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Diet-derived advanced glycation end products or lipofuscin disrupts proteostasis and reduces life span in Drosophila melanogaster
Abstract
Advanced glycation end product (AGE)-modified proteins are formed by the nonenzymatic glycation of free amino groups of proteins and, along with lipofuscin (a highly oxidized aggregate of covalently cross-linked proteins, sugars, and lipids), have been found to accumulate during aging and in several age-related diseases. As the in vivo effects of diet-derived AGEs or lipofuscin remain elusive, we sought to study the impact of oral administration of glucose-, fructose-, or ribose-modified albumin or of artificial lipofuscin in a genetically tractable model organism. We report herein that continuous feeding of young Drosophila flies with culture medium enriched in AGEs or in lipofuscin resulted in reduced locomotor performance and in accelerated rates of AGE-modified proteins and carbonylated proteins accumulation in the somatic tissues and hemolymph of flies, as well as in a significant reduction of flies health span and life span. These phenotypic effects were accompanied by reduced proteasome peptidase activities in both the hemolymph and the somatic tissues of flies and higher levels of oxidative stress; furthermore, oral administration of AGEs or lipofuscin in flies triggered an upregulation of the lysosomal cathepsin B, L activities. Finally, RNAi-mediated cathepsin D knockdown reduced flies longevity and significantly augmented the deleterious effects of AGEs and lipofuscin, indicating that lysosomal cathepsins reduce the toxicity of diet-derived AGEs or lipofuscin. Our…
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“For example, feeding D. melanogaster with advanced glycation end products (AGE) or lipofuscin (an aggregate of covalently crosslinked proteins, sugars, and lipids) causes the accumulation of AGE-modified and carbonylated proteins with a reduction of healthspan and lifespan that is further accentuated upon knockdown of the lysosomal protease cathepsin D 91 .”
From Hallmarks of aging: An expanding universe (2023) · cites this paper as [91]
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Cites
Stress-activated cap’n’collar transcription factors in aging and human disease
Sykiotis, G. P., & Bohmann, D. (2010) · Science Signaling · doi:10.1126/scisignal.3112re3 · Cited by 776
Cataldo, A. M., Barnett, J. L., Berman, S. A., Li, J., Quarless, S., Bursztajn, S., Lippa, C., & Nixon, R. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90324-0 · Cited by 379
Assar, S. H., Moloney, C., Lima, M., Magee, R., & Ames, J. M. (2009) · Amino Acids · doi:10.1007/s00726-008-0071-4 · Cited by 206
Research works printed but not linked: 63
- Ulrich, 2001, Protein glycation, diabetes, and aging, Recent Prog. Horm. Res., 56, 1, 10.1210/rp.56.1.1 · DOI
- Takeuchi, 2009, Involvement of toxic AGEs (TAGE) in the pathogenesis of diabetic vascular complications and Alzheimer's disease, J. Alzheimers Dis., 16, 845, 10.3233/JAD-2009-0974 · DOI
- Nedić, 2013, Molecular effects of advanced glycation end products on cell signalling pathways, ageing and pathophysiology, Free Radic. Res., 47, 28, 10.3109/10715762.2013.806798 · DOI · Paper page
- Uribarri, 2005, Diet-derived advanced glycation end products are major contributors to the body's AGE pool and induce inflammation in healthy subjects, Ann. N. Y. Acad. Sci., 1043, 461, 10.1196/annals.1333.052 · DOI
- Jung, 2007, Lipofuscin: formation, distribution, and metabolic consequences, Ann. N. Y. Acad. Sci., 1119, 97, 10.1196/annals.1404.008 · DOI · Paper page
- Marzabadi, 1991, Mechanisms of lipofuscinogenesis: effect of the inhibition of lysosomal proteinases and lipases under varying concentrations of ambient oxygen in cultured rat neonatal myocardial cells, APMIS, 99, 416, 10.1111/j.1699-0463.1991.tb05170.x · DOI
- Yin, 1996, Biochemical basis of lipofuscin, ceroid, and age pigment-like fluorophores, Free Radic. Biol. Med., 21, 871, 10.1016/0891-5849(96)00175-X · DOI
- Sitte, 2000, Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts, FASEB J., 14, 1490, 10.1096/fj.99-0843com · DOI
- Terman, 2006, Mitochondrial damage and intralysosomal degradation in cellular aging, Mol. Aspects Med., 27, 471, 10.1016/j.mam.2006.08.006 · DOI
- Kirkwood, 2000, Why do we age?, Nature, 408, 233, 10.1038/35041682 · DOI · Paper page
- Rattan, 2006, Theories of biological aging: genes, proteins, and free radicals, Free Radic. Res., 40, 1230, 10.1080/10715760600911303 · DOI
- Wensink, 2013, Age-specificity and the evolution of senescence: a discussion, Biogerontology, 14, 99, 10.1007/s10522-012-9410-7 · DOI
- Rattan, 2008, Increased molecular damage and heterogeneity as the basis of aging, Biol. Chem., 389, 267, 10.1515/BC.2008.030 · DOI
- Trougakos, 2013, Non-enzymatic post-translational protein modifications and proteostasis network deregulation in carcinogenesis, J. Proteomics, 10.1016/j.jprot.2013.02.024 · DOI
- Hubbard, 2012, Selective autophagy in the maintenance of cellular homeostasis in aging organisms, Biogerontology, 13, 21, 10.1007/s10522-011-9331-x · DOI
- Chondrogianni, 2012, Protein damage, repair and proteolysis, Mol. Aspects Med.
- Navon, 2009, The 26S proteasome: from basic mechanisms to drug targeting, J. Biol. Chem., 284, 33713, 10.1074/jbc.R109.018481 · DOI
- Baraibar, 2012, Changes of the proteasomal system during the aging process, Prog. Mol. Biol. Transl. Sci., 109, 249, 10.1016/B978-0-12-397863-9.00007-9 · DOI
- Pickering, 2012, Degradation of damaged proteins: the main function of the 20S proteasome, Prog. Mol. Biol. Transl. Sci., 109, 227, 10.1016/B978-0-12-397863-9.00006-7 · DOI
- Kastle, 2011, Protein oxidative modification in the aging organism and the role of the ubiquitin proteasomal system, Curr. Pharm. Des., 17, 4007, 10.2174/138161211798764898 · DOI
- Česen, 2012, Lysosomal pathways to cell death and their therapeutic applications, Exp. Cell Res., 318, 1245, 10.1016/j.yexcr.2012.03.005 · DOI
- Jacobson, 2010, Biomarkers of aging in Drosophila, Aging Cell, 9, 466, 10.1111/j.1474-9726.2010.00573.x · DOI
- Cai, 2007, Reduced oxidant stress and extended lifespan in mice exposed to a low glycotoxin diet: association with increased AGER1 expression, Am. J. Pathol., 170, 1893, 10.2353/ajpath.2007.061281 · DOI
- Cai, 2008, Oral glycotoxins determine the effects of calorie restriction on oxidant stress, age-related diseases, and lifespan, Am. J. Pathol., 173, 327, 10.2353/ajpath.2008.080152 · DOI
- Cai, 2012, Oral advanced glycation endproducts (AGEs) promote insulin resistance and diabetes by depleting the antioxidant defenses AGE receptor-1 and sirtuin 1, Proc. Natl. Acad. Sci. USA, 109, 15888, 10.1073/pnas.1205847109 · DOI
- Grimm, 2012, Cathepsins D and L reduce the toxicity of advanced glycation end products, Free Radic. Biol. Med., 52, 1011, 10.1016/j.freeradbiomed.2011.12.021 · DOI
- Höhn, 2010, Lipofuscin-bound iron is a major intracellular source of oxidants: role in senescent cells, Free Radic. Biol. Med., 48, 1100, 10.1016/j.freeradbiomed.2010.01.030 · DOI
- Höhn, 2011, Lipofuscin inhibits the proteasome by binding to surface motifs, Free Radic. Biol. Med., 50, 585, 10.1016/j.freeradbiomed.2010.12.011 · DOI
- Kim, 2007, Common aging pathways in worms, flies, mice and humans, J. Exp. Biol., 210, 1607, 10.1242/jeb.004887 · DOI
- Stolzing, 2006, Degradation of glycated bovine serum albumin in microglial cells, Free Radic. Biol. Med., 40, 1017, 10.1016/j.freeradbiomed.2005.10.061 · DOI
- Tsakiri, 2013, Differential regulation of proteasome functionality in reproductive vs. somatic tissues of Drosophila during aging or oxidative stress, FASEB J., 27, 2407, 10.1096/fj.12-221408 · DOI
- Vernace, 2007, Aging perturbs 26S proteasome assembly in Drosophila melanogaster, FASEB J., 21, 2672, 10.1096/fj.06-6751com · DOI
- Trougakos, 1999, Biochemical and immunocytochemical analysis of vitellogenesis in the olive fruit fly Dacus (bactrocera) oleae (Diptera: Tephritidae), Cell Biol. Int., 23, 417, 10.1006/cbir.1999.0380 · DOI
- Tsakiri, 2013, Proteasome dysfunction in Drosophila signals to an Nrf2-dependent regulatory circuit aiming to restore proteostasis and prevent premature aging, Aging Cell, 12, 802, 10.1111/acel.12111 · DOI
- Grimm, 2010, Cathepsin D is one of the major enzymes involved in intracellular degradation of AGE-modified proteins, Free Radic. Res., 44, 1013, 10.3109/10715762.2010.495127 · DOI
- Uribarri, 2010, Advanced glycation end products in foods and a practical guide to their reduction in the diet, J. Am. Diet. Assoc., 110, 911, 10.1016/j.jada.2010.03.018 · DOI · Paper page
- Sitte, 2001, Lipofuscin accumulation in proliferating fibroblasts in vitro: an indicator of oxidative stress, Exp. Gerontol., 36, 475, 10.1016/S0531-5565(00)00253-9 · DOI
- Höhn, 2012, Lipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblasts, Free Radic. Biol. Med., 53, 1760, 10.1016/j.freeradbiomed.2012.08.591 · DOI
- Grune, 2004, Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and ‘aggresomes’ during oxidative stress, aging, and disease, Int. J. Biochem. Cell Biol., 36, 2519, 10.1016/j.biocel.2004.04.020 · DOI
- Queisser, 2010, Hyperglycemia impairs proteasome function by methylglyoxal, Diabetes, 59, 670, 10.2337/db08-1565 · DOI
- Cervantes-Laurean, 2005, Nuclear proteasome activation and degradation of carboxymethylated histones in human keratinocytes following glyoxal treatment, Free Radic. Biol. Med., 38, 786, 10.1016/j.freeradbiomed.2004.11.030 · DOI
- Schmid, 2008, Induction of heat shock proteins and the proteasome system by casein-N epsilon-(carboxymethyl)lysine and N epsilon-(carboxymethyl)lysine in Caco-2 cells, Ann. N. Y. Acad. Sci., 1126, 257, 10.1196/annals.1433.062 · DOI
- Yamagishi, 2002, Advanced glycation end products induced apoptosis and overexpression of vascular endothelial growth factor in bovine retinal pericytes, Biochem. Biophys. Res. Commun., 290, 973, 10.1006/bbrc.2001.6312 · DOI
- Bansal, 2012, Advanced glycation end products enhance reactive oxygen and nitrogen species generation in neutrophils in vitro, Mol. Cell. Biochem., 361, 289, 10.1007/s11010-011-1114-9 · DOI
- Wautier, 2001, Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE, Am. J. Physiol. Endocrinol. Metab., 280, E685, 10.1152/ajpendo.2001.280.5.E685 · DOI
- Coughlan, 2009, RAGE-induced cytosolic ROS promote mitochondrial superoxide generation in diabetes, J. Am. Soc. Nephrol., 20, 742, 10.1681/ASN.2008050514 · DOI
- Uribarri, 2007, Single oral challenge by advanced glycation end products acutely impairs endothelial function in diabetic and nondiabetic subjects, Diabetes Care, 30, 2579, 10.2337/dc07-0320 · DOI
- Patel, 2012, Effect of dietary advanced glycation end products on mouse liver, PLoS One, 7, e35143, 10.1371/journal.pone.0035143 · DOI
- Wei, 2012, D-Ribose in glycation and protein aggregation, Biochim. Biophys. Acta, 1820, 488, 10.1016/j.bbagen.2012.01.005 · DOI
- Han, 2011, D-Ribose induces cellular protein glycation and impairs mouse spatial cognition, PLoS One, 6, e24623, 10.1371/journal.pone.0024623 · DOI
- Akhter, 2013, Moinuddin; Ahmad, S. Bio-physical characterization of ribose induced glycation: a mechanistic study on DNA perturbations, Int. J. Biol. Macromol., 58, 206, 10.1016/j.ijbiomac.2013.03.036 · DOI
- Chen, 2010, Ribosylation rapidly induces alpha-synuclein to form highly cytotoxic molten globules of advanced glycation end products, PLoS One, 5, e9052, 10.1371/journal.pone.0009052 · DOI
- Futerman, 2004, The cell biology of lysosomal storage disorders, Nat. Rev. Mol. Cell Biol., 5, 554, 10.1038/nrm1423 · DOI
- Pallauf, 2013, Autophagy, polyphenols and healthy ageing, Ageing Res. Rev., 12, 237, 10.1016/j.arr.2012.03.008 · DOI
- Hu, 2012, ERK and Akt signaling pathways are involved in advanced glycation end product-induced autophagy in rat vascular smooth muscle cells, Int. J. Mol. Med., 29, 613, 10.3892/ijmm.2012.891 · DOI
- Shacka, 2007, Cathepsin D deficiency induces persistent neurodegeneration in the absence of Bax-dependent apoptosis, J. Neurosci., 27, 2081, 10.1523/JNEUROSCI.5577-06.2007 · DOI
- Khurana, 2010, Lysosomal dysfunction promotes cleavage and neurotoxicity of tau in vivo, PLoS Genet., 6, e1001026, 10.1371/journal.pgen.1001026 · DOI
- Myllykangas, 2005, Cathepsin D-deficient Drosophila recapitulate the key features of neuronal ceroid lipofuscinoses, Neurobiol. Dis., 19, 194, 10.1016/j.nbd.2004.12.019 · DOI
- Lamore, 2010, Proteomic identification of cathepsin B and nucleophosmin as novel UVA-targets in human skin fibroblasts, Photochem. Photobiol., 86, 1307, 10.1111/j.1751-1097.2010.00818.x · DOI
- Miura, 2010, Translocation of lysosomal cathepsin D caused by oxidative stress or proteasome inhibition in primary cultured neurons and astrocytes, Biol. Pharm. Bull., 33, 22, 10.1248/bpb.33.22 · DOI
- Semba, 2009, Plasma carboxymethyl-lysine, an advanced glycation end product, and all-cause and cardiovascular disease mortality in older community-dwelling adults, J. Am. Geriatr. Soc., 57, 1874, 10.1111/j.1532-5415.2009.02438.x · DOI
- Lin, 2003, Dietary glycotoxins promote diabetic atherosclerosis in apolipoprotein E-deficient mice, Atherosclerosis, 168, 213, 10.1016/S0021-9150(03)00050-9 · DOI
- Zheng, 2002, Prevention of diabetic nephropathy in mice by a diet low in glycoxidation products, Diabetes Metab. Res. Rev, 18, 224, 10.1002/dmrr.283 · DOI
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Metadata
- Authors
- Tsakiri, E. N., Iliaki, K. K., Höhn, A., Grimm, S., Papassideri, I. S., Grune, T., & Trougakos, I. P.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2013-12
- Volume
- 65
- Pages
- 1155-1163
- ISSN
- 0891-5849
- Cited by
- 64
- References
- 3
- Language
- en
- Funders
- EU-FP7 Capacities (REGPOT-CT-2011-284460)
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