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Academic literature on the topic 'HMGA proteins'

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Published: 11 March 2023

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Journal articles on the topic "HMGA proteins"

1

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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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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PIERANTONI, Giovanna Maria, Valter AGOSTI, Monica FEDELE, Heather BOND, Irene CALIENDO, Gennaro CHIAPPETTA, Francesco LO COCO, et al. "High-mobility group A1 proteins are overexpressed in human leukaemias." Biochemical Journal 372, no. 1 (May 15, 2003): 145–50. http://dx.doi.org/10.1042/bj20021493.

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High-mobility group A (HMGA) proteins are non-histone nuclear proteins that bind DNA and several transcription factors. They are involved in the regulation of chromatin structure and function. HMGA protein expression is low in normal adult tissues, but abundant during embryonic development and in several human tumours. Rearrangements of the HMGA genes have been frequently detected in human benign tumours of mesenchymal origin, e.g. lipomas, lung hamartomas and uterine leiomiomas. HMGA proteins have been implicated in the control of cell growth and differentiation of the pre-adipocytic cell line 3T3-L1. In an attempt to better understand the role of HMGA1 proteins in haematological neoplasias and in the differentiation of haematopietic cells, we have investigated their expression in human leukaemias and in leukaemic cell lines induced to terminal differentiation. Here we report HMGA1 overexpression in most fresh human leukaemias of different origin and in several leukaemic cell lines. Moreover, differentiation of three cell lines towards the megakaryocytic phenotype was associated with HMGA1 protein induction, whereas induction of erythroid and monocytic differentiation generally resulted in reduced HMGA1 expression.
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Lichota, J., and K. D. Grasser. "Interaction of Maize Chromatin-Associated HMG Proteins with Mononucleosomes: Role of Core and Linker Histones." Biological Chemistry 384, no. 7 (July 15, 2003): 1019–27. http://dx.doi.org/10.1515/bc.2003.114.

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AbstractTwo groups of plant chromatin-associated high mobility group (HMG) proteins, namely the HMGA family, typically containing four A/T-hook DNA-binding motifs, and the HMGB family, containing a single HMG-box DNA-binding domain, have been identified. We have examined the interaction of recombinant maize HMGA and five different HMGB proteins with mononucleosomes (containing approx. 165 bp of DNA) purified from micrococcal nuclease-digested maize chromatin. The HMGB proteins interacted with the nucleosomes independent of the presence of the linker histone H1, while the binding of HMGA in the presence of H1 differed from that observed in the absence of H1. HMGA and the HMGB proteins bound H1-containing nucleosome particles with similar affinity. The plant HMG proteins could also bind nucleosomes that were briefly treated with trypsin (removing the N-terminal domains of the core histones), suggesting that the histone N-termini are dispensable for HMG protein binding. In the presence of untreated nucleosomes and trypsinised nucleosomes, HMGB1 could be chemically crosslinked with a core histone, which indicates that the trypsin-resistant part of the histones within the nucleosome is the main interaction partner of HMGB1 rather than the histone N-termini. In conclusion, these results indicate that specific nucleosome binding of the plant HMGB proteins requires simultaneous DNA and histone contacts.
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Balachandran, Akilandeswari, Ajit Zambre, Jagjot Singh Kainth, Lakshmi Dhevi Nagarajha Selvan, Sowmya Parameswaran, Zahra Afrasiabi, Subramanian Krishnakumar, Raghuraman Kannan, and Anandhi Upendran. "Targeting HMGA protein inhibits retinoblastoma cell proliferation." RSC Advances 8, no. 55 (2018): 31510–14. http://dx.doi.org/10.1039/c8ra06026f.

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7

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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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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Fedele, Monica, Giovanna Maria Pierantoni, Pierlorenzo Pallante, and Alfredo Fusco. "High mobility group A-interacting proteins in cancer: focus on chromobox protein homolog 7, homeodomain interacting protein kinase 2 and PATZ." Journal of Nucleic Acids Investigation 3, no. 1 (March 16, 2012): 1. http://dx.doi.org/10.4081/jnai.2012.3988.

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The High Mobility Group A (HMGA) proteins, a family of DNA architectural factors, by interacting with different proteins play crucial roles in neoplastic transformation of a wide range of tissues. Therefore, the search for HMGA-interacting partners was carried out by several laboratories in order to investigate the mechanisms underlying HMGA-dependent tumorigenesis. Three of the several HMGA-binding proteins are discussed in this review. These are the Chromobox family protein (chromobox protein homolog 7, CBX7), the homeodomain interacting protein kinase 2 (HIPK2) and the POZ/domain and Kruppel zinc finger family member, PATZ. All of them play a critical role in tumorigenesis, and may also be independent markers of cancer. Their activities are linked to cell cycle, apoptosis and senescence. In this review, we discuss the properties of each protein, including their effect on HMGA1 functions, and propose a model accounting for how their activities might be coordinated.
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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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Dissertations / Theses on the topic "HMGA proteins"

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Beitzel, Brett F. "The role of HMGA proteins in retroviral integration /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2003. http://wwwlib.umi.com/cr/ucsd/fullcit?p3099924.

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Pellarin, Ilenia. "HMGA PROTEINS IN EPITHELIAL-MESENCHYMAL TRANSITION AND TUMOUR PROGRESSION." Doctoral thesis, Università degli studi di Trieste, 2014. http://hdl.handle.net/10077/10117.

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2012/2013
High Mobility Group A (HMGA1a, HMGA1b and HMGA2) proteins are architectural nuclear factors, physiological expressed during embryonic development and re-expressed at high levels following neoplastic transformation, playing essential functions in both these processes thanks to their particular plasticity and consequently multifunctionality. HMGA are involved in a wide number of cellular processes, including Epithelial-Mesenchymal transition (EMT), a biologic developmental process characterized by the conversion of epithelial cells to motile mesenchymal ones, with increased capacity of migration and invasion. EMT plays a key role during the progression of different tumours, including breast cancer and also HMGA have been linked to these processes in the acquisition of tumourigenic features. Consequently taking advantage of different breast cancer cell lines to recreate an "EMT model" we have investigated the role of HMGA proteins in EMT and breast carcinoma. We have developed a cellular model, stable for the overexpression of HMGA1 using the human breast cancer cell line MCF7. We have explored different aspects of tumourigenesis, performing transwell migration and invasion assays, demonstrating that cells with high levels of HMGA1 migrate and invade at a higher and significant level in comparison to control cells. Moreover this data was also confirmed with the development of an inducible cell line for HMGA1 overexpression. Therefore we have examined the expression status of different genes, including several specific EMT markers at mRNA level with Real Time PCR, observing a pre-malignant change towards mesenchymal status. We have investigated the response after DNA damage induced by doxorubicin drug, by colony formation assay, demonstrating that HMGA1 overexpressing cells confer a survival advantage to the cells, being able to survive and form a significant higher number of colonies in respect to control cells. Therefore to study deeper the role of HMGA in EMT, we have developed other two cellular systems, a human cellular model of EMT in MDA-MB-468 human breast carcinoma cells treated with Epidermal Growth Factor (EGF) and the well known EMT model, elicited by Transforming Growth Factor-β (TGF-β) in murine mammary epithelial NMuMG cells, in which HMGA2 is functionally determinant. We have demonstrated by Real Time PCR of EMT markers, Western Blot analyses and immunofluorescence the effective reliability of these cellular models, confirmed also by a dramatic change in morphology of treated cells, towards a mesenchymal phenotype. Concluding we have interestingly observed that overexpression of HMGA1 could confer some tumourigenic features (i.e. migration, invasion) and survival advantage to the cells in the MCF7 model after a cellular DNA damage induction; therefore we have different suggestions that HMGA are involved in EMT in other different cellular models.
Le proteine HMGA (HMGA1a, HMGA1b e HMGA2), definite come fattori architetturali della cromatina, sono fisiologicamente espresse ad alti livelli nel corso dello sviluppo embrionale diminuendo gradualmente la loro espressione nel corso del differenziamento. Sono coinvolte, oltre all'aspetto fisiologico, anche in diverse condizioni patologiche, essendo ad esempio ri-espresse ad alti livelli nel corso della trasformazione neoplastica, esercitando funzioni essenziali grazie alla loro alta plasticità, alle peculiari caratteristiche biochimiche e conseguente multifunzionalità. Le proteine HMGA utilizzano diversi meccanismi per esercitare la loro funzione nell'acquisire capacità trasformanti, inclusa la transizione epitelio-mesenchimale. Questo processo biologico, primariamente identificato come fattore chiave dello sviluppo embrionale, è risultato di essere di fondamentale importanza anche nella trasformazione tumorale. Mediante questo meccanismo una cellula epiteliale, mediante molteplici cambiamenti genetici e biochimici acquisisce caratteristiche tipiche di uno "stato mesenchimale", caratterizzato ad esempio da un'aumentata capacità invasiva e migratoria. La transizione epitelio-mesenchimale esercita un ruolo chiave nel corso della progressione di diverse tipologie tumorali, incluso il cancro al seno, a cui in particolare anche le proteine HMGA sono state associate. L'obiettivo della Tesi è quindi quello di studiare il ruolo delle proteine HMGA nella transizione epitelio-mesenchimale e in particolare nel cancro al seno. A questo scopo abbiamo sviluppato diversi modelli cellulari di transizione epitelio-mesenchimale. Il primo modello ha previsto la creazione di un sistema stabile di over-espressione della proteina HMGA1 nella linea epiteliale di tumore al seno MCF7. Abbiamo analizzato diversi aspetti della tumorigenesi mediante saggi di migrazione ed invasione in transwell, dimostrando come alti livelli della proteina HMGA1 inducano un aumento di entrambi i processi rispetto ad una condizione di controllo. Inoltre i dati di migrazione sono stati confermati in un sistema inducibile per la over-espressione di HMGA1 nella stessa linea cellulare MCF7 e da saggi condotti in condizione di deplezione di HMGA1 attraverso strategie di silenziamento, dimostrando ulteriormente come la migrazione sia un fenomeno HMGA1 dipendente. Abbiamo inoltre esaminato lo stato di espressione di diversi geni, inclusi specifici marker di transizione epitelio-mesenchimale, mediante analisi di Real Time PCR, osservando un cambiamento verso una condizione di tipo pre-maligno e di parziale transizione ad uno stato mesenchimale. Inoltre è stata verificata la risposta al danno indotto da doxorubicina mediante saggio di colony formation, dimostrando come cellule over-esprimenti HMGA1 possiedano un vantaggio in termini di sopravvivenza e di numero di colonie formate, rispetto alle cellule di controllo. Per approfondire ulteriormente il ruolo esercitato dalle HMGA nella transizione epitelio-mesenchimale, sono stati sviluppati altri due modelli cellulari, uno nella linea epiteliale umana di cancro al seno MDA-MB-468 trattata con EGF (Epidermal Growth Factor), l'altro nella linea cellulare murina mammaria di tipo epiteliale NMuMG, trattata con TGF-β (Transforming Growth Factor-β), in cui l'azione di HMGA2 è stato dimostrato avere un ruolo determinante. Mediante analisi di Real Time PCR di marker di transizione epitelio-mesenchimale, di Western Blot e di immunofluorescenza abbiamo dimostrato l'effettiva solidità di questi modelli cellulari, confermato anche dal fatto che è possibile apprezzare un consistente cambio morfologico verso un fenotipo mesenchimale e una concomitante over-espressione delle proteine HMGA. Da questi modelli è stato quindi possibile evincere come le HMGA siano coinvolte nell'acquisizione di caratteristiche di tipo tumorale anche mediante processi di transizione epitelio-mesenchimale e come questi modelli siano utili al fine di semplificare network molecolari.
XXV Ciclo
1984
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Jakimovska, Frosina. "Characterization of the interaction between nucleophosmin (NPM) and highmobility group a (HMGA) proteins." Doctoral thesis, Università degli studi di Trieste, 2008. http://hdl.handle.net/10077/2760.

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2006/2007
ABSTRACT HMGA proteins are members of the high mobility group (HMG) non-histone, architectural chromosomal proteins. The HMGA family consists of: A1a, A1b and A2, the first two being isoforms produced by alternative splicing. These are small proteins, about 100aa residues long, characterized by three basic stretches of AT-hooks which bind to the AT-rich sequences on the DNA minor groove. They are normally present in rapidly proliferating cells (embryo) whereas upon differentiation the levels of these proteins decrease until they are nearly absent from adult cells. Overexpression of these proteins has been correlated with various types of neoplastic transformations. The interaction network of HMGA has been an object of study for years in our laboratory and one of the most intriguing protein-protein interactions studied is the one between HMGA and nucleophosmin. Nucleophosmin (NPM, B23, numatrin or NO38) is one of the most abundant phosphoproteins, mainly localized in the nucleoli but it also shuttles between the nucleus and the cytoplasm. This versatile protein has been proven to be involved in various cellular functions and related to both proliferative and growth-suppressive roles in the cell. The first evidence of the interaction HMGA2-NPM in our lab has been obtained by in vitro assays (affinity chromatography). The step ahead was to see if this interaction occurs in vivo and if it does, to try to find ts functional significance. Thus,immunoprecipitation (IP) experiments were performed.The first one gave the proof thet interaction between HMGA2 protein and NPM (transfected and endogenous) occurs. The second IP gave the evidence that interaction occurs between HMGA1a and NPM too. This in vivo protein-protein interaction was to be given a functional significance. We tested by siRNA HMGA1a treatment if downregulation of HMGA1a expression influences the expression of the SOD2 gene (regulated by NPM). The effect of the HMGA1a silencing has proven to be very slight on the SOD2 gene (a 14% of expression reduction). EMSA experiments have been performed in order to test the effect of NPM on the DNA binding properties of the HMGA2 protein with the DNA probes E3 and HCRII. In both cases it has been observed that NPM increases the DNA binding affinity of the HMGA2 protein.
1979
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Zammitti, Salvina. "Post-translational modifications of high mobility group a (HMGA) proteins in neoplastic transformation." Doctoral thesis, Università degli studi di Trieste, 2010. http://hdl.handle.net/10077/3614.

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2008/2009
Le proteine HMG (High Mobility Group) sono la famiglia più ampiamente e meglio caratterizata fra le proteine cromosomiche non istoniche. Esse sono raggruppate in tre sottofamiglie: HMGA, HMGB ed HMGN. Ciascuna sottofamiglia è caraterizzata da una sequenza o motivo funzionale attraverso il quale sono capaci di legarsi a specifiche strutture sul DNA o sulla cromatina. La famiglia HMGA di mammifero consiste di due geni funzionali: HMGA1 and HMGA2. Lo splicing alternativo del trascritto del gene HMGA1 dà origine alle proteine HMGA1a ed HMGA1b. La proteina HMGA2 è codificata dall’altro gene. Le proteine HMGA partecipano a specifiche interazioni proteina-DNA e proteina-proteina inducendo sia cambiamenti strutturali della cromatina che la formazione di complessi macromolecolari su regioni promotrici//enhancer di diversi geni. Pertanto esse sono descritte come fattori archietturali della trascrizione. Grazie alla loro multifunzionalità, ese partecipano a diversi processi biologici quali l’integrazione virale, l’embriogenesi e la differenziazione, l’apoptosi, la senescenza, la trasformazione neoplastica ed il riparo del DNA. La caratteristica di proteine oncofetali attribuita alle HMGA prende origine dal fatto che esse sono (i) altamente espresse durante l’embriogenesi, (ii) assenti o espresse a bassi livelli nei tessuti adulti e (iii) altamente riespresse nelle cellule trasformate. Queste proteine sono, tra le proteine nucleari, quelle più soggette a modificazioni post-traduzionali e le loro attività sono modulate da una ampia varietà di modificazioni post-traduzionali. In questo lavoro di tesi, grazie all’uso di linee cellulari di cancro mammario in cui è stata indotta la reversione del fenotipo neoplastico tramite trattamento farmacologico e successive analisi di spettrometria di massa, si è ricercata una connessione tra le modificazioni post-traduzionali delle HMGA ed il processo di trasformazione neoplastica. Inoltre, grazie ad una nuova strategia in vitro sviluppata nel nostro laboratorio per l’identificazione di partner molecolari delle proteine HMGA, si è dimostrato che la proteina HMGA1a si associa con la proteina Ku70, che è un fattore chiave coinvolto nel riparo delle rotture al doppio filamento di DNA attraverso il “non-homologous end joining”. Numerose evidenze sperimentali suggeriscono che l’inibizione del riparo del DNA da parte delle HMGA posa contribuire alle instabilità genetiche e cromosomiche comunemente ritrovate nelle celle cancerose. Perciò, si è ricercata una relazione funzionale tra le proteine HMGA e le proteine chiave nel meccanismo di riparo del DNA attraverso “non-homologous end joining”, focalizzando l’attenzione in particolare sulla proteina DNA-PK (DNA-dependent protein kinase), che ha una funzione regolatrice chiave in questo processo.
XXII Ciclo
1973
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ALTAMURA, SANDRO. "IDENTIFICAZIONE E CARATTERIZZAZIONE DI PARTNERS MOLECOLARI DELLE PROTEINE HMGA." Doctoral thesis, Università degli studi di Trieste, 2007. http://thesis2.sba.units.it/store/handle/item/12290.

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Uesugi, Hiroko. "Prevalence and characterization of novel P-ANCA, antibodies to the high mobility group non-histone chromosomal proteins HMG1 and HMG2, in systemic rheumatic diseases." Kyoto University, 2000. http://hdl.handle.net/2433/151400.

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Ragab, Anan. "Genetic and functional studies on abundant Drosophila HMGB proteins." Thesis, University of Cambridge, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.615068.

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Zayed, Hatem. "Improvement of the sleeping beauty transposon system." [S.l. : s.n.], 2003. http://www.diss.fu-berlin.de/2003/243/index.html.

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Adair, Jennifer Eileen. "Molecular and genetic influence of HMGA1 proteins on nucleotide excision repair." Online access for everyone, 2005. http://www.dissertations.wsu.edu/Dissertations/Fall2005/j%5Fadair%5F120605.pdf.

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Arnoldo, Laura. "HMGA1 proteins regulate gene expression by modulating histone H3 phosphorylation." Doctoral thesis, Università degli studi di Trieste, 2014. http://hdl.handle.net/10077/10112.

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2012/2013
HMGA1 is an oncogene encoding for an architectural transcription factor that affects fundamental cell processes, leading to neoplastic transformation. The two main mechanisms by which HMGA1 protein is known to be involved in cancer concern the regulation of gene expression by altering DNA structure and interacting with a conspicuous number of transcription factors. Here we provide evidence of an additional level of gene expression regulation exploited by HMGA1 to exert its oncogenic activity. Starting from protein-protein interaction data showing that HMGA1 interacts with histones, we show that HMGA1 regulates gene expression by affecting the epigenetic status of cancer cells. In particular, it modulates the signalling cascade mediated by the RAS/RAF/MEKK/ERK/RSK2 pathway regulating the levels of histone H3 phosphorylation at Serine 10 and Serine 28. We demonstrate that the down-regulation of these two H3 post-translational modifications by HMGA1 silencing and by inhibitors of the RAS/RAF/MEKK/ERK pathway is linked to cell migration decrease and morphological changes resembling the mesenchymal to epithelial transition.
HMGA1 è un oncogene codificante per un fattore trascrizionale architetturale che influenza fondamentali processi cellulari, portando alla trasformazione neoplastica. I due principali meccanismi tramite cui la proteina HMGA1 è nota essere coinvolta nel cancro riguardano la regolazione dell’espressione genica tramite l’alterazione della struttura del DNA e l’interazione con un cospicuo numero di fattori di trascrizione. Qui forniamo la prova di un addizionale livello di regolazione dell’espressione genica sfruttato da HMGA1 per esercitare la sua attività oncogenica. Partendo da dati d’interazione proteina-proteina che mostrano che HMGA1 interagisce con gli istoni, mostriamo che HMGA1 regola l’espressione genica influenzando lo stato epigenetico delle cellule cancerose. In particolare, essa modula la cascata di segnalazione mediata dalla via di RAS/RAF/MEKK/ERK/RSK2 regolando i livelli di fosforilazione dell’istone H3 sulla Serina 10 e sulla Serina 28. Noi dimostriamo che la down-regolazione di queste due modificazioni post-traduzionali di H3 tramite il silenziamento di HMGA1 e l’utilizzo di inibitori della via di RAS/RAF/MEKK/ERK/RSK2 è correlata alla diminuzione della migrazione cellulare e a cambiamenti morfologici che ricordano la transizione mesenchimo-epiteliale.
XXV Ciclo
1983
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Books on the topic "HMGA proteins"

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Mumford, Katherine Laura. Genomic cloning and gene organisation of the Drosophila HMG box protein DSox14. Portsmouth: University of Portsmouth, School of Biological Sciences, 1999.

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

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An, Woojin. Interaction of linker proteins, H1 and HMG1, with nucleosome reconstituted on positioning sequences. 1998.

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Siino, Joseph S. Replacement of conserved threonines by alanine residues: Effect on the dissociation constant of recombinant human HMG-I. 1992.

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Lehn, Donald Andrew. The non-histone chromosomal protein HMG-I(Y) and its interactions with nucleic acids. 1989.

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Wiklund, Olov, and Jan Borén. Pathogenesis of atherosclerosis: lipid metabolism. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780198755777.003.0011.

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Lipids are carried in plasma as microparticles, lipoproteins, composed of a core of hydrophobic lipids and a surface of amphipathic lipids. In addition, the particles carry proteins (i.e. apolipoproteins). The proteins have key functions in the metabolism as receptor ligands, enzymes or activators. Lipoproteins are classified based on density into: chylomicrons, VLDL, IDL, LDL, and HDL. Retention of apoB-containing lipoproteins (LDL, IDL, and VLDL) in the arterial intima is the initiating event in the development of atherosclerosis. Retention is mediated by binding of apoB to structural proteoglycans in the intima. Increased plasma concentration of apoB-containing lipoproteins is the main risk factor for atherosclerotic cardiovascular disease (CVD) and the causative role of LDL has been demonstrated in several studies. Lp(a) is a subclass of LDL and elevated Lp(a) is an independent risk-factor, primarily genetically mediated. Genetic data support that high Lp(a) causes atherosclerosis. Elevated triglycerides in plasma are associated with increased risk for CVD. Whether triglycerides directly induce atherogenesis is still unclear, but current data strongly support that remnant particles from triglyceride-rich lipoproteins are causal. HDL are lipoproteins that have been considered to be important for reversed cholesterol transport. Low HDL is a strong risk-factor for CVD. However, the causative role of HDL is debated and intervention studies to raise HDL have not been successful. Reduction of LDL is the main target for prevention and treatment, using drugs that inhibit the enzyme HMG-CoA reductase, i.e. statins. Other drugs for LDL reduction and to modify other lipoproteins may further reduce risk, and new therapeutic targets are explored.
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Book chapters on the topic "HMGA proteins"

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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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Kotzka, Jörg, Wilhelm Krone, and Dirk Müller-Wieland. "Sterol-regulatory element binding proteins (SREBPs): gene-regulatory target of statin action." In HMG-CoA Reductase Inhibitors, 35–54. Basel: Birkhäuser Basel, 2002. http://dx.doi.org/10.1007/978-3-0348-8135-7_3.

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Maher, L. James. "Studies of Sequence-Nonspecific HMGB DNA-Binding Proteins." In Biological and Medical Physics, Biomedical Engineering, 143–62. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-0-387-92808-1_7.

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Goodwin, G. H., R. H. Nicolas, C. A. Wright, and S. Zavou. "The Structures and Functions of the Low Molecular Weight HMG Proteins." In Chromosomal Proteins and Gene Expression, 221–38. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7615-6_15.

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Laland, S. G., T. Lund, and J. Holtlund. "Post-Translational Modification of the Low Molecular Weight HMG Chromosomal Proteins." In Chromosomal Proteins and Gene Expression, 239–47. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7615-6_16.

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Puigdomènech, Pere, and Matilde Jose. "Structure and Function in the HMG-1 Family of Chromosomal Proteins." In Chromosomal Proteins and Gene Expression, 249–61. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7615-6_17.

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Wittemann, B., F. A. Bautz, H. Michels, and H. Truckenbrodt. "Autoantibodies to Nonhistone Chromosomal Proteins HMG-1 and HMG-2 in Subsets of Juvenile Chronic Arthritis (JCA)." In Molecular and Cell Biology of Autoantibodies and Autoimmunity. Abstracts, 105–6. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-46681-6_89.

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McA’Nulty, M. M., and S. J. Lippard. "Consequences of HMG-Domain Protein Binding to Cisplatin-Modified DNA." In Nucleic Acids and Molecular Biology, 264–84. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79488-9_13.

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Billings, Paul C., and Edward N. Hughes. "Role of HMG and Other Proteins in Recognition of Cisplatin DNA Damage." In DNA Damage and Repair, 133–41. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-59259-455-9_9.

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Conference papers on the topic "HMGA proteins"

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Fatchiyah, Fatchiyah, and Shella Clarista Natasia. "Inhibition potency of HMGR enzyme against hypercholesterolemia by bioactive peptides of CSN1S2 protein from caprine milk." In THE 8TH ANNUAL BASIC SCIENCE INTERNATIONAL CONFERENCE: Coverage of Basic Sciences toward the World’s Sustainability Challanges. Author(s), 2018. http://dx.doi.org/10.1063/1.5062812.

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Sa’adah, Noor Nailis, Elshinta Riantica, Awik Puji Dyah Nurhayati, Nova Maulidina Ashuri, and Dewi Hidayati. "Molecular Docking of Anthocyanin Compound as Anti-Hyperlipidemia Against PPARα, HMG-CoA Reductase and ACAT Proteins." In 7th International Conference on Biological Science (ICBS 2021). Paris, France: Atlantis Press, 2022. http://dx.doi.org/10.2991/absr.k.220406.033.

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Esposito, Francesco, Mara Tornincasa, Eleonora Borbone, and Giovanna Maria Pierantoni. "Abstract 206: High mobility group A1(HMGA1) proteins localize at the mitochondria and inhibit the p53-mediated intrinsic-apoptotic pathway." 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.am2011-206.

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Takaha, Natsuki, Ichiro Takeuchi, Yoshihiro Sowa, Yasunori Kimura, Terukazu Nakamura, Fumiya Hongo, Kazuya Mikami, Akihiro Kawauchi, and Tsuneharu Miki. "Abstract 606: Expression and role of high mobility group protein AT-hook 1 (HMGA1) in human renal cell 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.am2011-606.

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Batista, Keila Zaniboni Siqueira, Andressa Karine Boehringer, Marina Schndeider, Vinicius Vialle Ferreira, and Mercedes Gabriela Ratto Reiter. "DOSAGEM DE IMUNOGLOBULINA A E PROTEÍNAS TOTAIS EM AMOSTRAS DO BANCO DE LEITE HUMANO DE BLUMENAU/SC." In I Congresso Brasileiro de Imunologia On-line. Revista Multidisciplinar em Saúde, 2021. http://dx.doi.org/10.51161/rems/959.

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Introdução: O leite humano apresenta componentes indispensáveis para defesa e proteção do recém-nascido. Variações na qualidade do leite materno afetam o desenvolvimento, saúde e crescimento do recém-nascido, tornando-o vulnerável. Objetivos: determinar a dosagem de Imunoglobulina A (IgA) e proteínas totais em amostras de leite materno do Banco de Leite Humano (BLH) de Blumenau/SC; assim como determinar possíveis fatores que podem influenciar nessas dosagens. Material e métodos: Estudo transversal, com análise de 105 amostras de leite provenientes do BLH de Blumenau/SC. A dosagem das proteínas totais foi realizada em equipamento Human Milk Analyser (HMA) por metodologia de infravermelho, enquanto a dosagem da IgA foi realizada pela técnica de turbidimetria. Dados sobre estágio do leite, idade materna, IMC, tipo de parto, tempo gestacional e peso do bebê ao nascer também foram coletados. Resultados: Em relação a dosagem do anticorpo secretório, o leite maduro apresentou uma redução de 26% na quantidade de IgA em relação ao colostro. Quando associado ao tipo de parto, observou-se uma redução de 21% na quantidade de proteínas do leite materno quando realizado parto vaginal. Os valores de proteínas totais apresentaram correlação estatisticamente significativa com a idade gestacional, IMC inicial e final. A correlação do nível de proteínas totais com o IMC, tanto inicial como final da mãe, demonstrou que há influência sobre a dosagem de proteínas no leite materno, ou seja, quanto maior o IMC da mãe, maior a dosagem de proteínas totais do leite. Não houve diferenças significativas entre IgA com as demais variáveis analisadas. Apesar disso, a quantidade de IgA apresentou uma tendência decrescente em relação ao aumento da idade materna. Conclusão: a dosagem média das proteínas foi relativamente abaixo da média da literatura; diferindo da dosagem da IgA que se apresentou como esperado. Houve redução na dosagem de IgA no leite maduro em relação ao colostro e diminuição na quantidade de proteínas no parto vaginal. Quanto as correlações, a variável proteínas apresentou associação com Idade materna, IMC inicial e final; diferente da variável IgA, na qual não houve nenhuma correlação significativa.
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Lobbardi, Riadh, Jordan Pinder, Barbara Martinez, Jessica Blackburn, Nouran Abdelfattah, Debra Toiber, Manon De Waard, et al. "Abstract 3865: Thymocyte selection-associated HMG box protein (TOX) induces genomic instability in T-cell acute lymphoblastic leukemia." 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.am2015-3865.

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Lobbardi, Riadh, Jordan Pinder, Barbara Martinez-Pastor, Jessica Blackburn, Brian J. Abraham, Marc Mansour, Nouran S. Abdelfattah, et al. "Abstract 3583: Thymocyte selection-associated HMG box protein (TOX) induces genomic instability in T-cell acute lymphoblastic leukemia." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3583.

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Chia, Lionel, Lingling Xian, Guangjing Zhu, Mohammad Heydarian, William B. Issacs, Karen Reddy, and Linda Smith Resar. "Abstract 3352: HMGA1 chromatin remodeling protein induces HOXB13 to drive cancer stem cell properties and tumor progression in prostate cancer models." 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.am2018-3352.

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Scott, Andrew C., Steven Camara, Peter Lauer, Alexandra Synder, Dmitriy Zamarin, Tyler Walther, Olivier Levy, et al. "Abstract A215: Thymocyte selection-associated HMG box protein TOX is a master regulator of tumor-specific T-cell dysfunction." In Abstracts: Fourth CRI-CIMT-EATI-AACR International Cancer Immunotherapy Conference: Translating Science into Survival; September 30 - October 3, 2018; New York, NY. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/2326-6074.cricimteatiaacr18-a215.

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Rajan, Neena, Nate Stetson, Robert Maidhof, Mitchell Levine, and Nadeen Chahine. "In Vivo Administration of an Inflammatory Stimulant can Trigger Loss of Biomechanical and Biochemical Properties of the Intervertebral Disc." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80495.

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Human intervertebral disc (IVD) degeneration is accompanied by chronic inflammation, particularly seen in the elevated levels of pro-inflammatory cytokines IL-1β and TNF-α [1–3]. Animal models of disc degeneration (DD) using stab or laceration of the disc generally reproduce morphological changes of IVD degeneration. However, inflammatory changes in these models are thought to be acute and transient post injury [4–6]. The goal of this study is to explore the effect of direct inflammatory stimulation of the IVD on disc biochemical and biomechanical properties in vivo. We utilize lipopolysaccharide (LPS), an inflammatory stimulant that provokes secretion of multiple cytokines by disc cells. We have previously shown that direct injection of LPS into the disc results in significantly higher protein levels of IL-1β, TNF-α, HMGB-1 and MIF vs. sham injection up to 7 days post administration [7]. The goal of this study is to explore the dose-dependent response of this inflammatory stimulation on the biochemical and biomechanical properties of IVD in vivo. We hypothesize that LPS stimulation mimics the pathophysiology of DD by triggering a group of cytokines that are associated with IVD degeneration. LPS is administered using micro needles (<10% disc height) in order to minimize the potential disruption by needle injection.
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Reports on the topic "HMGA proteins"

1

Boonyaratanakornkit, Viroj. Chromatin HMG-I (Y) as a Co-regulatory Protein for Estrogen Receptor Action in Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, May 1999. http://dx.doi.org/10.21236/ada368525.

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Boonyaratanakornkit, Viroj. Chromatin HMG-I(Y) as a Co-Regulatory Protein for Estrogen Receptor Action in Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, April 2000. http://dx.doi.org/10.21236/ada391523.

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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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