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  1. Article ; Online: Correction to "Histone H4K20 Trimethylation Is Decreased in Murine Models of Heart Disease".

    Hickenlooper, Samuel M / Davis, Kathryn / Szulik, Marta W / Sheikh, Hanin / Miller, Mickey / Valdez, Steven / Bia, Ryan / Franklin, Sarah

    ACS omega

    2023  Volume 8, Issue 6, Page(s) 6124–6125

    Abstract: This corrects the article DOI: 10.1021/acsomega.2c00984.]. ...

    Abstract [This corrects the article DOI: 10.1021/acsomega.2c00984.].
    Language English
    Publishing date 2023-01-31
    Publishing country United States
    Document type Published Erratum
    ISSN 2470-1343
    ISSN (online) 2470-1343
    DOI 10.1021/acsomega.3c00112
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Histone H4K20 Trimethylation Is Decreased in Murine Models of Heart Disease.

    Hickenlooper, Samuel M / Davis, Kathryn / Szulik, Marta W / Sheikh, Hanin / Miller, Mickey / Valdez, Steven / Bia, Ryan / Franklin, Sarah

    ACS omega

    2022  Volume 7, Issue 35, Page(s) 30710–30719

    Abstract: Heart disease is the leading cause of death in the developed world, and its comorbidities such as hypertension, diabetes, and heart failure are accompanied by major transcriptomic changes in the heart. During cardiac dysfunction, which leads to heart ... ...

    Abstract Heart disease is the leading cause of death in the developed world, and its comorbidities such as hypertension, diabetes, and heart failure are accompanied by major transcriptomic changes in the heart. During cardiac dysfunction, which leads to heart failure, there are global epigenetic alterations to chromatin that occur concomitantly with morphological changes in the heart in response to acute and chronic stress. These epigenetic alterations include the reversible methylation of lysine residues on histone proteins. Lysine methylations on histones H3K4 and H3K9 were among the first methylated lysine residues identified and have been linked to gene activation and silencing, respectively. However, much less is known regarding other methylated histone residues, including histone H4K20. Trimethylation of histone H4K20 has been shown to repress gene expression; however, this modification has never been examined in the heart. Here, we utilized immunoblotting and mass spectrometry to quantify histone H4K20 trimethylation in three models of cardiac dysfunction. Our results show that lysine methylation at this site is differentially regulated in the cardiomyocyte, leading to increased H4K20 trimethylation during acute hypertrophic stress in cell models and decreased H4K20 trimethylation during sustained ischemic injury and cardiac dysfunction in animal models. In addition, we examined publicly available data sets to analyze enzymes that regulate H4K20 methylation and identified two demethylases (KDM7B and KDM7C) and two methyltransferases (KMT5A and SMYD5) that were all differentially expressed in heart failure patients. This is the first study to examine histone H4K20 trimethylation in the heart and to determine how this post-translational modification is differentially regulated in multiple models of cardiac disease.
    Language English
    Publishing date 2022-08-23
    Publishing country United States
    Document type Journal Article
    ISSN 2470-1343
    ISSN (online) 2470-1343
    DOI 10.1021/acsomega.2c00984
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: SMYD1a protects the heart from ischemic injury by regulating OPA1-mediated cristae remodeling and supercomplex formation.

    Szulik, Marta W / Valdez, Steven / Walsh, Maureen / Davis, Kathryn / Bia, Ryan / Horiuchi, Emilee / O'Very, Sean / Laxman, Anil K / Sandaklie-Nicolova, Linda / Eberhardt, David R / Durrant, Jessica R / Sheikh, Hanin / Hickenlooper, Samuel / Creed, Magnus / Brady, Cameron / Miller, Mickey / Wang, Li / Garcia-Llana, June / Tracy, Christopher /
    Drakos, Stavros G / Funai, Katsuhiko / Chaudhuri, Dipayan / Boudina, Sihem / Franklin, Sarah

    Basic research in cardiology

    2023  Volume 118, Issue 1, Page(s) 20

    Abstract: SMYD1, a striated muscle-specific lysine methyltransferase, was originally shown to play a key role in embryonic cardiac development but more recently we demonstrated that loss of Smyd1 in the murine adult heart leads to cardiac hypertrophy and failure. ... ...

    Abstract SMYD1, a striated muscle-specific lysine methyltransferase, was originally shown to play a key role in embryonic cardiac development but more recently we demonstrated that loss of Smyd1 in the murine adult heart leads to cardiac hypertrophy and failure. However, the effects of SMYD1 overexpression in the heart and its molecular function in the cardiomyocyte in response to ischemic stress are unknown. In this study, we show that inducible, cardiomyocyte-specific overexpression of SMYD1a in mice protects the heart from ischemic injury as seen by a > 50% reduction in infarct size and decreased myocyte cell death. We also demonstrate that attenuated pathological remodeling is a result of enhanced mitochondrial respiration efficiency, which is driven by increased mitochondrial cristae formation and stabilization of respiratory chain supercomplexes within the cristae. These morphological changes occur concomitant with increased OPA1 expression, a known driver of cristae morphology and supercomplex formation. Together, these analyses identify OPA1 as a novel downstream target of SMYD1a whereby cardiomyocytes upregulate energy efficiency to dynamically adapt to the energy demands of the cell. In addition, these findings highlight a new epigenetic mechanism by which SMYD1a regulates mitochondrial energetics and functions to protect the heart from ischemic injury.
    MeSH term(s) Animals ; Mice ; Cardiomegaly/metabolism ; Mitochondria/metabolism ; Muscle, Skeletal/metabolism ; Myocytes, Cardiac/metabolism
    Chemical Substances Smyd1 protein, mouse ; Opa1 protein, mouse (EC 3.6.1.-)
    Language English
    Publishing date 2023-05-22
    Publishing country Germany
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 189755-x
    ISSN 1435-1803 ; 0300-8428 ; 0175-9418
    ISSN (online) 1435-1803
    ISSN 0300-8428 ; 0175-9418
    DOI 10.1007/s00395-023-00991-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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