Oxidative stress in skin fibroblasts cultures of patients with Huntington's disease

• Published in: Neurochemical research Vol. 31; no. 9; pp. 1103 - 1109
• Main Authors: del Hoyo, Pilar, García-Redondo, Alberto, de Bustos, Fernando, Molina, José Antonio, Sayed, Youssef, Alonso-Navarro, Hortensia, Caballero, Luis, Arenas, Joaquín, Jiménez-Jiménez, Félix Javier
• Format: Journal Article
• Language: English
• Published: United States Springer Nature B.V 01.09.2006
• Subjects: Adult; Animals; Catalase; Catalase - metabolism; Cells, Cultured; Chains; Citrate synthase; Coenzyme Q10; Coenzymes; Copper; Electron transport; Electron Transport - physiology; Enzymatic activity; Enzymes; Female; Fibroblasts; Fibroblasts - cytology; Fibroblasts - metabolism; Glutathione; Glutathione Peroxidase - metabolism; Humans; Huntington Disease - metabolism; Huntington's disease; Isoenzymes - metabolism; Male; Manganese; Middle Aged; Mitochondria; Mitochondria - enzymology; Multienzyme Complexes; Neostriatum; Neurodegeneration; Oxidative Stress; Pathogenesis; Peroxidase; Polyglutamine; Proteins; Skin - cytology; Superoxide dismutase; Superoxide Dismutase - metabolism; Trinucleotide repeats; Ubiquinone - analogs & derivatives; Ubiquinone - metabolism; Zinc
• ISSN: 0364-3190; 1573-6903
• DOI: 10.1007/s11064-006-9110-2

Oxidative stress and mitochondrial dysfunction should play a role in the neurodegeneration in Huntington's disease (HD). The most consistent finding is decreased activity of the mitochondrial complexes II/III and IV of the respiratory chain in the striatum. We assessed enzymatic activities of respiratory chain enzymes and other enzymes involved in oxidative processes in skin fibroblasts cultures of patients with HD. We studied respiratory chain enzyme activities, activities of total, Cu/Zn- and Mn-superoxide-dismutase, glutathione-peroxidase (GPx) and catalase, and coenzyme Q(10) (CoQ(10)) levels in skin fibroblasts cultures from 13 HD patients and 13 age- and sex-matched healthy controls. When compared with controls, HD patients showed significantly lower specific activities for catalase corrected by protein concentrations (P < 0.01). Oxidized, reduced and total CoQ(10) levels (both corrected by citrate synthase (CS) and protein concentrations), and activities of total, Cu/Zn- and Mn-superoxide-dismutase, and gluthatione-peroxidase, did not differ significantly between HD-patients and control groups. Values for enzyme activities in the HD group did not correlate with age at onset and of the disease and with the CAG triplet repeats. The primary finding of this study was the decreased activity of catalase in HD patients, suggesting a possible contribution of catalase, but not of other enzymes related with oxidative stress, to the pathogenesis of this disease.