Metallostasis And Amyloid Beta-Degrading Enzymes
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Metallostasis And Amyloid Beta-Degrading Enzymes (1035 views)

Grasso G, Giuffrida ML, Rizzarelli E

Metallomics (ISSN: 1756-5901, 1756-591x, 1756-591xelectronic), 2012 Sep; 4(9): 937-949.

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Paper type: Journal Article, Research Support, Non-U. S. Gov'T, Review,

Impact factor: 4.099, 5-year impact factor: 4.333

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84865503795&partnerID=40&md5=cc8f3eca5833b59b74a04d036b3c33e8

Keywords: Alzheimer, S Disease, Amyloid Betas, Amyloid Precursor Proteins, Degrading Enzymes, Enzymes Activity, Metal Ion Homeostasis, Metalloproteases, Proteolytic Cleavage, Proteolytic Enzyme, Senile Plaques, Signalling Cascades, Steady-State Level, Degradation, Glycoproteins, Physiology, Peptides, Amyloid Beta Protein, Clioquinol, Copper, Iron, Matrix Metalloproteinase, Stress Activated Protein Kinase, Synaptophysin, Alzheimer Disease, Concentration (parameters), Dna Damage, Human, Nonhuman, Priority Journal, Protein Degradation, Review, Amino Acid Sequence, Amyloid Beta-Peptides, Animals, Molecular Sequence Data, Proteolysis, Signal Transduction, Alzheimer Disease Metabolism Pathology, Amyloid Beta-Peptides Chemistry Metabolism, Metalloproteases Metabolism, Metals Metabolism,

Affiliations:
*** IBB - CNR ***

Dipartimento di Scienze Chimiche, Chemistry Department, Università di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Istituto Biostrutture e Bioimmagini, CNR, Viale A. Doria 6, Catania, Italy


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Metallostasis And Amyloid Beta-Degrading Enzymes

Amyloid-Beta (Aβ) is a major constituent of senile plaques and one of the principle hallmarks of Alzheimer's disease (AD). The peptide is produced by proteolytic cleavage of the larger amyloid precursor protein (APP). Increased production and aggregation of the peptide are associated with pathology. Emerging evidence suggests that the steady-state levels of Aβ are determined by the balance between its production and degradation. For this reason, the tuning of the activity of enzymes that degrade Aβ may be a promising approach in the development of novel therapeutics aimed at reducing Aβ concentration by enhancing its removal. A great part of Aβ degrading enzymes are known to be metalloproteases. In the last decade increasing evidence supported the idea that metal ion homeostasis is affected in several regions of AD brain and metals play an important role in tuning enzyme activity. There are three main different pathways by which metal ions can affect the proteolytic enzymes responsible for Aβ peptides degradation, as metal ions can: (i) form complexes with Aβ peptides that are not easily degraded; (ii) directly bind to degradative enzymes; (iii) produce signalling cascades that alter enzymes activity involved in Aβ catabolism. In the current literature the three points mentioned above are very often puzzled, resulting in a quite fragmentary scenario. The aim of this work is to find a link between metal ion homeostasis and Aβ degradation by separating and analysing the three different pathways proposed. © The 2012 Royal Society of Chemistry.
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Bellia F, Pietropaolo A,  Grasso G
* Formation of insulin fragments by insulin-degrading enzyme: The role of zinc(II) and cystine bridges (461 views)
J Mass Spectrom (ISSN: 1076-5174, 1096-9888), 2013; 48(2): 135-140.
Impact Factor: 2.709
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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 (576 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Feb 25; 17(9): 2752-2762.
Impact Factor: 5.925
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Grasso G, Rizzarelli E, Spoto G
* The proteolytic activity of insulin-degrading enzyme: a mass spectrometry study (520 views)
J Mass Spectrom (ISSN: 1096-9888, 1076-5174), 2009 May; 44(5): 735-741.
Impact Factor: 3.411
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3 Records (3 excluding Abstracts).
Total impact factor: 12.045 (12.045 excluding Abstracts).
Total 5 year impact factor: 12.036 (12.036 excluding Abstracts).

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