The double faced role of copper in Ab homeostasis: A survey on the interrelationship between metal dyshomeostasis, UPS functioning and autophagy in neurodegeneration (353 views)
Coordination Chemistry Reviews, 2017 Jun; N/D: 1-22.
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Paper type: Journal Article,
Impact factor: 13.324, 5-year impact factor: 12.743
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Affiliations:
*** IBB - CNR ***
References:
Not available.
Coordination Chemistry Reviews, 2017 Jun; N/D: 1-22.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 13.324, 5-year impact factor: 12.743
Url: Not available.
Keywords: Not available.
Affiliations:
*** IBB - CNR ***
References:
Not available.
The double faced role of copper in Ab homeostasis: A survey on the interrelationship between metal dyshomeostasis, UPS functioning and autophagy in neurodegeneration
Substantial evidence has accumulated over the last decade indicating that diverse age-related neurodegenerative
disorders share a common pathogenic mechanism: the misfolding, aggregation and accumulation
of proteins (termed ‘‘amyloid”) in neuronal tissues. The latest studies suggest that, in principle, any
deficiency in protein homeostasis (proteostasis) may lead to cell dysfunction thus underscoring the protective
key role played by systems regulating the clearance of misfolded or defective proteins in the cell.
On the other hand, an altered metal homeostasis (metallostasis) is thought to be tightly linked to the malfunction
of the ‘‘quality control” machinery of the cell. Metal ions have long been thought to catalyze
amyloid aggregation by initiating protein misfolding. More specifically, redox active metal ions such as
copper have been demonstrated to be majorly involved in a cascade of events resulting in oxidative damage
and neurodegeneration. However, drugs aimed at merely removing excess of such metal ions from
the cell have proven to be unsuccessful thus forcing scientists to amend these traditional views. In particular,
a comprehensive vision of the interplay between metal dyshomeostasis and systems engaged in
proteome maintenance, e.g. proteases, ubiquitin proteasome system (UPS) and autophagy, emerges as a
critical requirement to single out the many culprits of cell dysfunction occurring in aging and in neurodegenerative
pathologies such as Alzheimer’s disease. Here, we will first provide a chemical perspective of
the role of copper in Ab homeostasis, thus giving the necessary outline to the problem of age-related protein
misfolding and altered metallostasis which lead to accumulation processes and consequent decline
of neuron functions. Secondly, we will focus on the proteome maintenance system (UPS and autophagy)
and to the issues related to copper-mediated disturbances of the latter in AD. Finally, we will discuss the
therapeutic potential of copper chelating agents in the treatment of neurodegenerative disorders
Substantial evidence has accumulated over the last decade indicating that diverse age-related neurodegenerative
disorders share a common pathogenic mechanism: the misfolding, aggregation and accumulation
of proteins (termed ‘‘amyloid”) in neuronal tissues. The latest studies suggest that, in principle, any
deficiency in protein homeostasis (proteostasis) may lead to cell dysfunction thus underscoring the protective
key role played by systems regulating the clearance of misfolded or defective proteins in the cell.
On the other hand, an altered metal homeostasis (metallostasis) is thought to be tightly linked to the malfunction
of the ‘‘quality control” machinery of the cell. Metal ions have long been thought to catalyze
amyloid aggregation by initiating protein misfolding. More specifically, redox active metal ions such as
copper have been demonstrated to be majorly involved in a cascade of events resulting in oxidative damage
and neurodegeneration. However, drugs aimed at merely removing excess of such metal ions from
the cell have proven to be unsuccessful thus forcing scientists to amend these traditional views. In particular,
a comprehensive vision of the interplay between metal dyshomeostasis and systems engaged in
proteome maintenance, e.g. proteases, ubiquitin proteasome system (UPS) and autophagy, emerges as a
critical requirement to single out the many culprits of cell dysfunction occurring in aging and in neurodegenerative
pathologies such as Alzheimer’s disease. Here, we will first provide a chemical perspective of
the role of copper in Ab homeostasis, thus giving the necessary outline to the problem of age-related protein
misfolding and altered metallostasis which lead to accumulation processes and consequent decline
of neuron functions. Secondly, we will focus on the proteome maintenance system (UPS and autophagy)
and to the issues related to copper-mediated disturbances of the latter in AD. Finally, we will discuss the
therapeutic potential of copper chelating agents in the treatment of neurodegenerative disorders
The double faced role of copper in Ab homeostasis: A survey on the interrelationship between metal dyshomeostasis, UPS functioning and autophagy in neurodegeneration
The double faced role of copper in Ab homeostasis: A survey on the interrelationship between metal dyshomeostasis, UPS functioning and autophagy in neurodegeneration
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Impact Factor: 9.97
View Export to BibTeX Export to EndNote
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Impact Factor: 9.97
View Export to BibTeX Export to EndNote
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Impact Factor: 0
View Export to BibTeX Export to EndNote
Cirillo G, Bianco MR, Colangelo AM, Cavaliere C, Daniele DL, Zaccaro L, Alberghina L, Papa M
* Reactive astrocytosis-induced perturbation of synaptic homeostasis is restored by nerve growth factor (570 views)
Neurobiology Of Disease (ISSN: 0969-9961), 2011 Mar; 41(3): 630-639.
Impact Factor: 5.403
View Export to BibTeX Export to EndNote
Grasso G, Pietropaolo A, Spoto G, Pappalardo G, Tundo GR, Ciaccio C, Coletta M, Rizzarelli E
* Copper(I) and Copper(II) Inhibit A beta Peptides Proteolysis by Insulin-Degrading Enzyme Differently: Implications for Metallostasis Alteration in Alzheimer's Disease (657 views)
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Impact Factor: 5.925
View Export to BibTeX Export to EndNote
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Impact Factor: 3.354
View Export to BibTeX Export to EndNote
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Impact Factor: 2.266
View Export to BibTeX Export to EndNote
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* The Machinery for Oxidative Protein Folding in Thermophiles (vol 10, pg 157, 2008) (400 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2010 Jan; 12(1): 157-169.
Impact Factor: 8.209
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Calabrese V, Cornelius C, Mancuso C, Pennisi G, Calafato S, Bellia F, Bates TE, Giuffrida Stella AM, Schapira T, Dinkova Kostova AT, Rizzarelli E
* Cellular stress response: a novel target for chemoprevention and nutritional neuroprotection in aging, neurodegenerative disorders and longevity (1536 views)
Neurochemical Research (ISSN: 1573-6903, 0364-3190), 2008 Dec; 33(12): 2444-2471.
Impact Factor: 2.26
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Sciacca MFM, Pappalardo M, Milardi D, Grasso DM, La Rosa C
* Calcium-Activated Membrane Interaction Of The Islet Amyloid Polypeptide: Implications In The Pathogenesis Of Type Ii Diabetes Mellitus (1168 views)
Arch Biochem Biophys, 2008 Sep 15; 65(1-2): 291-298.
Impact Factor: 3.043
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Pedone E, Limauro D, Bartolucci S
* The machinery for oxidative protein folding in thermophiles (482 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2008 Jan; 10(1): 157-169.
Impact Factor: 6.19
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Colao A, Di Somma C, Cuocolo A, Spinelli L, Acampa W, Spiezia S, Rota F, Savanelli MC, Lombardi G
* Does a gender-related effect of growth hormone (GH) replacement exist on cardiovascular risk factors, cardiac morphology, and performance and atherosclerosis? Results of a two-year open, prospective study in young adult men and women with severe GH deficiency (551 views)
J Clin Endocrinol Metab (ISSN: 0021-972x), 2005 Sep; 90(9): 5146-5155.
Impact Factor: 6.02
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Foti D, Chiefari E, Fedele M, Iuliano R, Brunetti L, Paonessa F, Manfioletti G, Barbetti F, Brunetti A, Croce CM, Fusco A, Brunetti A
* Lack of the architectural factor HMGA1 causes insulin resistance and diabetes in humans and mice (491 views)
Nat Med (ISSN: 1078-8956, 0034-7264), 2005 Jul; 11(7): 765-773.
Impact Factor: 28.878
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Maurea S, Lastoria S, Cuocolo A, Celentano L, Salvatore M
The diagnosis of nonfunctioning pheochromocytoma the role of I-123 MIBG imaging (302 views)
Clin Nucl Med (ISSN: 0363-9762, 1536-0229, 1536-0229electronic), 1995 Jan; 20(1): 22-24.
Impact Factor: 0.34
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32 Records (31 excluding Abstracts).
Total impact factor: 175.892 (172.217 excluding Abstracts).
Total 5 year impact factor: 163.963 (163.963 excluding Abstracts).
Total impact factor: 175.892 (172.217 excluding Abstracts).
Total 5 year impact factor: 163.963 (163.963 excluding Abstracts).
353 views. Last view on Thursday 10 October 2024, 9:00:18
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