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Factor analysis of the activities of superoxide dismutase, catalase and glutathione peroxidase in normal tissues and neoplastic cell lines.
Free Radic Res Commun. 1987; 4(1):1-13.FR

Abstract

Exploratory factor analysis of reported specific activities of the antioxidant enzymes superoxide dismutase, catalase and glutathione peroxidase in normal human tissues, normal mouse tissues, vertebrate red blood cells and neoplastic human cell lines shows that the activities of copper-zinc superoxide dismutase, catalase and glutathione peroxidase in normal tissues are influenced by a single factor. Catalase activity has the highest loading and correlation with this factor, suggesting a catalase- or hydrogen peroxide-related influence. The activity of manganese superoxide dismutase is influenced by a separate factor. The activities of copper-zinc and manganese superoxide dismutases in normal tissues therefore appear to be dichotomously regulated. The activities of superoxide dismutase and glutathione peroxidase in vertebrate red blood cells are influenced by a single factor. The activity of catalase is influenced by a separate factor. The roles of glutathione peroxidase and catalase in hydrogen peroxide catabolism in red blood cells in fact differ. In neoplastic human cell lines, two bipolar factor factors appear to influence the activities of catalase and manganese superoxide dismutase, and glutathione peroxidase and copper-zinc superoxide dismutase, respectively. The factors are, however, mainly catalase and glutathione peroxidase activity factors as the loadings and correlations of manganese superoxide dismutase on the one hand and copper-zinc superoxide dismutase on the other, with the respective factors, are relatively small. Potentially low superoxide production and intrinsically low peroxidizability of tumour cell membranes underlie the peculiar variation of antioxidant enzyme activities in tumour cells. Factor analysis is proposed as a heuristic data reduction and hypothesis-creating technique for the variation of antioxidant and other functionally-linked enzyme activities in normal and pathological cells and tissues.

Authors+Show Affiliations

Biotechnology Centre, Cranfield Institute of Technology, Bedford, England.No affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

3506891

Citation

Bannister, W H., and J V. Bannister. "Factor Analysis of the Activities of Superoxide Dismutase, Catalase and Glutathione Peroxidase in Normal Tissues and Neoplastic Cell Lines." Free Radical Research Communications, vol. 4, no. 1, 1987, pp. 1-13.
Bannister WH, Bannister JV. Factor analysis of the activities of superoxide dismutase, catalase and glutathione peroxidase in normal tissues and neoplastic cell lines. Free Radic Res Commun. 1987;4(1):1-13.
Bannister, W. H., & Bannister, J. V. (1987). Factor analysis of the activities of superoxide dismutase, catalase and glutathione peroxidase in normal tissues and neoplastic cell lines. Free Radical Research Communications, 4(1), 1-13.
Bannister WH, Bannister JV. Factor Analysis of the Activities of Superoxide Dismutase, Catalase and Glutathione Peroxidase in Normal Tissues and Neoplastic Cell Lines. Free Radic Res Commun. 1987;4(1):1-13. PubMed PMID: 3506891.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Factor analysis of the activities of superoxide dismutase, catalase and glutathione peroxidase in normal tissues and neoplastic cell lines. AU - Bannister,W H, AU - Bannister,J V, PY - 1987/1/1/pubmed PY - 1987/1/1/medline PY - 1987/1/1/entrez SP - 1 EP - 13 JF - Free radical research communications JO - Free Radic Res Commun VL - 4 IS - 1 N2 - Exploratory factor analysis of reported specific activities of the antioxidant enzymes superoxide dismutase, catalase and glutathione peroxidase in normal human tissues, normal mouse tissues, vertebrate red blood cells and neoplastic human cell lines shows that the activities of copper-zinc superoxide dismutase, catalase and glutathione peroxidase in normal tissues are influenced by a single factor. Catalase activity has the highest loading and correlation with this factor, suggesting a catalase- or hydrogen peroxide-related influence. The activity of manganese superoxide dismutase is influenced by a separate factor. The activities of copper-zinc and manganese superoxide dismutases in normal tissues therefore appear to be dichotomously regulated. The activities of superoxide dismutase and glutathione peroxidase in vertebrate red blood cells are influenced by a single factor. The activity of catalase is influenced by a separate factor. The roles of glutathione peroxidase and catalase in hydrogen peroxide catabolism in red blood cells in fact differ. In neoplastic human cell lines, two bipolar factor factors appear to influence the activities of catalase and manganese superoxide dismutase, and glutathione peroxidase and copper-zinc superoxide dismutase, respectively. The factors are, however, mainly catalase and glutathione peroxidase activity factors as the loadings and correlations of manganese superoxide dismutase on the one hand and copper-zinc superoxide dismutase on the other, with the respective factors, are relatively small. Potentially low superoxide production and intrinsically low peroxidizability of tumour cell membranes underlie the peculiar variation of antioxidant enzyme activities in tumour cells. Factor analysis is proposed as a heuristic data reduction and hypothesis-creating technique for the variation of antioxidant and other functionally-linked enzyme activities in normal and pathological cells and tissues. SN - 8755-0199 UR - https://www.unboundmedicine.com/medline/citation/3506891/Factor_analysis_of_the_activities_of_superoxide_dismutase_catalase_and_glutathione_peroxidase_in_normal_tissues_and_neoplastic_cell_lines_ DB - PRIME DP - Unbound Medicine ER -