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  1. Article: YY1 Knockdown Relieves the Differentiation Block and Restores Apoptosis in AML Cells.

    Noguera, Nelida Ines / Travaglini, Serena / Scalea, Stefania / Catalanotto, Caterina / Reale, Anna / Zampieri, Michele / Zaza, Alessandra / Ricciardi, Maria Rosaria / Angelini, Daniela Francesca / Tafuri, Agostino / Ottone, Tiziana / Voso, Maria Teresa / Zardo, Giuseppe

    Cancers

    2023  Volume 15, Issue 15

    Abstract: In this study we analyzed the expression of Yin and Yang 1 protein (YY1), a member of the noncanonical PcG complexes, in AML patient samples and AML cell lines and the effect of YY1 downregulation on the AML differentiation block. Our results show that ... ...

    Abstract In this study we analyzed the expression of Yin and Yang 1 protein (YY1), a member of the noncanonical PcG complexes, in AML patient samples and AML cell lines and the effect of YY1 downregulation on the AML differentiation block. Our results show that YY1 is significantly overexpressed in AML patient samples and AML cell lines and that YY1 knockdown relieves the differentiation block. YY1 downregulation in two AML cell lines (HL-60 and OCI-AML3) and one AML patient sample restored the expression of members of the CEBP protein family, increased the expression of extrinsic growth factors/receptors and surface antigenic markers, induced morphological cell characteristics typical of myeloid differentiation, and sensitized cells to retinoic acid treatment and to apoptosis. Overall, our data show that YY1 is not a secondary regulator of myeloid differentiation but that, if overexpressed, it can play a predominant role in myeloid differentiation block.
    Language English
    Publishing date 2023-08-07
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2527080-1
    ISSN 2072-6694
    ISSN 2072-6694
    DOI 10.3390/cancers15154010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Effects of Triheptanoin on Mitochondrial Respiration and Glycolysis in Cultured Fibroblasts from Neutral Lipid Storage Disease Type M (NLSD-M) Patients.

    Noguera, Nelida Inés / Tavian, Daniela / Angelini, Corrado / Cortese, Francesca / Filosto, Massimiliano / Garibaldi, Matteo / Missaglia, Sara / Smigliani, Ariela / Zaza, Alessandra / Pennisi, Elena Maria

    Biomolecules

    2023  Volume 13, Issue 3

    Abstract: Neutral lipid storage disease type M (NLSD-M) is an ultra-rare, autosomal recessive disorder that causes severe skeletal and cardiac muscle damage and lipid accumulation in all body tissues. In this hereditary pathology, the defective action of the ... ...

    Abstract Neutral lipid storage disease type M (NLSD-M) is an ultra-rare, autosomal recessive disorder that causes severe skeletal and cardiac muscle damage and lipid accumulation in all body tissues. In this hereditary pathology, the defective action of the adipose triglyceride lipase (ATGL) enzyme induces the enlargement of cytoplasmic lipid droplets and reduction in the detachment of mono- (MG) and diglycerides (DG). Although the pathogenesis of muscle fiber necrosis is unknown, some studies have shown alterations in cellular energy production, probably because MG and DG, the substrates of Krebs cycle, are less available. No tests have been tried with medium-chain fatty acid molecules to evaluate the anaplerotic effect in NLSD cells. In this study, we evaluated the in vitro effect of triheptanoin (Dojolvi
    MeSH term(s) Humans ; Lipase/metabolism ; Triglycerides ; Glycolysis ; Fibroblasts/metabolism
    Chemical Substances triheptanoin (2P6O7CFW5K) ; Lipase (EC 3.1.1.3) ; Triglycerides
    Language English
    Publishing date 2023-03-01
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom13030452
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: MCL1 regulates AML cells metabolism via direct interaction with HK2. Metabolic signature at onset predicts overall survival in AMLs' patients.

    Catalano, Gianfranco / Zaza, Alessandra / Banella, Cristina / Pelosi, Elvira / Castelli, Germana / de Marinis, Elisabetta / Smigliani, Ariela / Travaglini, Serena / Ottone, Tiziana / Divona, Mariadomenica / Del Principe, Maria Ilaria / Buccisano, Francesco / Maurillo, Luca / Ammatuna, Emanuele / Testa, Ugo / Nervi, Clara / Venditti, Adriano / Voso, Maria Teresa / Noguera, Nelida Ines

    Leukemia

    2023  Volume 37, Issue 8, Page(s) 1600–1610

    Abstract: We characterize the metabolic background in distinct Acute Myeloid Leukemias (AMLs), by comparing the metabolism of primary AML blasts isolated at diagnosis with that of normal hematopoietic maturing progenitors, using the Seahorse XF Agilent. Leukemic ... ...

    Abstract We characterize the metabolic background in distinct Acute Myeloid Leukemias (AMLs), by comparing the metabolism of primary AML blasts isolated at diagnosis with that of normal hematopoietic maturing progenitors, using the Seahorse XF Agilent. Leukemic cells feature lower spare respiratory (SRC) and glycolytic capacities as compared to hematopoietic precursors (i.e. day 7, promyelocytes). According with Proton Leak (PL) values, AML blasts can be grouped in two well defined populations. The AML group with blasts presenting high PL or high basal OXPHOS plus high SRC levels had shorter overall survival time and significantly overexpressed myeloid cell leukemia 1 (MCL1) protein. We demonstrate that MCL1 directly binds to Hexokinase 2 (HK2) on the outer mitochondrial membrane (OMM). Overall, these results suggest that high PL and high SRC plus high basal OXPHOS levels at disease onset, arguably with the concourse of MCL1/HK2 action, are significantly linked with shorter overall survival time in AML. Our data describe a new function for MCL1 protein in AMLs' cells: by forming a complex with HK2, MCL1 co-localizes to VDAC on the OMM, thus inducing glycolysis and OXPHOS, ultimately conferring metabolic plasticity and promoting resistance to therapy.
    MeSH term(s) Humans ; Hexokinase ; Leukemia, Myeloid, Acute ; Myeloid Cell Leukemia Sequence 1 Protein/metabolism
    Chemical Substances Hexokinase (EC 2.7.1.1) ; MCL1 protein, human ; Myeloid Cell Leukemia Sequence 1 Protein ; HK2 protein, human (EC 2.7.1.1)
    Language English
    Publishing date 2023-06-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 807030-1
    ISSN 1476-5551 ; 0887-6924
    ISSN (online) 1476-5551
    ISSN 0887-6924
    DOI 10.1038/s41375-023-01946-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Ascorbate Plus Buformin in AML: A Metabolic Targeted Treatment.

    Banella, Cristina / Catalano, Gianfranco / Travaglini, Serena / Pelosi, Elvira / Ottone, Tiziana / Zaza, Alessandra / Guerrera, Gisella / Angelini, Daniela Francesca / Niscola, Pasquale / Divona, Mariadomenica / Battistini, Luca / Screnci, Maria / Ammatuna, Emanuele / Testa, Ugo / Nervi, Clara / Voso, Maria Teresa / Noguera, Nelida Ines

    Cancers

    2022  Volume 14, Issue 10

    Abstract: In the present study, we characterized the metabolic background of different Acute Myeloid Leukemias' (AMLs) cells and described a heterogeneous and highly flexible energetic metabolism. Using the Seahorse XF Agilent, we compared the metabolism of normal ...

    Abstract In the present study, we characterized the metabolic background of different Acute Myeloid Leukemias' (AMLs) cells and described a heterogeneous and highly flexible energetic metabolism. Using the Seahorse XF Agilent, we compared the metabolism of normal hematopoietic progenitors with that of primary AML blasts and five different AML cell lines. We assessed the efficacy and mechanism of action of the association of high doses of ascorbate, a powerful oxidant, with the metabolic inhibitor buformin, which inhibits mitochondrial complex I and completely shuts down mitochondrial contributions in ATP production. Primary blasts from seventeen AML patients, assayed for annexin V and live/dead exclusion by flow cytometry, showed an increase in the apoptotic effect using the drug combination, as compared with ascorbate alone. We show that ascorbate inhibits glycolysis through interfering with HK1/2 and GLUT1 functions in hematopoietic cells. Ascorbate combined with buformin decreases mitochondrial respiration and ATP production and downregulates glycolysis, enhancing the apoptotic effect of ascorbate in primary blasts from AMLs and sparing normal CD34+ bone marrow progenitors. In conclusion, our data have therapeutic implications especially in fragile patients since both agents have an excellent safety profile, and the data also support the clinical evaluation of ascorbate-buformin in association with different mechanism drugs for the treatment of refractory/relapsing AML patients with no other therapeutic options.
    Language English
    Publishing date 2022-05-23
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2527080-1
    ISSN 2072-6694
    ISSN 2072-6694
    DOI 10.3390/cancers14102565
    Database MEDical Literature Analysis and Retrieval System OnLINE

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