title: Proteasome activation delays aging in vitro and in vivo.
abstract: 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.
authors.affiliation: National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry, and Biotechnology, 116 35 Athens, Greece. Electronic address: nikichon@eie.gr.
authors.forename: Niki
authors.initials: N
authors.lastname: Chondrogianni
authors.affiliation: National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry, and Biotechnology, 116 35 Athens, Greece; Örebro University Medical School, Örebro, Sweden.
authors.forename: Marianthi
authors.initials: M
authors.lastname: Sakellari
authors.affiliation: National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry, and Biotechnology, 116 35 Athens, Greece.
authors.forename: Maria
authors.initials: M
authors.lastname: Lefaki
authors.affiliation: National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry, and Biotechnology, 116 35 Athens, Greece.
authors.forename: Nikoletta
authors.initials: N
authors.lastname: Papaevgeniou
authors.affiliation: National Hellenic Research Foundation, Institute of Biology, Medicinal Chemistry, and Biotechnology, 116 35 Athens, Greece; Örebro University Medical School, Örebro, Sweden.
authors.forename: Efstathios S
authors.initials: ES
authors.lastname: Gonos
mesh_terms: D000375:Aging / Q000187:drug effects* / Q000378:metabolism; D000818:Animals; D000975:Antioxidants / Q000494:pharmacology; D017173:Caenorhabditis elegans / Q000201:enzymology / Q000235:genetics; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics; D004789:Enzyme Activation; D005609:Free Radicals / Q000037:antagonists & inhibitors / Q000378:metabolism; D006801:Humans; D008136:Longevity / Q000187:drug effects* / Q000235:genetics; D051379:Mice; D009687:Nuclear Proteins / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D059748:Proteolysis; D051381:Rats; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics
chemical_list: D000975:Antioxidants; D005609:Free Radicals; D009687:Nuclear Proteins; D046988:Proteasome Endopeptidase Complex; C085834:PA700 proteasome activator; C521188:PSME4 protein, human; C119011:26S proteasome non-ATPase regulatory subunit 13
keywords: Aging; Free radicals; Longevity regulation; Proteasome activation; Senescence; Ubiquitin–proteasome system