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  • 1.
    Chondrogianni, Niki
    et al.
    Inst Biol Med Chem & Biotechnol, Natl Hellen Res Fdn, Athens, Greece.
    Sakellari, Marianthi
    Örebro University, School of Health and Medical Sciences, Örebro University, Sweden. Inst Biol Med Chem & Biotechnol, Natl Hellen Res Fdn, Athens, Greece.
    Lefaki, Maria
    Inst Biol Med Chem & Biotechnol, Natl Hellen Res Fdn, Athens, Greece.
    Papaevgeniou, Nikoletta
    Inst Biol Med Chem & Biotechnol, Natl Hellen Res Fdn, Athens, Greece.
    Gonos, Efstathios S.
    Inst Biol Med Chem & Biotechnol, Natl Hellen Res Fdn, Athens, Greece.
    Proteasome activation delays aging in vitro and in vivo2014In: Free Radical Biology & Medicine, ISSN 0891-5849, E-ISSN 1873-4596, Vol. 71, p. 303-320Article, review/survey (Refereed)
    Abstract [en]

    Aging is a natural biological process that is characterized by a progressive accumulation of macromolecular damage. In the proteome, aging is accompanied by decreased protein homeostasis and function of the major cellular proteolytic systems, leading to the accumulation of unfolded, misfolded, or aggregated proteins. In particular, the proteasome is responsible for the removal of normal as well as damaged or misfolded proteins. Extensive work during the past several years has clearly demonstrated that proteasome activation by either genetic means or use of compounds significantly retards aging. Importantly, this represents a common feature across evolution, thereby suggesting proteasome activation to be an evolutionarily conserved mechanism of aging and longevity regulation. This review article reports on the means of function of these proteasome activators and how they regulate aging in various species. (C) 2014 Elsevier Inc. All rights reserved.

  • 2.
    Chondrogianni, Niki
    et al.
    National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens, Greece.
    Voutetakis, Konstantinos
    National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens, Greece.
    Kapetanou, Marianna
    National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens, Greece.
    Delitsikou, Vasiliki
    National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens, Greece.
    Papaevgeniou, Nikoletta
    National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens, Greece.
    Sakellari, Marianthi
    Örebro University, School of Health and Medical Sciences, Örebro University, Sweden. National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens, Greece.
    Lefaki, Maria
    National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens, Greece.
    Filippopoulou, Konstantina
    National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens, Greece.
    Gonos, Efstathios S.
    National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry and Biotechnology, Athens, Greece; School of Medicine, Örebro University, Örebro, Sweden.
    Proteasome activation: an innovative promising approach for delaying aging and retarding age-related diseases2015In: Ageing Research Reviews, ISSN 1568-1637, E-ISSN 1872-9649, Vol. 23, p. 37-55Article, review/survey (Refereed)
    Abstract [en]

    Aging is a natural process accompanied by a progressive accumulation of damage in all constituent macromolecules (nucleic acids, lipids and proteins). Accumulation of damage in proteins leads to failure of proteostasis (or vice versa) due to increased levels of unfolded, misfolded or aggregated proteins and, in turn, to aging and/or age-related diseases. The major cellular proteolytic machineries, namely the proteasome and the lysosome, have been shown to dysfunction during aging and age-related diseases. Regarding the proteasome, it is well established that it can be activated either through genetic manipulation or through treatment with natural or chemical compounds that eventually result to extension of lifespan or deceleration of the progression of age-related diseases. This review article focuses on proteasome activation studies in several species and cellular models and their effects on aging and longevity. Moreover, it summarizes findings regarding proteasome activation in the major age-related diseases as well as in progeroid syndromes.

  • 3.
    Papaevgeniou, Nikoletta
    et al.
    Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece; Faculty of Biology and Pharmacy, Institute of Nutrition, Friedrich Schiller University of Jena, Jena, Germany.
    Sakellari, Marianthi
    Örebro University, School of Medical Sciences. Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece.
    Jha, Sweta
    Translational Cancer Biology Program, Research Programs Unit, University of Helsinki, Helsinki, Finland.
    Tavernarakis, Nektarios
    Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, Heraklion, Greece; Faculty of Medicine, Department of Basic Sciences, University of Crete, Heraklion, Greece.
    Holmberg, Carina I
    Programs Unit, University of Helsinki, Helsinki, Finland.
    Gonos, Efstathios S.
    Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece; Medical School, Örebro University, Örebro, Sweden.
    Chondrogianni, Niki
    Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece.
    18α-Glycyrrhetinic Acid Proteasome Activator Decelerates Aging and Alzheimer's Disease Progression in Caenorhabditis elegans and Neuronal Cultures2016In: Antioxidants and Redox Signaling, ISSN 1523-0864, E-ISSN 1557-7716, Vol. 25, no 16, p. 855-869Article in journal (Refereed)
    Abstract [en]

    Aims: Proteasomes are constituents of the cellular proteolytic networks that maintain protein homeostasis through regulated proteolysis of normal and abnormal (in any way) proteins. Genetically mediated proteasome activation in multicellular organisms has been shown to promote longevity and to exert protein antiaggregation activity. In this study, we investigate whether compound-mediated proteasome activation is feasible in a multicellular organism and we dissect the effects of such approach in aging and Alzheimer's disease (AD) progression.

    Results: Feeding of wild-type Caenorhabditis elegans with 18α-glycyrrhetinic acid (18α-GA; a previously shown proteasome activator in cell culture) results in enhanced levels of proteasome activities that lead to a skinhead-1- and proteasome activation-dependent life span extension. The elevated proteasome function confers lower paralysis rates in various AD nematode models accompanied by decreased Aβ deposits, thus ultimately decelerating the progression of AD phenotype. More importantly, similar positive results are also delivered when human and murine cells of nervous origin are subjected to 18α-GA treatment.

    Innovation: This is the first report of the use of 18α-GA, a diet-derived compound as prolongevity and antiaggregation factor in the context of a multicellular organism.

    Conclusion: Our results suggest that proteasome activation with downstream positive outcomes on aging and AD, an aggregation-related disease, is feasible in a nongenetic manipulation manner in a multicellular organism. Moreover, they unveil the need for identification of antiaging and antiamyloidogenic compounds among the nutrients found in our normal diet.

  • 4.
    Sakellari, Marianthi
    Örebro University, School of Medical Sciences.
    Functional analysis of the proteasome in eukaryotic organisms2020Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Proteasome degradation machinery is responsible for the turnover of a huge variety of normal and abnormal proteins, thus regulating a plethora of cellular processes. Aging is an inevitable biological process that is characterized by reduced proteasome function that leads to proteotoxic stress. Compound-related interventions, that ameliorate proteasome system collapse, retard aging process. In the present thesis, 18α-glycyrrhetinic acid (18α-GA), a natural compound with known proteasome activating properties in cells, was indicated to activate proteasome also in the multicellular organism Caenorhabditis elegans (C. elegans). Evaluation of the antiaging and protein anti-aggregation effects of this bioactive compound indicated that 18α-GA promoted longevity in nematodes through proteasome-and SKN-1-mediated activation and decelerated Alzheimer’sdisease progression and neuropathology both in nematodes and neuronal cells. Additionally, the crosstalk between protein synthesis and proteasome-mediated protein degradation was analyzed in eukaryotic organisms under various cellular conditions. Protein synthesis inhibition was observed to increase proteasome function and assembly in human primary embryonic fibroblasts, with heat shock protein chaperone machinery to contribute to the elevated proteasome assembly. Alternatively, protein synthesis inhibition increased the protein levels of specific proteasome subunits without influencing the proteasome activity in C. elegans. Furthermore, proteasome activation by means which have also pro-longevity effects decreased the protein synthesis rate both in human fibroblast cellsand nematodes. This thesis suggests: 1) that a diet-derived compound could act as a pro-longevity and anti-aggregation agent in the context of amulticellular organism and 2) the existence of a complex interplay between anabolic and catabolic processes under different cellular conditions, across species.

    List of papers
    1. 18α-Glycyrrhetinic Acid Proteasome Activator Decelerates Aging and Alzheimer's Disease Progression in Caenorhabditis elegans and Neuronal Cultures
    Open this publication in new window or tab >>18α-Glycyrrhetinic Acid Proteasome Activator Decelerates Aging and Alzheimer's Disease Progression in Caenorhabditis elegans and Neuronal Cultures
    Show others...
    2016 (English)In: Antioxidants and Redox Signaling, ISSN 1523-0864, E-ISSN 1557-7716, Vol. 25, no 16, p. 855-869Article in journal (Refereed) Published
    Abstract [en]

    Aims: Proteasomes are constituents of the cellular proteolytic networks that maintain protein homeostasis through regulated proteolysis of normal and abnormal (in any way) proteins. Genetically mediated proteasome activation in multicellular organisms has been shown to promote longevity and to exert protein antiaggregation activity. In this study, we investigate whether compound-mediated proteasome activation is feasible in a multicellular organism and we dissect the effects of such approach in aging and Alzheimer's disease (AD) progression.

    Results: Feeding of wild-type Caenorhabditis elegans with 18α-glycyrrhetinic acid (18α-GA; a previously shown proteasome activator in cell culture) results in enhanced levels of proteasome activities that lead to a skinhead-1- and proteasome activation-dependent life span extension. The elevated proteasome function confers lower paralysis rates in various AD nematode models accompanied by decreased Aβ deposits, thus ultimately decelerating the progression of AD phenotype. More importantly, similar positive results are also delivered when human and murine cells of nervous origin are subjected to 18α-GA treatment.

    Innovation: This is the first report of the use of 18α-GA, a diet-derived compound as prolongevity and antiaggregation factor in the context of a multicellular organism.

    Conclusion: Our results suggest that proteasome activation with downstream positive outcomes on aging and AD, an aggregation-related disease, is feasible in a nongenetic manipulation manner in a multicellular organism. Moreover, they unveil the need for identification of antiaging and antiamyloidogenic compounds among the nutrients found in our normal diet.

    Place, publisher, year, edition, pages
    New Rochelle, USA: Mary Ann Liebert, 2016
    Keywords
    Proteasome activation, lifespan extension, aging, Alzheimer’s disease, aggregation, proteostasis
    National Category
    Biochemistry and Molecular Biology
    Identifiers
    urn:nbn:se:oru:diva-49639 (URN)10.1089/ars.2015.6494 (DOI)000388262600001 ()26886723 (PubMedID)
    Note

    Funding Agencies:

    U.S. National Institutes of Health National Center for Research Resources

    Thales GenAge QALHS AP:10479/3.7.12 MIS380228

    MAESTRO by the European Union (European Social Fund)

    Operational Program, Education and Lifelong Learning, of the National Strategic Reference Framework (NSRF)

    European Union 266486

    IKYDA fellowship

    Empirikion Foundation Scientific Project

    John S. Latsis Public Benefit Foundation

    Academy of Finland 259797

    COST Actions PROTEOS-TASIS BM1307

    GENiE BM1408

    COST (European Cooperation in Science and Technology)

    Available from: 2016-04-20 Created: 2016-04-05 Last updated: 2020-03-30Bibliographically approved
    2. Protein synthesis inhibition induces proteasome assembly and function
    Open this publication in new window or tab >>Protein synthesis inhibition induces proteasome assembly and function
    2019 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 514, no 1, p. 224-230Article in journal (Refereed) Published
    Abstract [en]

    Protein synthesis and degradation balance have a crucial role in maintenance of cellular homeostasis and function. The ubiquitin-proteasome system is one of the major cellular proteolytic machineries responsible for the removal of normal, abnormal, denatured or in general damaged proteins. Proteasome is a multisubunit enzyme that consists of the 20S core and the 19S regulatory complexes giving rise to multiple active forms. In the present study we investigated the crosstalk between protein synthesis and proteasome-mediated protein degradation. Pharmacological protein synthesis inhibition led to increased proteasome function and assembly of 30S/26S proteasome complexes, in human primary embryonic fibroblasts. The enhancement in proteasome function counted for the degradation of ubiquitinated, misfolded and oxidized proteins. Additionally, it was found that heat shock proteins 70 and 90 are probably involved in the elevated proteasome assembly. Our results provide an insight on how the mechanisms of protein synthesis, protein degradation and heat shock protein chaperones machinery interact under various cellular conditions.

    Place, publisher, year, edition, pages
    Elsevier, 2019
    Keywords
    Proteasome, Proteasome activation, Protein synthesis inhibition, Hsp70, Hsp90
    National Category
    Biochemistry and Molecular Biology
    Identifiers
    urn:nbn:se:oru:diva-79901 (URN)10.1016/j.bbrc.2019.04.114 (DOI)000469406800033 ()31029420 (PubMedID)2-s2.0-85064700180 (Scopus ID)
    Note

    Funding Agencies:

    Research Funding Program: Thales "GenAge" - European Union  QALHS AP:10479/3.7.12 MIS380228

    Greek national funds through the Operational Program "Education and Lifelong Learning" of the National Strategic Reference Framework (NSRF) 

    Available from: 2020-02-14 Created: 2020-02-14 Last updated: 2020-03-30Bibliographically approved
    3. Study of the effects of protein synthesis inhibition on proteasome-mediated protein degradation in Caenorhabditis elegans
    Open this publication in new window or tab >>Study of the effects of protein synthesis inhibition on proteasome-mediated protein degradation in Caenorhabditis elegans
    (English)Manuscript (preprint) (Other academic)
    National Category
    Other Basic Medicine
    Identifiers
    urn:nbn:se:oru:diva-80902 (URN)
    Available from: 2020-03-30 Created: 2020-03-30 Last updated: 2020-03-30Bibliographically approved
    4. Study of the effects of increased proteasome-mediated proteolysis on protein synthesis rate
    Open this publication in new window or tab >>Study of the effects of increased proteasome-mediated proteolysis on protein synthesis rate
    (English)Manuscript (preprint) (Other academic)
    National Category
    Other Basic Medicine
    Identifiers
    urn:nbn:se:oru:diva-80903 (URN)
    Available from: 2020-03-30 Created: 2020-03-30 Last updated: 2020-03-30Bibliographically approved
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    Functional Analysis of the Proteasome in Eukaryotic Organisms
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  • 5.
    Sakellari, Marianthi
    et al.
    Örebro University, School of Medical Sciences. Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece.
    Chondrogianni, Niki
    Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece.
    Gonos, Efstathios S.
    Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece; Örebro University, Medical School, Örebro, Sweden.
    Protein synthesis inhibition induces proteasome assembly and function2019In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 514, no 1, p. 224-230Article in journal (Refereed)
    Abstract [en]

    Protein synthesis and degradation balance have a crucial role in maintenance of cellular homeostasis and function. The ubiquitin-proteasome system is one of the major cellular proteolytic machineries responsible for the removal of normal, abnormal, denatured or in general damaged proteins. Proteasome is a multisubunit enzyme that consists of the 20S core and the 19S regulatory complexes giving rise to multiple active forms. In the present study we investigated the crosstalk between protein synthesis and proteasome-mediated protein degradation. Pharmacological protein synthesis inhibition led to increased proteasome function and assembly of 30S/26S proteasome complexes, in human primary embryonic fibroblasts. The enhancement in proteasome function counted for the degradation of ubiquitinated, misfolded and oxidized proteins. Additionally, it was found that heat shock proteins 70 and 90 are probably involved in the elevated proteasome assembly. Our results provide an insight on how the mechanisms of protein synthesis, protein degradation and heat shock protein chaperones machinery interact under various cellular conditions.

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