Relevant bibliographies by topics / High mobility group phosphoprotein A2

Academic literature on the topic 'High mobility group phosphoprotein A2'

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Published: 4 June 2021
Last updated: 20 February 2023

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Journal articles on the topic "High mobility group phosphoprotein A2"

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Natarajan, Suchitra, Farhana Begum, Jeonga Gim, Landon Wark, Dana Henderson, James R. Davie, Sabine Hombach-Klonisch, and Thomas Klonisch. "High Mobility Group A2 protects cancer cells against telomere dysfunction." Oncotarget 7, no. 11 (January 18, 2016): 12761–82. http://dx.doi.org/10.18632/oncotarget.6938.

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Li, A. Y. J., H. H. Lin, C. Y. Kuo, H. M. Shih, C. C. C. Wang, Y. Yen, and D. K. Ann. "High-Mobility Group A2 Protein Modulates hTERT Transcription To Promote Tumorigenesis." Molecular and Cellular Biology 31, no. 13 (May 2, 2011): 2605–17. http://dx.doi.org/10.1128/mcb.05447-11.

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Wang, Ya-Dong, Jia-Ding Mao, Jun-Feng Wang, and Mao-Qi Xu. "MiR-590 Suppresses Proliferation and Induces Apoptosis in Pancreatic Cancer by Targeting High Mobility Group A2." Technology in Cancer Research & Treatment 19 (January 1, 2020): 153303382092814. http://dx.doi.org/10.1177/1533033820928143.

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Background: Pancreatic ductal adenocarcinoma is a common malignancy with high morbidity. MicroRNAs have been demonstrated to be critical posttranscriptional regulators in tumorigenesis. This study aimed to investigate the effect of microRNA-590 on the proliferation and apoptosis of pancreatic ductal adenocarcinoma. Material and Methods: The expression of microRNA-590 and high mobility group AT-hook 2 were examined in clinical pancreatic ductal adenocarcinoma tissues. Pancreatic ductal adenocarcinoma cell line Capan-2 was employed and transfected with microRNA-590 mimics or inhibitor. The correlation between microRNA-590 and high mobility group AT-hook 2 was verified by luciferase reporter assay. Cell viability and apoptosis were detected by MTT and flow cytometry assay. The protein level of high mobility group AT-hook 2, AKT, p-AKT, mTOR, and phosphorylated mTOR were analyzed by Western blotting. Results: MicroRNA-590 was found to be negatively correlated with the expression of high mobility group AT-hook 2 in pancreatic ductal adenocarcinoma tissues. Further studies identified high mobility group AT-hook 2 as a direct target of microRNA-590. Moreover, overexpression of microRNA-590 downregulated expression of high mobility group AT-hook 2, reduced cell viability, and promoted cell apoptosis, while knockdown of miR-590 led to an inverse result. MicroRNA-590 also suppressed the phosphorylation of AKT and mTOR without altering total AKT and mTOR levels. Conclusion: Our study indicated that microRNA-590 negatively regulates the expression of high mobility group AT-hook 2 in clinical specimens and in vitro. MicroRNA-590 can inhibit cell proliferation and induce cell apoptosis in pancreatic ductal adenocarcinoma cells. This regulatory effect of microRNA-590 may be associated with AKT signaling pathway. Therefore, microRNA-590 has the potential to be used as a biomarker for predicting the progression of pancreatic ductal adenocarcinoma.
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Hawsawi, Ohuod, Veronica Henderson, Liza J. Burton, Jodi Dougan, Peri Nagappan, and Valerie Odero-Marah. "High mobility group A2 (HMGA2) promotes EMT via MAPK pathway in prostate cancer." Biochemical and Biophysical Research Communications 504, no. 1 (September 2018): 196–202. http://dx.doi.org/10.1016/j.bbrc.2018.08.155.

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Gong, Jian, Yuxiang Wang, Buping Jiang, Bin Xu, and Chuanzhen Hu. "Impact of high-mobility-group A2 overexpression on epithelial-mesenchymal transition in pancreatic cancer." Cancer Management and Research Volume 11 (May 2019): 4075–84. http://dx.doi.org/10.2147/cmar.s199289.

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Cui, Tengjiao, Suzanne Joynt, Victor Morillo, Maria Baez, Zhichun Hua, Xiaotang Wang, and Fenfei Leng. "Large Scale Preparation of the Mammalian High Mobility Group Protein A2 for Biophysical Studies." Protein & Peptide Letters 14, no. 1 (January 1, 2007): 87–91. http://dx.doi.org/10.2174/092986607779117281.

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Gong, Yan, Xin Jin, Quan-Shun Wang, Shi-Hui Wei, Bao-Ke Hou, Hong-Yang Li, Mao-Nian Zhang, and Zhao-Hui Li. "The involvement of high mobility group 1 cytokine and phospholipases A2 in diabetic retinopathy." Lipids in Health and Disease 13, no. 1 (2014): 156. http://dx.doi.org/10.1186/1476-511x-13-156.

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Heilmann, Thorsten, Florian Vondung, Christoph Borzikowsky, Sandra Krüger, Mohamed Elessawy, Ibrahim Alkatout, Antonia Wenners, et al. "Cytoplasmic levels of high mobility group A2 determine survival prognoses in breast cancer patients." International Journal of Biological Markers 35, no. 2 (May 12, 2020): 20–28. http://dx.doi.org/10.1177/1724600820917990.

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Background: High mobility group A proteins are involved in chromatin remodeling, thereby influencing multiple fundamental biological processes. HMGA2 has been linked to oncogenic traits among a variety of malignancies. Objective: To determine the prognostic implications of subcellular distribution patterns of HMGA2 in breast cancer. Methods: Nuclear and cytoplasmic HMGA2 was evaluated in 342 breast cancer specimens and matched with clinico-pathological parameters. Results: Overall and cytoplasmic, but not nuclear, levels of HMGA2 correlated with better survival prognoses in our collective (hazard ratio (HR) 0.34, P = 0.001 and HR 0.34, P < 0.001, respectively). The protective effect of cytoplasmic HMGA2 persisted in the Luminal A and triple negative breast cancer subgroups. Evaluating Luminal A and B subgroups jointly, only cytoplasmic, but not overall or nuclear HMGA2 levels were associated with better survival (HR 0.42, 95% confidence interval 0.21, 0.86, P = 0.017), irrespective of tumor size and node status. The addition of HMGA2 overall and cytoplasmic scores strengthened the prognostic selectivity in a model of conventional breast cancer risk factors. No predictive significance with regard to endocrine or chemoendocrine therapies was observed. Conclusion: Unexpectedly, we found a favorable survival probability upon overall levels of HMGA2 in our breast cancer collective, which was predominantly determined by the presence of HMGA2 in the cytoplasm.
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Binabaj, Maryam Moradi, Atena Soleimani, Farzad Rahmani, Amir Avan, Majid Khazaei, Hamid Fiuji, Saman Soleimanpour, et al. "Prognostic value of high mobility group protein A2 (HMGA2) over-expression in cancer progression." Gene 706 (July 2019): 131–39. http://dx.doi.org/10.1016/j.gene.2019.04.088.

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Peng, Yi, Jordan Laser, Guizhi Shi, Khush Mittal, Jonathan Melamed, Peng Lee, and Jian-Jun Wei. "Antiproliferative Effects by Let-7 Repression of High-Mobility Group A2 in Uterine Leiomyoma." Molecular Cancer Research 6, no. 4 (April 2008): 663–73. http://dx.doi.org/10.1158/1541-7786.mcr-07-0370.

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Dissertations / Theses on the topic "High mobility group phosphoprotein A2"

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Sneesby, Kyra, and n/a. "Gene Expression in Embryonic Chick Heart Development." Griffith University. School of Biomolecular and Biomedical Science, 2003. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20030924.153514.

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Establishment of the biochemical and molecular nature of cardiac development is essential for us to understand the relationship between genetic and morphological aspects of heart formation. The molecular mechanisms that underly heart development are still not clearly defined. To address this issue we have used two approaches to identify genes involved in early chick cardiac development. Differential display previously conducted in our laboratory led to the identification of two gene fragments differentially expressed in the heart that are further described in this thesis. The full-length cDNA sequence of both eukaryotic translation initiation factor-2b (eIF-2b) and NADH cytochrome b5 reductase (b5R) were isolated using library screening. The upreglation of these genes during heart development is expected given the heart is the first functional organ to form in vertebrates and protein synthesis and cell metabolism at this stage of development is maximal. Limitations in the differential display approach led to the development and optimisation of a subtractive hybridisation approach for use with small amounts of cells or tissue. To focus on cardiac gene expression during the initial phases of heart development, subtractive hybridization was performed between the cardiogenic lateral plate mesoderm of Hamburger and Hamilton stage 4 embryos and the heart primordia of stage 9 embryos. Of the 87 independent clones identified by this procedure, 59 matched known sequences with high homology, 25 matched unknown expressed sequence tag (EST) sequences with high homology, and 3 did not match any known sequence on the database. Known genes isolated included those involved in transcription, translation, cell signalling, RNA processing, and energy production. Two of these genes, high mobility group phosphoprotein A2 (HMGA2) and C1-20C, an unknown gene, were chosen for further characterisation. The role of each gene in early chick heart development and indeed development in general, was addressed using techniques such as in situ hybridisation, transfection analysis, in ovo electroporation and RNAi. HMGA2 is a nuclear phosphoprotein commonly referred to as an architectural transcription factor due to its ability to modulate DNA conformation. In keeping with this function, HMGA2/GFP fusion protein was shown to localise to the nucleus and in particular, the nucleolus. In situ hybridisation analysis suggested a role for HMGA2 in heart and somite development. HMGA2 expression was first detected at HH stage 5 in the lateral plate mesoderm, a region synonymous with cells specified to the cardiac fate. HMGA2 was also strongly expressed in the presomitic segmental plate mesoderm and as somites developed from the segmental plate mesoderm, the expression of HMGA2 showed an increasingly more restricted domain corresponding to the level of maturation of the somite. Restriction of HMGA2 expression was first detected in the dorsal region of the epithelial somite, then the dorsomedial lip of the dermomyotome, and finally the migrating epaxial myotome cells. The novel intronless gene, C1-20C, predicts a protein of 148 amino acids containing a putative zinc finger binding domain and prenyl binding motif. Zinc binding assays showed that the zinc finger domain of C1-20C/MBP fusion protein bound over six times the quantity of zinc compared to MBP alone, although not in a 1:1 stoichiometric molar ratio. C1-20C/GFP fusion protein was shown to localise to as yet unidentified intracellular cytoplasmic vesicular compartments. These compartments did not colocalise with the endosome/lysosome pathway, aparently ruling out a role for C1-20C in protein trafficking, recycling or degradation. Expression of C1-20C in the chick embryo suggests a possible role in heart and notochord development and preliminary results using siRNA suggest that C1-20C is involved in normal heart looping.
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Sneesby, Kyra. "Gene Expression in Embryonic Chick Heart Development." Thesis, Griffith University, 2003. http://hdl.handle.net/10072/367647.

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Abstract:
Establishment of the biochemical and molecular nature of cardiac development is essential for us to understand the relationship between genetic and morphological aspects of heart formation. The molecular mechanisms that underly heart development are still not clearly defined. To address this issue we have used two approaches to identify genes involved in early chick cardiac development. Differential display previously conducted in our laboratory led to the identification of two gene fragments differentially expressed in the heart that are further described in this thesis. The full-length cDNA sequence of both eukaryotic translation initiation factor-2b (eIF-2b) and NADH cytochrome b5 reductase (b5R) were isolated using library screening. The upreglation of these genes during heart development is expected given the heart is the first functional organ to form in vertebrates and protein synthesis and cell metabolism at this stage of development is maximal. Limitations in the differential display approach led to the development and optimisation of a subtractive hybridisation approach for use with small amounts of cells or tissue. To focus on cardiac gene expression during the initial phases of heart development, subtractive hybridization was performed between the cardiogenic lateral plate mesoderm of Hamburger and Hamilton stage 4 embryos and the heart primordia of stage 9 embryos. Of the 87 independent clones identified by this procedure, 59 matched known sequences with high homology, 25 matched unknown expressed sequence tag (EST) sequences with high homology, and 3 did not match any known sequence on the database. Known genes isolated included those involved in transcription, translation, cell signalling, RNA processing, and energy production. Two of these genes, high mobility group phosphoprotein A2 (HMGA2) and C1-20C, an unknown gene, were chosen for further characterisation. The role of each gene in early chick heart development and indeed development in general, was addressed using techniques such as in situ hybridisation, transfection analysis, in ovo electroporation and RNAi. HMGA2 is a nuclear phosphoprotein commonly referred to as an architectural transcription factor due to its ability to modulate DNA conformation. In keeping with this function, HMGA2/GFP fusion protein was shown to localise to the nucleus and in particular, the nucleolus. In situ hybridisation analysis suggested a role for HMGA2 in heart and somite development. HMGA2 expression was first detected at HH stage 5 in the lateral plate mesoderm, a region synonymous with cells specified to the cardiac fate. HMGA2 was also strongly expressed in the presomitic segmental plate mesoderm and as somites developed from the segmental plate mesoderm, the expression of HMGA2 showed an increasingly more restricted domain corresponding to the level of maturation of the somite. Restriction of HMGA2 expression was first detected in the dorsal region of the epithelial somite, then the dorsomedial lip of the dermomyotome, and finally the migrating epaxial myotome cells. The novel intronless gene, C1-20C, predicts a protein of 148 amino acids containing a putative zinc finger binding domain and prenyl binding motif. Zinc binding assays showed that the zinc finger domain of C1-20C/MBP fusion protein bound over six times the quantity of zinc compared to MBP alone, although not in a 1:1 stoichiometric molar ratio. C1-20C/GFP fusion protein was shown to localise to as yet unidentified intracellular cytoplasmic vesicular compartments. These compartments did not colocalise with the endosome/lysosome pathway, aparently ruling out a role for C1-20C in protein trafficking, recycling or degradation. Expression of C1-20C in the chick embryo suggests a possible role in heart and notochord development and preliminary results using siRNA suggest that C1-20C is involved in normal heart looping.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Biomedical Sciences
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3

Edwards, Lorraine Katy. "Biochemical characterization of mammalian high mobility group protein A2." FIU Digital Commons, 2006. http://digitalcommons.fiu.edu/etd/3118.

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The high mobility group protein HMGA2 is an architectural transcription factor, which is expressed during embryogenesis. Aberrant expression causes benign and malignant tumor formation. The protein possesses three "AT hook" domains and an acidic Cterminal. HMGA2 is natively unstructured, however it forms a homodimer. In this study site-directed mutagenesis was used to create single methionine mutants, HMGA2Q37M, HMGA2I71M and HMGA2Q85M. These mutants were cross-linked using EDC and then cleaved using CNBr to determine which domains are involved in homodimer formation. Our results indicate that the second "AT hook" domain may interact with the C-terminal. We then labeled a peptide containing the C-terminal (CTP) with tetramethylrhodamine-5- maleimide (TRM). We found that the CTP-TMR binds to HMGA2Α95-108, which lacks the C-terminal. These results suggest that the C-terminal is required for homodimer formation. The techniques used within this study can be applied to forensics and with further research HMGA2 may have a forensic application.
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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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Conference papers on the topic "High mobility group phosphoprotein A2"

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Gaffney, Adam W., Takayuki Shiomi, David Sternberg, Divya Mehra, Joshua Sonett, Kiran Chada, and Jeanine M. D'Armiento. "The High Mobility Group A2 Protein As A Lung Cancer Biomarker." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a3059.

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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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Heilmann, T., F. Vondung, C. Borzikowsky, S. Krüger, M. Elessawy, I. Alkatout, A. Wenners, et al. "Cytoplasmic expression of High mobility group A2 (HMGA2) determines survival prognoses in breast cancer patients." In 40. Jahrestagung der Deutschen Gesellschaft für Senologie e.V. © Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0040-1710683.

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