our data support the hypothesis of an early and major role of HMGA2 in the genesis well differentiated AT
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INGRAHAM, SUSAN ELIZABETH. "THE BALANCED, RECIPROCAL TRANSLOCATION OF CHROMOSOMAL SUBBANDS 12q15 AND 14q24 AND ALTERED GENE EXPRESSION IN UTERINE LEIOMYOMA." University of Cincinnati / OhioLINK, 2002. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1029433658.

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Andrieux, Joris. "Anomalies cytogénétiques et moléculaires des myélofibroses avec métaplasie myéloi͏̈de : dérégulation et hyperexpression du gène HMGA2." Lille 2, 2003. http://www.theses.fr/2003LIL2MT21.

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Tan, E.-Jean. "Transcriptional and Epigenetic Regulation of Epithelial-Mesenchymal Transition." Doctoral thesis, Uppsala universitet, Ludwiginstitutet för cancerforskning, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-206120.

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The transforming growth factor beta (TGFβ) is a cytokine that regulates a plethora of cellular processes such as cell proliferation, differentiation, migration and apoptosis. TGFβ signals via serine/threonine kinase receptors and activates the Smads to regulate gene expression. Enigmatically, TGFβ has a dichotomous role as a tumor suppressor and a tumor promoter in cancer. At early stages of tumorigenesis, TGFβ acts as a tumor suppressor by exerting growth inhibitory effects and inducing apoptosis. However, at advanced stages, TGFβ contributes to tumor malignancy by promoting invasion and metastasis. The pro-tumorigenic TGFβ potently triggers an embryonic program known as epithelial-mesenchymal transition (EMT). EMT is a dynamic process whereby polarized epithelial cells adapt a mesenchymal morphology, thereby facilitating migration and invasion. Downregulation of cell-cell adhesion molecules, such as E-cadherin and ZO-1, is an eminent feature of EMT. TGFβ induces EMT by upregulating a non-histone chromatin factor, high mobility group A2 (HMGA2). This thesis focuses on elucidating the molecular mechanisms by which HMGA2 elicits EMT. We found that HMGA2 regulates a network of EMT transcription factors (EMT-TFs), such as members of the Snail, ZEB and Twist families, during TGFβ-induced EMT. HMGA2 can interact with Smad complexes to synergistically induce Snail expression. HMGA2 also directly binds and activates the Twist promoter. We used mouse mammary epithelial cells overexpressing HMGA2, which are mesenchymal in morphology and highly invasive, as a constitutive EMT model. Snail and Twist have complementary roles in HMGA2-mesenchymal cells during EMT, and tight junctions were restored upon silencing of both Snail and Twist in these cells. Finally, we also demonstrate that HMGA2 can epigenetically silence the E-cadherin gene. In summary, HMGA2 modulates multiple reprogramming events to promote EMT and invasion.
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Books on the topic "HMGA2"

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Gelder, Wiebke. Identifizierung von mit HMGA2 interagierenden Proteinen. GRIN Verlag GmbH, 2011.

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Book chapters on the topic "HMGA2"

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Fedele, Monica, and Alfredo Fusco. "Pituitary Adenoma: Role of HMGA Proteins." In Tumors of the Central Nervous System, Volume 10, 161–68. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-5681-6_18.

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Travers, Andrew A. "Gene Regulation by HMGA and HMGB Chromosomal Proteins and Related Architectural DNA-Binding Proteins." In DNA Conformation and Transcription, 147–58. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-29148-2_11.

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"HMGA2." In Encyclopedia of Cancer, 1710–11. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_2773.

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Chauvet, Norbert, Evelyne Galibert, Anne-Cecile Meunier, Valerie Rigau, Guillaume Osterstock, Eric Baccino, Monica Fedele, et al. "Cadherin Changes in Human Pituitary Adenomas Can Be Reproduced in cKO-Men1 and HMGA2 Mouse Models." In TRANSLATIONAL - Pituitary Neoplasia, P1–423—P1–423. The Endocrine Society, 2011. http://dx.doi.org/10.1210/endo-meetings.2011.part2.p4.p1-423.

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"HMGA1." In Encyclopedia of Cancer, 1710. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_2772.

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Chiefari, Eusebio, Francesco Paonessa, Stefania Iiritano, Ilaria Le Pera, Dario Palmieri, Giuseppe Brunetti, Angelo Lupo, et al. "The Camp-HMGA1-RBP4 System." In Recent Advances in Biochemistry, 175–97. Apple Academic Press, 2011. http://dx.doi.org/10.1201/b13131-11.

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Reeves, Raymond, and Dale Edberg. "HMGA proteins: multifaceted players in nuclear function." In Chromatin Structure and Dynamics: State-of-the-Art, 155–80. Elsevier, 2004. http://dx.doi.org/10.1016/s0167-7306(03)39007-6.

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Reeves, Raymond. "HMGA Proteins: Isolation, Biochemical Modifications, and Nucleosome Interactions." In Chromatin and Chromatin Remodeling Enzymes, Part A, 297–322. Elsevier, 2003. http://dx.doi.org/10.1016/s0076-6879(03)75020-4.

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"Mechanism of Heavy Metal ATPase (HMA2, HMA3 and HMA4) Genes." In Nano-Phytoremediation Technologies for Groundwater Contaminates, 104–17. IGI Global, 2020. http://dx.doi.org/10.4018/978-1-5225-9016-3.ch008.

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Heavy metals are the most important pollutants that are non-biodegradable and increasingly accumulate in the environment. Phytoremediation can be defined as the use of plants for the extraction, immobilization, containment, or degradation of contaminants. It provides an ecologically, environmentally sound and safe method for restoration and remediation of contaminated land. Plant species vary in their capacity of hyper-accumulation of heavy metals. The chapter reviews the current findings on the molecular mechanism involved in heavy metals tolerance, which is a valuable tool for phytoremediation. The heavy metal tolerance genes help in the hyper-accumulation trait of a plant. Heavy metal transporter ATPases (HMAs) genes help in the refluxing of heavy metal ions from the cytosol, either into the apoplast, the vacuole, or other organelles, which help in the hyperaccumulation of metal. Understanding the signaling mechanism of transporter genes will be an important tool to understand the genetics of hyperaccumulation.
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West, Natalie, Kaspar Matiasek, and Clare Rusbridge. "Suspected 3-hydroxy-3-methylglutaric aciduria (HMGA) in domestic shorthaired cats." In BSAVA Congress Proceedings 2020, 442. British Small Animal Veterinary Association, 2020. http://dx.doi.org/10.22233/9781910443774.61.5.

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Conference papers on the topic "HMGA2"

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Piscuoglio, Salvatore, Pierlorenzo Pallante, Federico Cappuzzo, Inti Zlobec, Alessandro Lugli, Alfredo Fusco, and Luigi M. Terracciano. "Abstract 3195: HMGA1 and HMGA2 over-expression in human lung carcinoma." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3195.

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Kaur, Harpreet, Marianne Hütt, Xing-gang Mao, Brent A. Orr, Charles G. Eberhart, and Eric H. Raabe. "Abstract 3031: HMGA2 promotes invasion and stemness in glioblastoma." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-3031.

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Dobersch, S., K. Rubio, and G. Barreto. "HMGA2 mediated histone deposition is required for TGFB1 induced transcription." In 60. Kongress der Deutschen Gesellschaft für Pneumologie und Beatmungsmedizin e. V. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1678058.

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Kaur, Harpreet, Marianne Hütt-Cabezas, Isabella Taylor, Laura Asnaghi, Fausto Rodriguez, Brent A. Orr, Charles G. Eberhart, and Eric H. Raabe. "Abstract 4222: Targeting HMGA2 suppresses GBM stemness, invasion and tumorigenicity." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4222.

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Burnett, Riesa, Hitesh Appaiah, Poornima Bhat-Nakshatri, Jim Wikel, Peter Crooks, William Mathews, and Harikrishna Nakshatri. "Abstract 1344: HMGA2-targeted drug discovery for breast cancer brain metastasis." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1344.

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Li, Zhizhong. "Abstract A58: HMGA2 controls muscle stem cell activation and rhabdomyosarcoma progression." In Abstracts: AACR Special Conference: Pediatric Cancer at the Crossroads: Translating Discovery into Improved Outcomes; November 3-6, 2013; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.pedcan-a58.

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Hawsawi, Ohuod A., Liza Burton, Jodi Dougan, Ana Cecillia Millena, Peri Nagappan, Shafiq Khan, and Valerie Odero-Marah. "Abstract 1089: Role of high mobility group A2 (HMGA2) in prostate cancer." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1089.

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Волеводз, Н. Н., З. С. Зюзикова, Е. А. Писарева, В. В. Шестерикова, К. Д. Кокорева, and К. Г. Забудская. "АТИПИЧНАЯ ФОРМА СИНДРОМА СИЛЬВЕРА-РАССЕЛА, АССОЦИИРОВАННАЯ С НОВОЙ МУТАЦИЕЙ В ГЕНЕ HMGA2." In IV Конференция по орфанным и детским эндокринным заболеваниям "Эндокринная орфанетика: достижения и перспективы". ФГБУ «НМИЦ эндокринологии» Минздрава России, 2024. http://dx.doi.org/10.14341/eoap2024-025.

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Kaur, Harpreet, Marianne Hutt, Xing-gang Mao, Charles G. Eberhart, and Eric H. Raabe. "Abstract 3742: Targeting the stem cell factor HMGA2 to improve outcomes in glioblastoma." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3742.

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Singh, Indrabahadur, Aditi Mehta, Nihan Öztürk, Julio Cordero, Adriana Contreras, Diya Hasan, Claudia Cosentino, et al. "HMGA2 mediated epigenetic regulation of Gata6 controls epithelial WNT signaling during lung development." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.oa3228.

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Reports on the topic "HMGA2"

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Aly, Radi, James H. Westwood, and Carole L. Cramer. Novel Approach to Parasitic Weed Control Based on Inducible Expression of Cecropin in Transgenic Plants. United States Department of Agriculture, May 2003. http://dx.doi.org/10.32747/2003.7586467.bard.

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Our overall goal was to engineer crop plants with enhanced resistance to Orobanche (broomrape) based on the inducible expression of sarcotoxin-like peptide (SLP). A secondary objective was to localize small proteins such as SLP in the host-parasite union in order to begin characterizing the mechanism of SLP toxicity to Orobanche. We have successfully accomplished both of these objectives and have demonstrated that transgenic tobacco plants expressing SLP under control of the HMG2 promoter show enhanced resistance to O. aegyptiaca and O. ramosa . Furthermore, we have shown that proteins much larger than the SLP move into Orobanche tubercles from the host root via either symplastic or apoplastic routes. This project was initiated with the finding that enhanced resistance to Orobanche could be conferred on tobacco, potato, and tomato by expression of SLP (Sarcotoxin IA is a 40-residue peptide produced as an antibiotic by the flesh fly, Sarcophaga peregrina ) under the control of a low-level, root-specific promoter. To improve the level of resistance, we linked the SLP gene to the promoter from HMG2, which is strongly inducible by Orobanche as it parasitizes the host. The resulting transgenic plants express SLP and show increased resistance to Orobanche. Resistance in this case is manifested by increased growth and yield of the host in the presence of the parasite as compared to non-transgenic plants, and decreased parasite growth. The mechanism of resistance appears to operate post-attachment as the parasite tubercles attached to the transgenic root plants turned necrotic and failed to develop normally. Studies examining the movement of GFP (approximately 6X the size of SLP) produced in tobacco roots showed accumulation of green fluorescence in tubercles growing on transformed plants but not in those growing on wild-type plants. This accumulation occurs regardless of whether the GFP is targeted to the cytoplasm (translocated symplastically) or the apoplastic space (translocated in xylem). Plants expressing SLP appear normal as compared to non-transgenic plants in the absence of Orobanche, so there is no obvious unintended impact on the host plant from SLP expression. This project required the creation of several gene constructs and generation of many transformed plant lines in order to address the research questions. The specific objectives of the project were to: 1. Make gene constructs fusing Orobanche-inducible promoter sequences to either the sarcotoxin-like peptide (SLP) gene or the GFP reporter gene. 2. Create transgenic plants containing gene constructs. 3. Characterize patterns of transgene expression and host-to-parasite movement of gene products in tobacco ( Nicotiana tabacum L.) and Arabidopsis thaliana (L.). 4. Characterize response of transgenic potato ( Solanum tuberosum L.) and tomato ( Lycopersicon esculentum Mill .) to Orobanche in lab, greenhouse, and field. Objectives 1 and 2 were largely accomplished during the first year during Dr. Aly's sabbatical visit to Virginia Tech. Transforming and analyzing plants with all the constructs has taken longer than expected, so efforts have concentrated on the most important constructs. Work on objective 4 has been delayed pending the final results of analysis on tobacco and Arabidopsis transgenic plants. The implications of this work are profound, because the Orobanche spp. is an extremely destructive weed that is not controlled effectively by traditional cultural or herbicidal weed control strategies. This is the first example of engineering resistance to parasitic weeds and represents a unique mode of action for selective control of these weeds. This research highlights the possibility of using this technique for resistance to other parasitic species and demonstrates the feasibility of developing other novel strategies for engineering resistance to parasitic weeds.
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Ginzberg, Idit, Richard E. Veilleux, and James G. Tokuhisa. Identification and Allelic Variation of Genes Involved in the Potato Glycoalkaloid Biosynthetic Pathway. United States Department of Agriculture, August 2012. http://dx.doi.org/10.32747/2012.7593386.bard.

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Steroidal glycoalkaloids (SGAs) are secondary metabolites being part of the plant defense response. The two major SGAs in cultivated potato (Solanum tuberosum) are α-chaconine and α-solanine, which exhibit strong cellular lytic properties and inhibit acetylcholinesterase activity, and are poisonous at high concentrations for humans. As SGAs are not destroyed during cooking and frying commercial cultivars have been bred to contain low levels, and their content in tubers should not exceed 20 mg/100 g fresh weight. However, environmental factors can increase tuber SGA content above the safe level. The focus of the proposed research was to apply genomic approaches to identify candidate genes that control potato SGA content in order to develop tools for potato improvement by marker-assisted selection and/or transgenic approaches. To this end, the objectives of the proposal included identification of genes, metabolic intermediates and allelic variations in the potato SGAbiosynthetic pathway. The SGAs are biosynthesized by the sterol branch of the mevalonic acid/isoprenoid pathway. Transgenic potato plants that overexpress 3-hydroxy-3-methylglutaryl-CoA reductase 1 (HMG1) or squalene synthase 1 (SQS1), key enzymes of the mevalonic acid/isoprenoid pathway, exhibited elevated levels of solanine and chaconine as well as induced expression of genes downstream the pathway. These results suggest of coordinated regulation of isoprenoid (primary) metabolism and SGA secondary metabolism. The transgenic plants were further used to identify new SGA-related candidate genes by cDNA-AFLP approach and a novel glycosyltransferase was isolated. In addition, genes involved in phytosterol biosynthesis may have dual role and synthesize defense-related steroidal metabolites, such as SGAs, via lanosterol pathway. Potato lanosterol synthase sequence (LAS) was isolated and used to prepare transgenic plants with overexpressing and silencing constructs. Plants are currently being analyzed for SGA content. The dynamics of SGA accumulation in the various organs of a potato species with high SGA content gave insights into the general regulation of SGA abundance. Leaf SGA levels in S. chacoense were 10 to 20-fold greater than those of S. tuberosum. The leptines, SGAs with strong antifeedant properties against Colorado potato beetles, were present in all aerial tissues except for early and mid-developmental stages of above ground stolons, and accounted for the high SGA content of S. chacoense. These results indicate the presence of regulatory mechanisms in most tissues except in stolons that limit the levels of α-solanine and α-chaconine and confine leptine accumulation to the aerial tissues. The genomes of cultivated and wild potato contain a 4-member gene family coding for SQS. Three orthologs were cloned as cDNAs from S. chacoense and heterologously expressed in E. coli. Squalene accumulated in all E. coli lines transformed with each of the three gene constructs. Differential transcript abundance in various organs and amino acid sequence differences in the conserved domains of three isoenzymes indicate subfunctionalization of SQS activity and triterpene/sterol metabolism. Because S. chacoense and S. phureja differ so greatly for presence and accumulation of SGAs, we selected four candidate genes from different points along the biosynthetic pathway to determine if chcor phuspecific alleles were associated with SGA expression in a segregating interspecific diploid population. For two of the four genes (HMG2 and SGT2) F2 plants with chcalleles expressed significantly greater total SGAs compared with heterozygotes and those with phualleles. Although there are other determinants of SGA biosynthesis and composition in potato, the ability of allelic states at two genes to affect SGA levels confirms some of the above transgenic work where chcalleles at two other loci altered SGA expression in Desiree. Present results reveal new opportunities to manipulate triterpene/sterol biosynthesis in more targeted ways with the objective of altering SGA content for both human health concerns and natural pesticide content without disrupting the essential metabolism and function of the phytosterol component of the membranes and the growth regulating brassinosteroids.
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