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  1. Article ; Online: Redox and proteolytic regulation of cardiomyocyte β

    Steinberg, Susan F

    Frontiers in immunology

    2023  Volume 14, Page(s) 1306467

    Abstract: Conventional models view ... ...

    Abstract Conventional models view β
    MeSH term(s) Myocytes, Cardiac/metabolism ; Catecholamines/metabolism ; Signal Transduction ; Oxidation-Reduction ; Receptors, Adrenergic/metabolism
    Chemical Substances Catecholamines ; Receptors, Adrenergic
    Language English
    Publishing date 2023-12-04
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2023.1306467
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Beta

    Zhu, Jing / Steinberg, Susan F

    JACC. Basic to translational science

    2023  Volume 8, Issue 8, Page(s) 976–988

    Abstract: The decrease in ... ...

    Abstract The decrease in β
    Language English
    Publishing date 2023-05-17
    Publishing country United States
    Document type Journal Article
    ISSN 2452-302X
    ISSN (online) 2452-302X
    DOI 10.1016/j.jacbts.2023.02.002
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  3. Article ; Online: N-Tertaining a New Signaling Paradigm for the Cardiomyocyte β 1 -Adrenergic Receptor.

    Steinberg, Susan F

    Journal of cardiovascular pharmacology

    2022  Volume 80, Issue 3, Page(s) 328–333

    Abstract: Abstract: β 1 -adrenergic receptors (β 1 ARs) are the principle mediators of catecholamine actions in cardiomyocytes. β 1 ARs rapidly adjust cardiac output and provide short-term hemodynamic support for the failing heart by activating a Gs-adenylyl ... ...

    Abstract Abstract: β 1 -adrenergic receptors (β 1 ARs) are the principle mediators of catecholamine actions in cardiomyocytes. β 1 ARs rapidly adjust cardiac output and provide short-term hemodynamic support for the failing heart by activating a Gs-adenylyl cyclase pathway that increases 3'-5'-cyclic adenosine monophosphate and leads to the activation of protein kinase A and the phosphorylation of substrates involved in excitation-contraction coupling. However, chronic persistent β 1 AR activation in the setting of heart failure leads to a spectrum of maladaptive changes that contribute to the evolution of heart failure. The molecular basis for β 1 AR-driven maladaptive responses remains uncertain because chronic persistent β 1 AR activation has been linked to the activation of both proapoptotic and antiapoptotic signaling pathways. Of note, studies to date have been predicated on the assumption that β 1 ARs signal exclusively as full-length receptor proteins. Our recent studies show that β 1 ARs are detected as both full-length and N-terminally truncated species in cardiomyocytes, that N-terminal cleavage is regulated by O-glycan modifications at specific sites on the β 1 AR N-terminus, and that N-terminally truncated β 1 ARs remain signaling competent, but their signaling properties differ from those of the full-length β 1 AR. The N-terminally truncated form of the β 1 AR constitutively activates the protein kinase B signaling pathway and confers protection against doxorubicin-dependent apoptosis in cardiomyocytes. These studies identify a novel signaling paradigm for the β 1 AR, implicating the N-terminus as a heretofore-unrecognized structural determinant of β 1 AR responsiveness that could be pharmacologically targeted for therapeutic advantage.
    MeSH term(s) Adenylyl Cyclases/metabolism ; Cyclic AMP/metabolism ; Heart Failure/drug therapy ; Heart Failure/metabolism ; Humans ; Myocytes, Cardiac/metabolism ; Receptors, Adrenergic, beta/metabolism ; Receptors, Adrenergic, beta-1/metabolism ; Receptors, Adrenergic, beta-2/metabolism ; Signal Transduction/physiology
    Chemical Substances Receptors, Adrenergic, beta ; Receptors, Adrenergic, beta-1 ; Receptors, Adrenergic, beta-2 ; Cyclic AMP (E0399OZS9N) ; Adenylyl Cyclases (EC 4.6.1.1)
    Language English
    Publishing date 2022-09-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 391970-5
    ISSN 1533-4023 ; 0160-2446
    ISSN (online) 1533-4023
    ISSN 0160-2446
    DOI 10.1097/FJC.0000000000001194
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  4. Article ; Online: Decoding the Cardiac Actions of Protein Kinase D Isoforms.

    Steinberg, Susan F

    Molecular pharmacology

    2021  Volume 100, Issue 6, Page(s) 558–567

    Abstract: Protein kinase D (PKD) consists of a family of three structurally related enzymes that play key roles in a wide range of biological functions that contribute to the evolution of cardiac hypertrophy and heart failure. PKD1 (the founding member of this ... ...

    Abstract Protein kinase D (PKD) consists of a family of three structurally related enzymes that play key roles in a wide range of biological functions that contribute to the evolution of cardiac hypertrophy and heart failure. PKD1 (the founding member of this enzyme family) has been implicated in the phosphorylation of substrates that regulate cardiac hypertrophy, contraction, and susceptibility to ischemia/reperfusion injury, and de novo
    MeSH term(s) Animals ; Heart Defects, Congenital/genetics ; Heart Defects, Congenital/metabolism ; Humans ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Mutation ; Myocytes, Cardiac/metabolism ; Protein Kinase C/genetics ; Protein Kinase C/metabolism
    Chemical Substances Isoenzymes ; protein kinase D (EC 2.7.10.-) ; Protein Kinase C (EC 2.7.11.13)
    Language English
    Publishing date 2021-09-16
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 124034-1
    ISSN 1521-0111 ; 0026-895X
    ISSN (online) 1521-0111
    ISSN 0026-895X
    DOI 10.1124/molpharm.121.000341
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  5. Article ; Online: G Protein-Coupled Receptors-Receptors With New Tricks Up Their Sleeves.

    Steinberg, Susan F / Booz, George W

    Journal of cardiovascular pharmacology

    2022  Volume 80, Issue 3, Page(s) 325–327

    MeSH term(s) Arthroplasty, Replacement, Knee ; Receptors, G-Protein-Coupled
    Chemical Substances Receptors, G-Protein-Coupled
    Language English
    Publishing date 2022-09-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 391970-5
    ISSN 1533-4023 ; 0160-2446
    ISSN (online) 1533-4023
    ISSN 0160-2446
    DOI 10.1097/FJC.0000000000001318
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  6. Article ; Online: Trypsin cleavage of the β

    Zhu, Jing / Steinberg, Susan F

    American journal of physiology. Heart and circulatory physiology

    2022  Volume 322, Issue 3, Page(s) H486–H491

    Abstract: ... ...

    Abstract β
    MeSH term(s) Catecholamines/metabolism ; Myocytes, Cardiac/metabolism ; Proteolysis ; Receptors, Adrenergic, beta-1/genetics ; Receptors, Adrenergic, beta-1/metabolism ; Signal Transduction ; Trypsin/metabolism
    Chemical Substances Catecholamines ; Receptors, Adrenergic, beta-1 ; Trypsin (EC 3.4.21.4)
    Language English
    Publishing date 2022-02-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 603838-4
    ISSN 1522-1539 ; 0363-6135
    ISSN (online) 1522-1539
    ISSN 0363-6135
    DOI 10.1152/ajpheart.00005.2022
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  7. Article ; Online: Michael R. Rosen, MD (1938-2023).

    Cohen, Ira S / Robinson, Richard B / Steinberg, Susan F

    Heart rhythm

    2022  Volume 20, Issue 5, Page(s) 791–792

    Language English
    Publishing date 2022-12-29
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2229357-7
    ISSN 1556-3871 ; 1547-5271
    ISSN (online) 1556-3871
    ISSN 1547-5271
    DOI 10.1016/j.hrthm.2023.02.019
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  8. Article ; Online: β

    Zhu, Jing / Steinberg, Susan F

    Journal of molecular and cellular cardiology

    2021  Volume 154, Page(s) 70–79

    Abstract: ... ...

    Abstract β
    MeSH term(s) ADAM17 Protein/metabolism ; Gene Expression ; Glycosylation ; Humans ; Myocytes, Cardiac/metabolism ; Oxidation-Reduction ; Oxidative Stress ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Processing, Post-Translational ; Proteolysis ; Receptors, Adrenergic, beta-1/chemistry ; Receptors, Adrenergic, beta-1/genetics ; Receptors, Adrenergic, beta-1/metabolism
    Chemical Substances Receptors, Adrenergic, beta-1 ; ADAM17 Protein (EC 3.4.24.86) ; ADAM17 protein, human (EC 3.4.24.86)
    Language English
    Publishing date 2021-02-06
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 80157-4
    ISSN 1095-8584 ; 0022-2828
    ISSN (online) 1095-8584
    ISSN 0022-2828
    DOI 10.1016/j.yjmcc.2021.01.012
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  9. Article ; Online: Beta

    Steinberg, Susan F

    Circulation research

    2018  Volume 123, Issue 11, Page(s) 1199–1201

    MeSH term(s) Adrenergic beta-Antagonists/pharmacology ; Adrenergic beta-Antagonists/therapeutic use ; Animals ; Heart Diseases/drug therapy ; Humans ; Myocytes, Cardiac/drug effects ; Myocytes, Cardiac/metabolism ; Myocytes, Cardiac/physiology ; Receptors, Adrenergic, beta/chemistry ; Receptors, Adrenergic, beta/genetics ; Receptors, Adrenergic, beta/metabolism
    Chemical Substances Adrenergic beta-Antagonists ; Receptors, Adrenergic, beta
    Language English
    Publishing date 2018-12-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 80100-8
    ISSN 1524-4571 ; 0009-7330 ; 0931-6876
    ISSN (online) 1524-4571
    ISSN 0009-7330 ; 0931-6876
    DOI 10.1161/CIRCRESAHA.118.313884
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  10. Article ; Online: Post-translational modifications at the ATP-positioning G-loop that regulate protein kinase activity.

    Steinberg, Susan F

    Pharmacological research

    2018  Volume 135, Page(s) 181–187

    Abstract: Protein kinases are a superfamily of enzymes that control a wide range of cellular functions. These enzymes share a highly conserved catalytic core that folds into a similar bilobar three-dimensional structure. One highly conserved region in the protein ... ...

    Abstract Protein kinases are a superfamily of enzymes that control a wide range of cellular functions. These enzymes share a highly conserved catalytic core that folds into a similar bilobar three-dimensional structure. One highly conserved region in the protein kinase core is the glycine-rich loop (or G-loop), a highly flexible loop that is characterized by a consensus GxGxxG sequence. The G-loop points toward the catalytic cleft and functions to bind and position ATP for phosphotransfer. Of note, in many protein kinases, the second and third glycine residues in the G-loop triad flank residues that can be targets for phosphorylation (Ser, Thr, or Tyr) or other post-translational modifications (ubiquitination, acetylation, O-GlcNAcylation, oxidation). There is considerable evidence that cyclin-dependent kinases are held inactive through inhibitory phosphorylation of the conserved Thr/Tyr residues in this position of the G-loop and that dephosphorylation by cellular phosphatases is required for CDK activation and progression through the cell cycle. This review summarizes literature that identifies residues in or adjacent to the G-loop in other protein kinases that are targets for functionally important post-translational modifications.
    MeSH term(s) Adenosine Triphosphate/metabolism ; Animals ; Humans ; Protein Conformation ; Protein Kinases/chemistry ; Protein Kinases/metabolism ; Protein Processing, Post-Translational
    Chemical Substances Adenosine Triphosphate (8L70Q75FXE) ; Protein Kinases (EC 2.7.-)
    Language English
    Publishing date 2018-07-23
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1003347-6
    ISSN 1096-1186 ; 0031-6989 ; 1043-6618
    ISSN (online) 1096-1186
    ISSN 0031-6989 ; 1043-6618
    DOI 10.1016/j.phrs.2018.07.009
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