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  1. AU="Spadotto, Valeria"
  2. AU="Jimenez-Macias, Jorge L"

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  1. Article ; Online: LKB1 signaling is altered in skeletal muscle of a Duchenne muscular dystrophy mouse model.

    Boccanegra, Brigida / Mantuano, Paola / Conte, Elena / Cerchiara, Alessandro Giovanni / Tulimiero, Lisamaura / Quarta, Raffaella / Caputo, Erika / Sanarica, Francesca / Forino, Monica / Spadotto, Valeria / Cappellari, Ornella / Fossati, Gianluca / Steinkühler, Christian / De Luca, Annamaria

    Disease models & mechanisms

    2023  Volume 16, Issue 7

    Abstract: The potential role of liver kinase B1 (LKB1) in the altered activation of the master metabolic and epigenetic regulator adenosine monophosphate-activated protein kinase (AMPK) in Duchenne muscular dystrophy has not been investigated so far. Hence, we ... ...

    Abstract The potential role of liver kinase B1 (LKB1) in the altered activation of the master metabolic and epigenetic regulator adenosine monophosphate-activated protein kinase (AMPK) in Duchenne muscular dystrophy has not been investigated so far. Hence, we analyzed both gene and protein levels of LKB1 and its related targets in gastrocnemius muscles of adult C57BL/10 mdx mice and D2 mdx mice, a model with a more severe dystrophic phenotype, as well as the sensitivity of the LKB1-AMPK pathway to AMPK activators, such as chronic exercise. Our data show, for the first time, a reduction in the levels of LKB1 and accessory proteins, MO25 and STRADα, in both mdx strains versus the respective wild type, which was further impaired by exercise, in parallel with a lack of further phosphorylation of AMPK. The AMPK-like kinase salt-inducible kinase (SIK) and class II histone deacetylases, along with expression of the HDAC target gene Mef2c, were also altered, supporting an impairment of LKB1-SIK-class II histone deacetylase signaling. Our results demonstrate that LKB1 may be involved in dystrophic progression, paving the way for future preclinical studies.
    MeSH term(s) Animals ; Mice ; AMP-Activated Protein Kinases/metabolism ; Disease Models, Animal ; Mice, Inbred C57BL ; Mice, Inbred mdx ; Muscle, Skeletal/metabolism ; Muscular Dystrophy, Duchenne/genetics ; Muscular Dystrophy, Duchenne/metabolism ; Protein Serine-Threonine Kinases/metabolism
    Chemical Substances AMP-Activated Protein Kinases (EC 2.7.11.31) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Stk11 protein, mouse (EC 2.7.11.1)
    Language English
    Publishing date 2023-07-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2451104-3
    ISSN 1754-8411 ; 1754-8403
    ISSN (online) 1754-8411
    ISSN 1754-8403
    DOI 10.1242/dmm.049930
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: HDAC Inhibition as Potential Therapeutic Strategy to Restore the Deregulated Immune Response in Severe COVID-19.

    Ripamonti, Chiara / Spadotto, Valeria / Pozzi, Pietro / Stevenazzi, Andrea / Vergani, Barbara / Marchini, Mattia / Sandrone, Giovanni / Bonetti, Emanuele / Mazzarella, Luca / Minucci, Saverio / Steinkühler, Christian / Fossati, Gianluca

    Frontiers in immunology

    2022  Volume 13, Page(s) 841716

    Abstract: The COVID-19 pandemic has had a devastating impact worldwide and has been a great challenge for the scientific community. Vaccines against SARS-CoV-2 are now efficiently lessening COVID-19 mortality, although finding a cure for this infection is still a ... ...

    Abstract The COVID-19 pandemic has had a devastating impact worldwide and has been a great challenge for the scientific community. Vaccines against SARS-CoV-2 are now efficiently lessening COVID-19 mortality, although finding a cure for this infection is still a priority. An unbalanced immune response and the uncontrolled release of proinflammatory cytokines are features of COVID-19 pathophysiology and contribute to disease progression and worsening. Histone deacetylases (HDACs) have gained interest in immunology, as they regulate the innate and adaptative immune response at different levels. Inhibitors of these enzymes have already proven therapeutic potential in cancer and are currently being investigated for the treatment of autoimmune diseases. We thus tested the effects of different HDAC inhibitors, with a focus on a selective HDAC6 inhibitor, on immune and epithelial cells in
    MeSH term(s) COVID-19/drug therapy ; COVID-19 Vaccines ; Cytokines/metabolism ; Histone Deacetylase Inhibitors/pharmacology ; Histone Deacetylase Inhibitors/therapeutic use ; Histone Deacetylases/metabolism ; Humans ; Immunity ; Pandemics ; SARS-CoV-2
    Chemical Substances COVID-19 Vaccines ; Cytokines ; Histone Deacetylase Inhibitors ; Histone Deacetylases (EC 3.5.1.98)
    Language English
    Publishing date 2022-05-03
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2022.841716
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: PRMT1-mediated methylation of the microprocessor-associated proteins regulates microRNA biogenesis.

    Spadotto, Valeria / Giambruno, Roberto / Massignani, Enrico / Mihailovich, Marija / Maniaci, Marianna / Patuzzo, Francesca / Ghini, Francesco / Nicassio, Francesco / Bonaldi, Tiziana

    Nucleic acids research

    2019  Volume 48, Issue 1, Page(s) 96–115

    Abstract: MicroRNA (miRNA) biogenesis is a tightly controlled multi-step process operated in the nucleus by the activity of the Microprocessor and its associated proteins. Through high resolution mass spectrometry (MS)- proteomics we discovered that this complex ... ...

    Abstract MicroRNA (miRNA) biogenesis is a tightly controlled multi-step process operated in the nucleus by the activity of the Microprocessor and its associated proteins. Through high resolution mass spectrometry (MS)- proteomics we discovered that this complex is extensively methylated, with 84 methylated sites associated to 19 out of its 24 subunits. The majority of the modifications occurs on arginine (R) residues (61), leading to 81 methylation events, while 30 lysine (K)-methylation events occurs on 23 sites of the complex. Interestingly, both depletion and pharmacological inhibition of the Type-I Protein Arginine Methyltransferases (PRMTs) lead to a widespread change in the methylation state of the complex and induce global decrease of miRNA expression, as a consequence of the impairment of the pri-to-pre-miRNA processing step. In particular, we show that the reduced methylation of the Microprocessor subunit ILF3 is linked to its diminished binding to the pri-miRNAs miR-15a/16, miR-17-92, miR-301a and miR-331. Our study uncovers a previously uncharacterized role of R-methylation in the regulation of miRNA biogenesis in mammalian cells.
    MeSH term(s) Animals ; Arginine/metabolism ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Epigenesis, Genetic ; HEK293 Cells ; HeLa Cells ; Humans ; Isotope Labeling ; Lysine/metabolism ; Methylation ; MicroRNAs/biosynthesis ; MicroRNAs/classification ; MicroRNAs/genetics ; Nuclear Factor 90 Proteins/genetics ; Nuclear Factor 90 Proteins/metabolism ; Protein Binding ; Protein-Arginine N-Methyltransferases/antagonists & inhibitors ; Protein-Arginine N-Methyltransferases/genetics ; Protein-Arginine N-Methyltransferases/metabolism ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; Repressor Proteins/antagonists & inhibitors ; Repressor Proteins/genetics ; Repressor Proteins/metabolism
    Chemical Substances ILF3 protein, human ; MicroRNAs ; Nuclear Factor 90 Proteins ; RNA, Small Interfering ; Repressor Proteins ; Arginine (94ZLA3W45F) ; PRMT1 protein, human (EC 2.1.1.319) ; Protein-Arginine N-Methyltransferases (EC 2.1.1.319) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2019-11-28
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkz1051
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.

    Bremang, Michael / Cuomo, Alessandro / Agresta, Anna Maria / Stugiewicz, Magdalena / Spadotto, Valeria / Bonaldi, Tiziana

    Molecular bioSystems

    2013  Volume 9, Issue 9, Page(s) 2231–2247

    Abstract: Protein methylation is a post-translational modification (PTM) by which a variable number of methyl groups are transferred to lysine and arginine residues within proteins. Despite increased interest in this modification due to its reversible nature and ... ...

    Abstract Protein methylation is a post-translational modification (PTM) by which a variable number of methyl groups are transferred to lysine and arginine residues within proteins. Despite increased interest in this modification due to its reversible nature and its emerging role in a diverse set of biological pathways beyond chromatin, global identification of protein methylation has remained an unachieved goal. To characterise sites of lysine and arginine methylation beyond histones, we employed an approach that combines heavy methyl stable isotope labelling by amino acids in cell culture (hmSILAC) with high-resolution mass spectrometry-based proteomics. Through a broad evaluation of immuno-affinity enrichment and the application of two classical protein separation techniques prior to mass spectrometry, to nucleosolic and cytosolic fractions separately, we identified a total of 501 different methylation types, on 397 distinct lysine and arginine sites, present on 139 unique proteins. Our results considerably extend the number of known in vivo methylation sites and indicate their significant presence on several protein complexes involved at all stages of gene expression, from chromatin remodelling and transcription to splicing and translation. In addition, we describe the potential of the hmSILAC approach for accurate relative quantification of methylation levels between distinct functional states.
    MeSH term(s) Arginine/chemistry ; Arginine/metabolism ; Humans ; Lysine/chemistry ; Lysine/metabolism ; Mass Spectrometry ; Methylation ; Proteome/chemistry ; Proteome/metabolism ; Proteomics
    Chemical Substances Proteome ; Arginine (94ZLA3W45F) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2013-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2188635-0
    ISSN 1742-2051 ; 1742-206X
    ISSN (online) 1742-2051
    ISSN 1742-206X
    DOI 10.1039/c3mb00009e
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: miR-17-92 fine-tunes MYC expression and function to ensure optimal B cell lymphoma growth.

    Mihailovich, Marija / Bremang, Michael / Spadotto, Valeria / Musiani, Daniele / Vitale, Elena / Varano, Gabriele / Zambelli, Federico / Mancuso, Francesco M / Cairns, David A / Pavesi, Giulio / Casola, Stefano / Bonaldi, Tiziana

    Nature communications

    2015  Volume 6, Page(s) 8725

    Abstract: The synergism between c-MYC and miR-17-19b, a truncated version of the miR-17-92 cluster, is well-documented during tumor initiation. However, little is known about miR-17-19b function in established cancers. Here we investigate the role of miR-17-19b in ...

    Abstract The synergism between c-MYC and miR-17-19b, a truncated version of the miR-17-92 cluster, is well-documented during tumor initiation. However, little is known about miR-17-19b function in established cancers. Here we investigate the role of miR-17-19b in c-MYC-driven lymphomas by integrating SILAC-based quantitative proteomics, transcriptomics and 3' untranslated region (UTR) analysis upon miR-17-19b overexpression. We identify over one hundred miR-17-19b targets, of which 40% are co-regulated by c-MYC. Downregulation of a new miR-17/20 target, checkpoint kinase 2 (Chek2), increases the recruitment of HuR to c-MYC transcripts, resulting in the inhibition of c-MYC translation and thus interfering with in vivo tumor growth. Hence, in established lymphomas, miR-17-19b fine-tunes c-MYC activity through a tight control of its function and expression, ultimately ensuring cancer cell homeostasis. Our data highlight the plasticity of miRNA function, reflecting changes in the mRNA landscape and 3' UTR shortening at different stages of tumorigenesis.
    MeSH term(s) Animals ; Cell Line, Tumor ; Checkpoint Kinase 2/genetics ; Checkpoint Kinase 2/metabolism ; Cloning, Molecular ; ELAV-Like Protein 1/genetics ; ELAV-Like Protein 1/metabolism ; Gene Expression Regulation, Neoplastic/physiology ; Lymphoma, B-Cell/metabolism ; Mice ; Mice, Transgenic ; MicroRNAs/genetics ; MicroRNAs/metabolism ; Proteome ; Proto-Oncogene Proteins c-myc/genetics ; Proto-Oncogene Proteins c-myc/metabolism
    Chemical Substances ELAV-Like Protein 1 ; Elavl1 protein, mouse ; MIRN17-92 microRNA, mouse ; MicroRNAs ; Mirn17 microRNA, mouse ; Mirn20 microRNA, mouse ; Myc protein, mouse ; Proteome ; Proto-Oncogene Proteins c-myc ; Checkpoint Kinase 2 (EC 2.7.1.11) ; Chek2 protein, mouse (EC 2.7.11.1)
    Language English
    Publishing date 2015-11-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/ncomms9725
    Database MEDical Literature Analysis and Retrieval System OnLINE

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