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  1. Article ; Online: Proteasome inhibitors in myocardial ischemia, some concerns.

    Powell, Saul R

    The Annals of thoracic surgery

    2008  Volume 85, Issue 4, Page(s) 1503–4; author reply 1504

    MeSH term(s) Acetylcysteine/analogs & derivatives ; Acetylcysteine/pharmacology ; Animals ; Disease Models, Animal ; Humans ; Ischemic Preconditioning, Myocardial/methods ; Mice ; Myocardial Ischemia/drug therapy ; Myocardial Ischemia/physiopathology ; NF-kappa B/metabolism ; Oxidation-Reduction/drug effects ; Proteasome Endopeptidase Complex/metabolism ; Proteasome Inhibitors ; Reperfusion Injury/prevention & control ; Risk Factors ; Sensitivity and Specificity
    Chemical Substances NF-kappa B ; PS519 ; Proteasome Inhibitors ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Acetylcysteine (WYQ7N0BPYC)
    Language English
    Publishing date 2008-04
    Publishing country Netherlands
    Document type Comment ; Letter
    ZDB-ID 211007-6
    ISSN 1552-6259 ; 0003-4975
    ISSN (online) 1552-6259
    ISSN 0003-4975
    DOI 10.1016/j.athoracsur.2007.10.049
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  2. Article ; Online: The cardiac 26S proteasome: regulating the regulator.

    Powell, Saul R

    Circulation research

    2006  Volume 99, Issue 4, Page(s) 342–345

    MeSH term(s) Animals ; Electrophoresis, Gel, Two-Dimensional ; Homeostasis ; Mice ; Myocardium/enzymology ; Proteasome Endopeptidase Complex/chemistry ; Proteasome Endopeptidase Complex/isolation & purification ; Proteasome Endopeptidase Complex/metabolism
    Chemical Substances Proteasome Endopeptidase Complex (EC 3.4.25.1) ; ATP dependent 26S protease (EC 3.4.99.-)
    Language English
    Publishing date 2006-08-18
    Publishing country United States
    Document type Comment ; Editorial ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80100-8
    ISSN 1524-4571 ; 0009-7330 ; 0931-6876
    ISSN (online) 1524-4571
    ISSN 0009-7330 ; 0931-6876
    DOI 10.1161/01.RES.0000239412.40685.61
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  3. Article: The ubiquitin-proteasome system in cardiac physiology and pathology.

    Powell, Saul R

    American journal of physiology. Heart and circulatory physiology

    2006  Volume 291, Issue 1, Page(s) H1–H19

    Abstract: The ubiquitin-proteasome system (UPS) is the major nonlysosomal pathway for intracellular protein degradation, generally requiring a covalent linkage of one or more chains of polyubiquitins to the protein intended for degradation. It has become clear ... ...

    Abstract The ubiquitin-proteasome system (UPS) is the major nonlysosomal pathway for intracellular protein degradation, generally requiring a covalent linkage of one or more chains of polyubiquitins to the protein intended for degradation. It has become clear that the UPS plays major roles in regulating many cellular processes, including the cell cycle, immune responses, apoptosis, cell signaling, and protein turnover under normal and pathological conditions, as well as in protein quality control by removal of damaged, oxidized, and/or misfolded proteins. This review will present an overview of the structure, biochemistry, and physiology of the UPS with emphasis on its role in the heart, if known. In addition, evidence will be presented supporting the role of certain muscle-specific ubiquitin protein ligases, key regulatory components of the UPS, in regulation of sarcomere protein turnover and cardiomyocyte size and how this might play a role in induction of the hypertrophic phenotype. Moreover, this review will present the evidence suggesting that proteasomal dysfunction may play a role in cardiac pathologies such as myocardial ischemia, congestive heart failure, and myofilament-related and idiopathic-dilated cardiomyopathies, as well as cardiomyocyte loss in the aging heart. Finally, certain pitfalls of proteasome studies will be described with the intent of providing investigators with enough information to avoid these problems. This review should provide current investigators in the field with an up-to-date analysis of the literature and at the same time provide an impetus for new investigators to enter this important and rapidly changing area of research.
    MeSH term(s) Animals ; Apoptosis ; Heart/physiopathology ; Heart Diseases/metabolism ; Heart Diseases/pathology ; Humans ; Models, Cardiovascular ; Myocardium/pathology ; Myocytes, Cardiac/metabolism ; Myocytes, Cardiac/pathology ; Proteasome Endopeptidase Complex/metabolism ; Protein Biosynthesis ; Ubiquitin/metabolism
    Chemical Substances Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2006-02-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 603838-4
    ISSN 1522-1539 ; 0363-6135
    ISSN (online) 1522-1539
    ISSN 0363-6135
    DOI 10.1152/ajpheart.00062.2006
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  4. Article ; Online: The ubiquitin proteasome system and myocardial ischemia.

    Calise, Justine / Powell, Saul R

    American journal of physiology. Heart and circulatory physiology

    2012  Volume 304, Issue 3, Page(s) H337–49

    Abstract: The ubiquitin proteasome system (UPS) has been the subject of intensive research over the past 20 years to define its role in normal physiology and in pathophysiology. Many of these studies have focused in on the cardiovascular system and have determined ...

    Abstract The ubiquitin proteasome system (UPS) has been the subject of intensive research over the past 20 years to define its role in normal physiology and in pathophysiology. Many of these studies have focused in on the cardiovascular system and have determined that the UPS becomes dysfunctional in several pathologies such as familial and idiopathic cardiomyopathies, atherosclerosis, and myocardial ischemia. This review presents a synopsis of the literature as it relates to the role of the UPS in myocardial ischemia. Studies have shown that the UPS is dysfunctional during myocardial ischemia, and recent studies have shed some light on possible mechanisms. Other studies have defined a role for the UPS in ischemic preconditioning which is best associated with myocardial ischemia and is thus presented here. Very recent studies have started to define roles for specific proteasome subunits and components of the ubiquitination machinery in various aspects of myocardial ischemia. Lastly, despite the evidence linking myocardial ischemia and proteasome dysfunction, there are continuing suggestions that proteasome inhibitors may be useful to mitigate ischemic injury. This review presents the rationale behind this and discusses both supportive and nonsupportive studies and presents possible future directions that may help in clarifying this controversy.
    MeSH term(s) Animals ; Autophagy ; Heart/physiology ; Humans ; Ischemic Preconditioning ; Myocardial Ischemia/pathology ; Myocardial Ischemia/physiopathology ; Myocardium/pathology ; Oxidative Stress/physiology ; Proteasome Endopeptidase Complex/physiology ; Ubiquitin/physiology
    Chemical Substances Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2012-12-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 603838-4
    ISSN 1522-1539 ; 0363-6135
    ISSN (online) 1522-1539
    ISSN 0363-6135
    DOI 10.1152/ajpheart.00604.2012
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  5. Article ; Online: Assessment of cytokine-modulated proteasome activity.

    Kirk, Christopher J / Powell, Saul R / Miller, Edmund J

    Methods in molecular biology (Clifton, N.J.)

    2014  Volume 1172, Page(s) 147–162

    Abstract: This chapter presents two methods for assessment of proteasome function. The first is a modification of the standard fluorogenic peptide cleavage assay which takes into account the effect of ATP on proteasome activity. This method is described in both ... ...

    Abstract This chapter presents two methods for assessment of proteasome function. The first is a modification of the standard fluorogenic peptide cleavage assay which takes into account the effect of ATP on proteasome activity. This method is described in both its macro and high throughput micro-assay forms. The second is the Proteasome Constitutive Immuno-Subunit (active site) ELISA or ProCISE method. ProCISE is a modification of active site directed probe analysis and allows for convenient differentiation between active constitutive and immuno-subunits. While the utility of measuring proteasome activity and its relationship to cytokine action and inflammation are clear, the assessment and interpretation is not always straightforward. Therefore, we also discuss the pitfalls of the standard fluorogenic assay, particularly in the interpretation of results obtained, and the advantages of the newer, ProCISE assay.
    MeSH term(s) Acetylcysteine/analogs & derivatives ; Acetylcysteine/chemistry ; Adenosine Triphosphate/chemistry ; Adenosine Triphosphate/metabolism ; Animals ; Antibodies/chemistry ; Catalytic Domain ; Cysteine Proteinase Inhibitors/chemistry ; Cytokines/metabolism ; Fluorescent Dyes/chemistry ; Horseradish Peroxidase/chemistry ; Humans ; Immunoassay ; Kinetics ; Luminescent Measurements ; Peptides/chemical synthesis ; Peptides/metabolism ; Proteasome Endopeptidase Complex/analysis ; Proteasome Endopeptidase Complex/metabolism ; Protein Subunits/analysis ; Protein Subunits/metabolism ; Proteolysis ; Spectrometry, Fluorescence ; Tissue Extracts/chemistry ; Tissue Extracts/metabolism
    Chemical Substances Antibodies ; Cysteine Proteinase Inhibitors ; Cytokines ; Fluorescent Dyes ; Peptides ; Protein Subunits ; Tissue Extracts ; lactacystin (133343-34-7) ; Adenosine Triphosphate (8L70Q75FXE) ; Horseradish Peroxidase (EC 1.11.1.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Acetylcysteine (WYQ7N0BPYC)
    Language English
    Publishing date 2014-06-08
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-0928-5_13
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  6. Article ; Online: Decreased sensitivity associated with an altered formulation of a commercially available kit for detection of protein carbonyls.

    Wang, Ping / Powell, Saul R

    Free radical biology & medicine

    2010  Volume 49, Issue 2, Page(s) 119–121

    Abstract: Carbonylation is a commonly studied form of oxidative modification to proteins which can be conveniently detected using commercially available kits. The most common of these kits is the Oxyblot Protein Oxidation Detection Kit (Chemicon/Millipore). Over ... ...

    Abstract Carbonylation is a commonly studied form of oxidative modification to proteins which can be conveniently detected using commercially available kits. The most common of these kits is the Oxyblot Protein Oxidation Detection Kit (Chemicon/Millipore). Over the past year we have observed severely diminished sensitivity of these kits which was shown to be a result of a change in the formulation of one of the components supplied in the kit. This component, the 10X 2,4-dinitrophenylhydrazine derivatization solution, which had previously been dissolved in 100% trifluoroacetic acid (TFA), was now dissolved in 2N hydrochloric acid, which according to our results is not acid enough. Further, we observed that upon storage even DNPH dissolved in TFA is subject to degradation. Based on these studies, we make recomendations that should improve the sensitivity and reproducibilty of this assay.
    MeSH term(s) Animals ; Biochemistry/methods ; Complex Mixtures/chemistry ; Fluorenes/chemistry ; Humans ; Hydrazines/chemistry ; Hydrochloric Acid/chemistry ; Hydrogen-Ion Concentration ; Protein Carbonylation ; Reagent Kits, Diagnostic ; Reproducibility of Results ; Sensitivity and Specificity
    Chemical Substances Complex Mixtures ; Fluorenes ; Hydrazines ; Reagent Kits, Diagnostic ; dinitrophenylhydrazine ; trifluorenylamine ; Hydrochloric Acid (QTT17582CB)
    Language English
    Publishing date 2010-07-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 807032-5
    ISSN 1873-4596 ; 0891-5849
    ISSN (online) 1873-4596
    ISSN 0891-5849
    DOI 10.1016/j.freeradbiomed.2010.03.005
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  7. Article ; Online: The ubiquitin-proteasome system in myocardial ischaemia and preconditioning.

    Powell, Saul R / Divald, Andras

    Cardiovascular research

    2009  Volume 85, Issue 2, Page(s) 303–311

    Abstract: The ubiquitin-proteasome system (UPS) represents the major pathway for degradation of intracellular proteins. This article reviews the major components and configurations of the UPS including the 26S proteasome and 11S activated proteasome relevant to ... ...

    Abstract The ubiquitin-proteasome system (UPS) represents the major pathway for degradation of intracellular proteins. This article reviews the major components and configurations of the UPS including the 26S proteasome and 11S activated proteasome relevant to myocardial ischaemia. We then present the evidence that the UPS is dysfunctional during myocardial ischaemia as well as potential consequences of this, including dysregulation of target substrates, many of them active signalling proteins, and accumulation of oxidized proteins. As part of this discussion, potential mechanisms, including ATP depletion, inhibition by insoluble protein aggregates, and oxidation of proteasome and regulatory particle subunits, are discussed. Finally, the evidence suggesting a role for the UPS in ischaemic preconditioning is presented. Much of this is inferential but clearly indicates the need for additional research.
    MeSH term(s) Adenosine Triphosphate/metabolism ; Animals ; Autophagy ; Humans ; Ischemic Preconditioning, Myocardial ; Myocardial Ischemia/drug therapy ; Myocardial Ischemia/etiology ; Myocardial Reperfusion ; Proteasome Endopeptidase Complex/chemistry ; Proteasome Endopeptidase Complex/physiology ; Proteasome Inhibitors ; Proteins/chemistry ; Ubiquitin/metabolism
    Chemical Substances Proteasome Inhibitors ; Proteins ; Ubiquitin ; Adenosine Triphosphate (8L70Q75FXE) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2009-09-30
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 80340-6
    ISSN 1755-3245 ; 0008-6363
    ISSN (online) 1755-3245
    ISSN 0008-6363
    DOI 10.1093/cvr/cvp321
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  8. Article ; Online: The role of the ubiquitin-proteasome pathway in cardiovascular disease.

    Depre, Christophe / Powell, Saul R / Wang, Xuejun

    Cardiovascular research

    2009  Volume 85, Issue 2, Page(s) 251–252

    MeSH term(s) Animals ; Cardiovascular Diseases/etiology ; Humans ; Proteasome Endopeptidase Complex/physiology ; Signal Transduction ; Ubiquitin/metabolism
    Chemical Substances Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2009-11-05
    Publishing country England
    Document type Editorial
    ZDB-ID 80340-6
    ISSN 1755-3245 ; 0008-6363
    ISSN (online) 1755-3245
    ISSN 0008-6363
    DOI 10.1093/cvr/cvp362
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  9. Article: Upregulation of proteasome activity rescues cardiomyocytes following pulse treatment with a proteasome inhibitor.

    Wang, Ping / Calise, Justine / Powell, Keren / Divald, Andras / Powell, Saul R

    American journal of cardiovascular disease

    2014  Volume 4, Issue 1, Page(s) 6–13

    Abstract: This study examined the hypothesis that cardiomyocyte metabolism is inherently linked to the Ubiquitin Proteasome System. Rat neonatal ventricular cardiomyocytes were pulse-treated with 5 αM lactacystin for 30 min, resulting in 95% loss of proteasome ... ...

    Abstract This study examined the hypothesis that cardiomyocyte metabolism is inherently linked to the Ubiquitin Proteasome System. Rat neonatal ventricular cardiomyocytes were pulse-treated with 5 αM lactacystin for 30 min, resulting in 95% loss of proteasome activity, and then maintained in culture for up to 24 h. Pulse-treatment resulted in 36% decrease in cardiomyocyte mitochondrial reductase activity by 8 h which improved to 15% by 24 h. Bax proteins were increased 2.5-fold by 8 h but declined by 16 h. Similar effects were observed for ubiquitinated proteins suggesting recovery of proteasome function. Proteasome activity started to increase by 4 h and was back to baseline by 16 h. Multiple proteasome subunits, including α1, were upregulated with peak 2 to 2.5-fold increased protein levels at 8-16 h post-lactacystin which then declined. Incubating cardiomyocytes with 4 αM morpholino-antisense oligonucleotides to the α1-subunit for up to 24 h post-lactacystin diminished recovery of proteasome activity (45% at 24 h) and prevented the increase in α1 protein levels. Ubiquitinated proteins remained elevated and cardiomyocyte mitochondrial reductase activity was decreased 35% by 16 h. These results show that diminished function of the ubiquitin proteasome system decreases cardiomyocyte metabolism. If proteasome activity recovers, function improves, but preventing recovery diminishes metabolic function supporting the hypothesis that cardiomyocyte metabolism is inherently linked to the ubiquitin proteasome system.
    Language English
    Publishing date 2014-01-15
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2616844-3
    ISSN 2160-200X
    ISSN 2160-200X
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  10. Article ; Online: Enhancement of proteasome function by PA28α overexpression protects against oxidative stress.

    Li, Jie / Powell, Saul R / Wang, Xuejun

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology

    2010  Volume 25, Issue 3, Page(s) 883–893

    Abstract: The principal function of the proteasome is targeted degradation of intracellular proteins. Proteasome dysfunction has been observed in experimental cardiomyopathies and implicated in human congestive heart failure. Measures to enhance proteasome ... ...

    Abstract The principal function of the proteasome is targeted degradation of intracellular proteins. Proteasome dysfunction has been observed in experimental cardiomyopathies and implicated in human congestive heart failure. Measures to enhance proteasome proteolytic function are currently lacking but would be beneficial in testing the pathogenic role of proteasome dysfunction and could have significant therapeutic potential. The association of proteasome activator 28 (PA28) with the 20S proteasome may play a role in antigen processing. It is unclear, however, whether the PA28 plays any important role outside of antigen presentation, although up-regulation of PA28 has been observed in certain types of cardiomyopathy. Here, we show that PA28α overexpression (PA28αOE) stabilized PA28β, increased 11S proteasomes, and enhanced the degradation of a previously validated proteasome surrogate substrate (GFPu) in cultured neonatal rat cardiomyocytes. PA28αOE significantly attenuated H(2)O(2)-induced increases in the protein carbonyls and markedly suppressed apoptosis in cultured cardiomyocytes under basal conditions or when stressed by H(2)O(2). We conclude that PA28αOE is sufficient to up-regulate 11S proteasomes, enhance proteasome-mediated removal of misfolded and oxidized proteins, and protect against oxidative stress in cardiomyocytes, providing a highly sought means to increase proteasomal degradation of abnormal cellular proteins.
    MeSH term(s) Animals ; Animals, Newborn ; Antibodies/pharmacology ; Apoptosis/physiology ; Cell Cycle Proteins ; Cells, Cultured ; Gene Expression Regulation, Enzymologic/physiology ; Green Fluorescent Proteins/genetics ; HEK293 Cells ; Humans ; Mice ; Myocytes, Cardiac/cytology ; Myocytes, Cardiac/enzymology ; Oxidative Stress/physiology ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/immunology ; Proteasome Endopeptidase Complex/metabolism ; Proteins/genetics ; Proteins/immunology ; Proteins/metabolism ; Rabbits ; Rats
    Chemical Substances Antibodies ; Cell Cycle Proteins ; Proteins ; Psme1 protein, rat ; Green Fluorescent Proteins (147336-22-9) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Psme1 protein, mouse (EC 3.4.25.1) ; Psme2 protein, mouse (EC 3.4.25.1) ; 26S proteasome non-ATPase regulatory subunit 13 (EC 3.6.1.-)
    Language English
    Publishing date 2010-11-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 639186-2
    ISSN 1530-6860 ; 0892-6638
    ISSN (online) 1530-6860
    ISSN 0892-6638
    DOI 10.1096/fj.10-160895
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