Relevant bibliographies by topics / PML-retinoic acid receptor-a

Contents

  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'PML-retinoic acid receptor-a'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'PML-retinoic acid receptor-a.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "PML-retinoic acid receptor-a"

1

Yoshida, Hitoshi, Hitoshi Ichikawa, Yusuke Tagata, Takuo Katsumoto, Kazunori Ohnishi, Yukihiro Akao, Tomoki Naoe, Pier Paolo Pandolfi, and Issay Kitabayashi. "PML-Retinoic Acid Receptor α Inhibits PML IV Enhancement of PU.1-Induced C/EBPε Expression in Myeloid Differentiation." Molecular and Cellular Biology 27, no. 16 (June 11, 2007): 5819–34. http://dx.doi.org/10.1128/mcb.02422-06.

Full text
Abstract:
ABSTRACT PML and PU.1 play important roles in myeloid differentiation. PML-deficient mice have an impaired capacity for terminal maturation of their myeloid precursor cells. This finding has been explained, at least in part, by the lack of PML action to modulate retinoic acid-differentiating activities. In this study, we found that C/EBPε expression is reduced in PML-deficient mice. We showed that PU.1 directly activates the transcription of the C/EBPε gene that is essential for granulocytic differentiation. The type IV isoform of PML interacted with PU.1, promoted its association with p300, and then enhanced PU.1-induced transcription and granulocytic differentiation. In contrast to PML IV, the leukemia-associated PML-retinoic acid receptor α fusion protein dissociated the PU.1/PML IV/p300 complex and inhibited PU.1-induced transcription. These results suggest a novel pathogenic mechanism of the PML-retinoic acid receptor α fusion protein in acute promyelocytic leukemia.
APA, Harvard, Vancouver, ISO, and other styles
2

van Wageningen, Sake, Marleen C. Breems-de Ridder, Gorica Nikoloski, Claudia A. J. Erpelinck-Verschueren, Jeannet Nigten, Bob Löwenberg, Theo de Witte, Bert A. van der Reijden, and Joop H. Jansen. "SP1 and NF-Y-Dependent Gene Transactivation Defines a Gain-of-Function for the PML-RARα Oncoprotein." Blood 106, no. 11 (November 16, 2005): 743. http://dx.doi.org/10.1182/blood.v106.11.743.743.

Full text
Abstract:
Abstract PML-RARa is the product of the chromosomal translocation t(15;17) and is the causative oncogene in more than 98% of the cases of acute promyelocytic leukemia. PML-RARa interferes with the transcription of retinoic acid receptor target genes in a dominant manner, contributing to the transformation of the cells. RARa regulates transcription via heterodimerisation with RXR. PML-RARa can bind as a homodimer to the same sequences as RARa/RXR. At supra-physiological dosis of all-trans retionoic acid (ATRA), the block in differentiation in APL can be overcome. ATRA releases co-repressors from PML-RARa and activates RARa target genes. The ID1 gene is rapidly induced by ATRA in acute promyelocytic leukemia cells. Promoter analysis showed that the ID1 promoter was activated by PML-RARa but, unexpectedly, not by wild type RARa/RXR. Surprisingly, PML-RARa lacking the DNA binding domain could still transactivate the ID1 promoter indicating that transactivation was mediated without direct DNA binding. Promoter deletion studies showed that adjacent NF-Y and SP1 binding sites were essential for this transactivation. A direct physical interaction was shown between PML-RARa and SP1 in vitro and chromatin immunoprecepitation assays confirmed that a complex of PML-RARa/NF-Y/Sp1 is present on the ID1 promoter in vivo. In addition, we found that ectopic expression of PML-RARa induced expression of the endogenous ID1 gene in response to retinoic acid. We propose a novel, gain-of-function model for PML-RARa in which the fusion protein interferes with the transcription of SP1-NF-Y regulated genes. Interference is mediated without DNA-binding, through direct interaction with SP1. This implicates that apart from the previously described deregulation of retinoic acid receptor target genes, PML-RARa may deregulate an additional class of genes that are nomally not regulated by retinoid receptors.
APA, Harvard, Vancouver, ISO, and other styles
3

Müller, Carsten, Rong Yang, Dorothy J. Park, Hubert Serve, Wolfgang E. Berdel, and H. Phillip Koeffler. "The aberrant fusion proteins PML-RARα and PLZF-RARα contribute to the overexpression of cyclin A1 in acute promyelocytic leukemia." Blood 96, no. 12 (December 1, 2000): 3894–99. http://dx.doi.org/10.1182/blood.v96.12.3894.

Full text
Abstract:
Abstract Cyclin A1 is a newly discovered cyclin that is overexpressed in certain myeloid leukemias. Previously, the authors found that the frequency of cyclin A1 overexpression is especially high in acute promyelocytic leukemia (APL). In this study, the authors investigated the mechanism of cyclin A1 overexpression in APL cells and showed that the APL-associated aberrant fusion proteins (PML–retinoic acid receptor alpha [PML-RARα] or PLZF-RARα) caused the increased levels of cyclin A1 in these cells. The ectopic expression of either PML-RARα or PLZF-RARα in U937 cells, a non-APL myeloid cell line, led to a dramatic increase of cyclin A1 messenger RNA and protein. This elevation of cyclin A1 was reversed by treatment with all-trans retinoic acid (ATRA) in cells expressing PML-RARα but not PLZF-RARα. ATRA also greatly reduced the high levels of cyclin A1 in the APL cell lines NB4 and UF-1. No effect of ATRA on cyclin A1 levels was found in the ATRA-resistant NB4-R2 cells. Further studies using ligands selective for various retinoic acid receptors suggested that cyclin A1 expression is negatively regulated by activated RARα. Reporter assays showed that PML-RARα led to activation of the cyclin A1 promoter. Addition of ATRA inhibited PML-RARα–induced cyclin A1 promoter activity. Taken together, our data suggest that PML-RARα and PLZF-RARα cause the high-level expression of cyclin A1 seen in acute promyelocytic leukemia.
APA, Harvard, Vancouver, ISO, and other styles
4

Müller, Carsten, Rong Yang, Dorothy J. Park, Hubert Serve, Wolfgang E. Berdel, and H. Phillip Koeffler. "The aberrant fusion proteins PML-RARα and PLZF-RARα contribute to the overexpression of cyclin A1 in acute promyelocytic leukemia." Blood 96, no. 12 (December 1, 2000): 3894–99. http://dx.doi.org/10.1182/blood.v96.12.3894.h8003894_3894_3899.

Full text
Abstract:
Cyclin A1 is a newly discovered cyclin that is overexpressed in certain myeloid leukemias. Previously, the authors found that the frequency of cyclin A1 overexpression is especially high in acute promyelocytic leukemia (APL). In this study, the authors investigated the mechanism of cyclin A1 overexpression in APL cells and showed that the APL-associated aberrant fusion proteins (PML–retinoic acid receptor alpha [PML-RARα] or PLZF-RARα) caused the increased levels of cyclin A1 in these cells. The ectopic expression of either PML-RARα or PLZF-RARα in U937 cells, a non-APL myeloid cell line, led to a dramatic increase of cyclin A1 messenger RNA and protein. This elevation of cyclin A1 was reversed by treatment with all-trans retinoic acid (ATRA) in cells expressing PML-RARα but not PLZF-RARα. ATRA also greatly reduced the high levels of cyclin A1 in the APL cell lines NB4 and UF-1. No effect of ATRA on cyclin A1 levels was found in the ATRA-resistant NB4-R2 cells. Further studies using ligands selective for various retinoic acid receptors suggested that cyclin A1 expression is negatively regulated by activated RARα. Reporter assays showed that PML-RARα led to activation of the cyclin A1 promoter. Addition of ATRA inhibited PML-RARα–induced cyclin A1 promoter activity. Taken together, our data suggest that PML-RARα and PLZF-RARα cause the high-level expression of cyclin A1 seen in acute promyelocytic leukemia.
APA, Harvard, Vancouver, ISO, and other styles
5

O'Connell, Paul A., Patricia A. Madureira, Jason N. Berman, Robert S. Liwski, and David M. Waisman. "Regulation of S100A10 by the PML-RAR-α oncoprotein." Blood 117, no. 15 (April 14, 2011): 4095–105. http://dx.doi.org/10.1182/blood-2010-07-298851.

Full text
Abstract:
Abstract Acute promyelocytic leukemia (APL) is a distinct subtype of acute myeloid leukemia that results from the expression of the promyelocytic leukemia–retinoic acid receptor α (PML-RAR-α) oncoprotein. It is characterized by severe hemorrhagic complications due in part to excessive fibrinolysis, resulting from the excessive generation of the fibrinolytic enzyme, plasmin, at the cell surface of the PML cells. The treatment of patients with all-trans retinoic acid (ATRA) effectively ameliorates the disease by promoting the destruction of the PML-RAR-α oncoprotein. In the present study we show for the first time that the plasminogen receptor, S100A10, is present on the extracellular surface of APL cells and is rapidly down-regulated in response to all-trans retinoic acid. The loss of S100A10 is concomitant with a loss in fibrinolytic activity. Furthermore, the induced expression of the PML-RAR-α oncoprotein increased the expression of cell surface S100A10 and also caused a dramatic increase in fibrinolytic activity. Depletion of S100A10 by RNA interference effectively blocked the enhanced fibrinolytic activity observed after induction of the PML-RAR-α oncoprotein. These experiments show that S100A10 plays a crucial role in the generation of plasmin leading to fibrinolysis, thus providing a link to the clinical hemorrhagic phenotype of APL.
APA, Harvard, Vancouver, ISO, and other styles
6

Sohal, Jastinder, Vernon T. Phan, Philip V. Chan, Elizabeth M. Davis, Bhumi Patel, Louise M. Kelly, Tinya J. Abrams, et al. "A model of APL with FLT3 mutation is responsive to retinoic acid and a receptor tyrosine kinase inhibitor, SU11657." Blood 101, no. 8 (April 15, 2003): 3188–97. http://dx.doi.org/10.1182/blood-2002-06-1800.

Full text
Abstract:
Abstract The PML-RARα fusion protein is central to the pathogenesis of acute promyelocytic leukemia (APL). Expression of this protein in transgenic mice initiates myeloid leukemias with features of human APL, but only after a long latency (8.5 months in MRP8 PML-RARAmice). Thus, additional changes contribute to leukemic transformation. Activating mutations of the FLT3 receptor tyrosine kinase are common in human acute myeloid leukemias and are frequent in human APL. To assess how activating mutations of FLT3 contribute to APL pathogenesis and impact therapy, we used retroviral transduction to introduce an activated allele of FLT3 into control and MRP8 PML-RARA transgenic bone marrow. Activated FLT3 cooperated with PML-RARα to induce leukemias in 62 to 299 days (median latency, 105 days). In contrast to the leukemias that arose spontaneously inMRP8 PML-RARA mice, the activated FLT3/PML-RARα leukemias were characterized by leukocytosis, similar to human APL with FLT3 mutations. Cytogenetic analysis revealed clonal karyotypic abnormalities, which may contribute to pathogenesis or progression. SU11657, a selective, oral, multitargeted tyrosine kinase inhibitor that targets FLT3, cooperated with all-trans retinoic acid to rapidly cause regression of leukemia. Our results suggest that the acquisition of FLT3 mutations by cells with a pre-existing t(15;17) is a frequent pathway to the development of APL. Our findings also indicate that APL patients with FLT3 mutations may benefit from combination therapy with all-trans retinoic acid plus an FLT3 inhibitor.
APA, Harvard, Vancouver, ISO, and other styles
7

Han, Xiaoyan, Chunxiang Jin, Gaofeng Zheng, Yi Li, Yungui Wang, Enfan Zhang, Honghu Zhu, and Zhen Cai. "Acute myeloid leukemia with CPSF6–RARG fusion resembling acute promyelocytic leukemia with extramedullary infiltration." Therapeutic Advances in Hematology 12 (January 2021): 204062072097698. http://dx.doi.org/10.1177/2040620720976984.

Full text
Abstract:
Some subtypes of acute myeloid leukemia (AML) share morphologic, immunophenotypic, and clinical features of acute promyelocytic leukemia (APL), but lack a PML–RARA (promyelocytic leukemia–retinoic acid receptor alpha) fusion gene. Instead, they have the retinoic acid receptor beta (RARB) or retinoic acid receptor gamma (RARG) rearranged. Almost all of these AML subtypes exhibit resistance to all-trans retinoic acid (ATRA); undoubtedly, the prognosis is poor. Here, we present an AML patient resembling APL with a novel cleavage and polyadenylation specific factor 6 ( CPSF6) –RARG fusion, showing resistance to ATRA and poor response to chemotherapy with homoharringtonine and cytarabine. Simultaneously, the patient also had extramedullary infiltration.
APA, Harvard, Vancouver, ISO, and other styles
8

Lallemand-Breitenbach, Valérie, Jun Zhu, Francine Puvion, Marcel Koken, Nicole Honoré, Alexandre Doubeikovsky, Estelle Duprez, et al. "Role of Promyelocytic Leukemia (Pml) Sumolation in Nuclear Body Formation, 11s Proteasome Recruitment, and as2O3-Induced Pml or Pml/Retinoic Acid Receptor α Degradation." Journal of Experimental Medicine 193, no. 12 (June 11, 2001): 1361–72. http://dx.doi.org/10.1084/jem.193.12.1361.

Full text
Abstract:
Promyelocytic leukemia (PML) is the organizer of nuclear matrix domains, PML nuclear bodies (NBs), with a proposed role in apoptosis control. In acute promyelocytic leukemia, PML/retinoic acid receptor (RAR) α expression disrupts NBs, but therapies such as retinoic acid or arsenic trioxide (As2O3) restore them. PML is conjugated by the ubiquitin-related peptide SUMO-1, a process enhanced by As2O3 and proposed to target PML to the nuclear matrix. We demonstrate that As2O3 triggers the proteasome-dependent degradation of PML and PML/RARα and that this process requires a specific sumolation site in PML, K160. PML sumolation is dispensable for its As2O3-induced matrix targeting and formation of primary nuclear aggregates, but is required for the formation of secondary shell-like NBs. Interestingly, only these mature NBs harbor 11S proteasome components, which are further recruited upon As2O3 exposure. Proteasome recruitment by sumolated PML only likely accounts for the failure of PML-K160R to be degraded. Therefore, studying the basis of As2O3-induced PML/RARα degradation we show that PML sumolation directly or indirectly promotes its catabolism, suggesting that mature NBs could be sites of intranuclear proteolysis and opening new insights into NB alterations found in viral infections or transformation.
APA, Harvard, Vancouver, ISO, and other styles
9

Chen, Sai-Juan, Guang-Biao Zhou, Xiao-Wei Zhang, Jian-Hua Mao, Hugues de Thé, and Zhu Chen. "From an old remedy to a magic bullet: molecular mechanisms underlying the therapeutic effects of arsenic in fighting leukemia." Blood 117, no. 24 (June 16, 2011): 6425–37. http://dx.doi.org/10.1182/blood-2010-11-283598.

Full text
Abstract:
Abstract Arsenic had been used in treating malignancies from the 18th to mid-20th century. In the past 3 decades, arsenic was revived and shown to be able to induce complete remission and to achieve, when combined with all-trans retinoic acid and chemotherapy, a 5-year overall survival of 90% in patients with acute promyelocytic leukemia driven by the t(15;17) translocation-generated promyelocytic leukemia–retinoic acid receptor α (PML-RARα) fusion. Molecularly, arsenic binds thiol residues and induces the formation of reactive oxygen species, thus affecting numerous signaling pathways. Interestingly, arsenic directly binds the C3HC4 zinc finger motif in the RBCC domain of PML and PML-RARα, induces their homodimerization and multimerization, and enhances their interaction with the SUMO E2 conjugase Ubc9, facilitating subsequent sumoylation/ubiquitination and proteasomal degradation. Arsenic-caused intermolecular disulfide formation in PML also contributes to PML-multimerization. All-trans retinoic acid, which targets PML-RARα for degradation through its RARα moiety, synergizes with arsenic in eliminating leukemia-initiating cells. Arsenic perturbs a number of proteins involved in other hematologic malignancies, including chronic myeloid leukemia and adult T-cell leukemia/lymphoma, whereby it may bring new therapeutic benefits. The successful revival of arsenic in acute promyelocytic leukemia, together with modern mechanistic studies, has thus allowed a new paradigm to emerge in translational medicine.
APA, Harvard, Vancouver, ISO, and other styles
10

McNamara, Suzan, Hongling Wang, Nessrine Hanna, and Wilson H. Miller. "Topoisomerase IIβ Negatively Modulates Retinoic Acid Receptor α Function: a Novel Mechanism of Retinoic Acid Resistance." Molecular and Cellular Biology 28, no. 6 (January 22, 2008): 2066–77. http://dx.doi.org/10.1128/mcb.01576-07.

Full text
Abstract:
ABSTRACT Interactions between retinoic acid (RA) receptor α (RARα) and coregulators play a key role in coordinating gene transcription and myeloid differentiation. In patients with acute promyelocytic leukemia (APL), the RARα gene is fused with the promyelocytic leukemia (PML) gene via the t(15;17) translocation, resulting in the expression of a PML/RARα fusion protein. Here, we report that topoisomerase II beta (TopoIIβ) associates with and negatively modulates RARα transcriptional activity and that increased levels of and association with TopoIIβ cause resistance to RA in APL cell lines. Knockdown of TopoIIβ was able to overcome resistance by permitting RA-induced differentiation and increased RA gene expression. Overexpression of TopoIIβ in clones from an RA-sensitive cell line conferred resistance by a reduction in RA-induced expression of target genes and differentiation. Chromatin immunoprecipitation assays indicated that TopoIIβ is bound to an RA response element and that inhibition of TopoIIβ causes hyperacetylation of histone 3 at lysine 9 and activation of transcription. Our results identify a novel mechanism of resistance in APL and provide further insight to the role of TopoIIβ in gene regulation and differentiation.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "PML-retinoic acid receptor-a"

1

Bellodi, Cristian. "Novel insights into the cytoplasmic function of promyelocytic leukaemia (PML) and PML-retinoic acid receptor-α." Thesis, University of Leicester, 2008. http://hdl.handle.net/2381/30784.

Full text
Abstract:
The promyelocytic leukaemia protein (PML) is a tumour suppressor initially identified in acute promyelocytic leukaemia (APL). In APL, PML and the retinoic acid receptor alpha (RARalpha) genes are fused as a consequence of the translocation t(15;17). The product of the chimeric gene is the oncogenic PML-RARalpha protein. The PML gene encodes multiple nuclear and cytoplasmic isoforms. PML nuclear isoforms (nPML) are the main components of the PML nuclear bodies (PML-NBs), sub-nuclear structures involved in the modulation of essential cellular players including the tumour suppressor p53. Nuclear PML has been intensively studied, while, the role of cytoplasmic PML remains poorly understood. Increasing evidence indicates that PML could bear cytoplasmic functions in both physiological and pathological settings. This study aims to gain more insights into the function of PML and PML-RARalpha cytoplasmic pool of proteins. Recently, two missense mutations resulting in truncated PML cytoplasmic protein (Mut PML) have been identified in aggressive APL cases. We found that Mut PML alters the structure and the function of the PML-NB mainly through the cytoplasmic relocation of nPML. Remarkably, Mut PML inhibits p53 transcriptional, growth suppressive and apoptotic functions. In the cytoplasm, Mut PML interacts and stabilizes PML-RARalpha, thus potentiating its block of RA-induced transcription and differentiation. A mutant of PML-RARalpha (Delta2) accumulating in the cytoplasm is able to inhibit RA-dependent transcription and differentiation, suggesting that cytoplasmic localization of PML-RARalpha may contribute to transformation. Finally, we found that Delta2 expression blocks G-CSF-dependent myeloid differentiation and causes partial transformation of primary haematopoietic progenitor cells.
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'PML-retinoic acid receptor-a' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography