Using Microwave-Assisted Metal-Catalyzed Oxidation Reactions and Mass Spectrometry To Increase the Rate at Which the Copper-Binding Sites of a Protein Are Determined

2005 ◽  
Vol 77 (14) ◽  
pp. 4649-4653 ◽  
Author(s):  
Juma D. Bridgewater ◽  
Richard W. Vachet
Metallomics ◽  
2016 ◽  
Vol 8 (10) ◽  
pp. 1081-1089 ◽  
Author(s):  
Clémence Cheignon ◽  
Peter Faller ◽  
Denis Testemale ◽  
Christelle Hureau ◽  
Fabrice Collin

Aβ oxidation due to HO˙ production by Cu–Aβ/ascorbate changes copper coordination and leads to the self-enhancement of HO˙ production and release.


1997 ◽  
Vol 185 (1) ◽  
pp. 71-80 ◽  
Author(s):  
Livia Casciola-Rosen ◽  
Fredrick Wigley ◽  
Antony Rosen

The observation that revelation of immunocryptic epitopes in self antigens may initiate the autoimmune response has prompted the search for processes which induce novel fragmentation of autoantigens as potential initiators of autoimmunity. The reversible ischemia reperfusion which characterizes scleroderma has focused attention on reactive oxygen species as molecules which might induce autoantigen fragmentation. We demonstrate that several of the autoantigens targeted in diffuse scleroderma are uniquely susceptible to cleavage by reactive oxygen species, in a metal-dependent manner. Multiple features of the fragmentation reaction and its inhibition indicate that these autoantigens possess metal-binding sites, which focus metal-catalyzed oxidation reactions (and consequent fragmentation) to specific regions of the antigens. These data suggest that the autoantibody response in scleroderma is the immune marker of unique protein fragmentation, induced by ischemia reperfusion in the presence of appropriate metals, and focus attention on abnormal metal status as a potential pathogenic principle in this disease.


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