Superoxide dismutase and catalase blood levels in patients with malignant diseases

Casado, Ángela; Torre, R. de la; López‐Fernández, M.E.; Carrascosa, Diana; Casado, M C; Ramirez, Magdalena

doi:10.1016/0304-3835(95)03808-a

Cited by 33 publications

(25 citation statements)

References 7 publications

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“…In humans, SOD activity decreases with age (24). In this study, we did not find any evidence for the SOD1 protein reduction as cells approached senescence (Fig.…”

Section: Sod1 Rnai Induces Premature Senescencecontrasting

confidence: 55%

Superoxide Dismutase 1 Knock-down Induces Senescence in Human Fibroblasts

Blander

Oliveira

Conboy

et al. 2003

Journal of Biological Chemistry

154

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Reactive oxygen species (ROS) such as superoxide radicals are responsible for the pathogenesis of various human diseases. ROS are generated during normal metabolic process in all of the oxygen-utilizing organisms. The copper-zinc-containing SOD (SOD1) acts as a major defense against ROS by detoxifying the superoxide anion. In model organisms, SOD1 has been shown to play a role in the aging process. However, the exact role of the SOD1 protein in the human aging process remains to be resolved. We show that SOD1 RNA interference (RNAi) induces senescence in normal human fibroblasts. This premature senescence depends on p53 induction. In contrast, in human fibroblastic cells with inactivated p53, the SOD1 RNAi is without effect. Surprisingly, in cancer cells (HeLa), the SOD1 RNAi induces cell death rather then senescence. Together, these findings support the notion that in normal human cells the SOD1 protein may play a role in the regulation of cellular lifespan by p53 and may also regulate the death signals in cancer cells. ROS1 are generated by normal metabolic processes in all of the oxygen-utilizing organisms. It is estimated that around 1% of the total oxygen consumed in the mitochondria becomes the superoxide anion (1). Damage induced by ROS includes DNA mutation, protein oxidation, and lipid peroxidation. ROS may contribute to the development of various diseases, such as cancer, diabetes, atherosclerosis, inflammation, and premature aging (2, 3).The superoxide dismutases (SODs) constitute a family of antioxidant enzymes that catalyzes the conversion of superoxide anions to oxygen and hydrogen peroxide (for recent review on SODs, see Ref. 4). They include the manganese-containing SOD (SOD2) in the mitochondria (5) and the copper-zinc-containing SOD (SOD1) in the cytoplasm (5) with a small fraction in the mitochondria intermembrane space (6). Ͼ90 different mutations in the SOD1 gene have been found to associate with amyotrophic lateral sclerosis, a disease that causes the degradation of motor neurons (7).The free radical theory of aging states that ROS generation during metabolism can cause damage to cellular constituents (8). During the life of a cell or an organism, SODs and catalase detoxify ROS. However this process is not perfect and ROS species can cause cumulative damage, which causes the physiological decline characteristic of aging (for review, see Ref. 9). In yeast survival, the stationary phase appears to be limited by ROS because deletion of either SOD1 or SOD2 shortens survival time (10). In Drosophila, overexpression of the human SOD1 extends the fly life span by 40% over controls (11).After a finite number of divisions, primary human cells in culture enter into a state of replicative senescence in which they are growth-arrested and resistant to mitogenic stimulation. Senescence is considered a mechanism to suppress tumorigenesis because it inhibits cell proliferation (12). Oxidants appear to be important in the development of the senescent phenotype. Cells grown in low oxygen tension exhibit a pr...

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“…In humans, SOD activity decreases with age (24). In this study, we did not find any evidence for the SOD1 protein reduction as cells approached senescence (Fig.…”

Section: Sod1 Rnai Induces Premature Senescencecontrasting

confidence: 55%

Superoxide Dismutase 1 Knock-down Induces Senescence in Human Fibroblasts

Blander

Oliveira

Conboy

et al. 2003

Journal of Biological Chemistry

154

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“…It has been established that SOD activity is inhibited in cancer (JiauJian & Larry, 1977;Oberley & Oberley, 1997). The lowering of both SOD and CAT activities as a result of tumor growth was reported (Casado et al, 1995;Marklund et al, 1982). The decrease in hepatic SOD and CAT activities was also reported in EAC bearing mice (Gupta et al, 2004b), and the similar findings were observed in our present investigation in EAC control mice.…”

Section: Discussionmentioning

confidence: 71%

“…Neoplastic growth has been found to co-exist with an impairment in the endogenous antioxidant status (Oberley, 2002). Low activity of endogenous antioxidant system was found in cancer patients (Balasubramaniyan et al, 1994;Casado et al, 1995) and in experimental carcinoma cell lines (Yellin et al, 1994;Sharma et al, 1993). Several evidences suggest that EAC induces oxidative stress in mice (Baumgartner et al, 1978;Gupta et al, 2004a,b) Oxidative stress is caused by a relative overproduction of oxidative free radicals or reactive oxygen species (ROS).…”

Section: Discussionmentioning

confidence: 99%

Antitumor efficacy and amelioration of oxidative stress byTrichosanthes dioicaroot against Ehrlich ascites carcinoma in mice

Bhattacharya¹,

Prasanna

Majumdar

et al. 2011

Pharmaceutical Biology

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“…There were some reports of the relationship investigated between cancer and the following serum constituents: insulin-like growth factor (IGF)-I, IGF-II, [3][4][5] insulinlike growth factor-binding protein 3 (IGFBP-3), 6 transforming growth factor (TGF)-1, 7,8 soluble Fas (sFas), 9 and superoxide dismutase (SOD) activity. [10][11][12][13] Although reports indicate that serum levels of constituents such as proteins and minerals are stable in long-term refrigerated storage, [14][15][16][17] there have been no reports indicating whether serum levels of cytokines, such as IGFs, TGFand sFas, remain stable after approximately 10 years of storage at -80 .…”

mentioning

confidence: 99%

Stability of Frozen Serum Levels of Insulin-like Growth Factor-I, Insulin-like Growth Factor-II, Insulin-like Growth Factor Binding Protein-3, Transforming Growth Factorβ, Soluble Fas, and Superoxide Dismutase Activity for the JACC Study

Ito

Nakachi

Imai

et al. 2005

Journal of Epidemiology

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BACKGROUND: Subjects of the Japan Collaborate Cohort Study (JACC Study) gave peripheral blood samples collected between 1988 and 1990. We conducted to investigate whether levels of serum components measured after 9 years of frozen storage are stable or not. METHODS: To assess the degradation of frozen serum components in the JACC Study, we compared levels of various components (IGF-I, IGF-II, IGFBP-3, TGF- β 1, sFas, and total SOD activity) between fresh and stored sera collected from other inhabitants. Serum levels of constituents were measured by immunoradiometric assay (IGF-I, IGF-II and IGFBP-3), quantitative enzyme immunoassay (TGF- β 1), enzyme-linked immuno-adsorbent assay (sFas), and an improved nitrite method (SOD activity). RESULTS: The coefficients of variation for intra- and inter-assay precisions of the measurements were less than 9%. Levels of IGF-I, IGF-II, IGFBP-3, TGF- β 1 and sFas in sera after storage for 9 years at -80°C were similar to those of fresh sera newly collected from inhabitants. The distributions of serum IGF-I, IGF-II, IGFBP-3, TGF- β 1, sFas and SOD activity for specimens collected from different individuals tended to be similar to those of serum levels for frozen specimens collected from different individuals and stored for 9 years. CONCLUSIONS: There was no statistically significant difference in distribution of measured values of IGF-I, IGF-II, IGFBP-3, TGF- β 1, and sFas between newly collected sera and frozen specimens stored for 9 years. Thus, measurements of these serum constituents of specimens stored for the JACC Study can be reliably used in nested case-control study.

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Superoxide dismutase and catalase blood levels in patients with malignant diseases

Cited by 33 publications

References 7 publications

Superoxide Dismutase 1 Knock-down Induces Senescence in Human Fibroblasts

Superoxide Dismutase 1 Knock-down Induces Senescence in Human Fibroblasts

Antitumor efficacy and amelioration of oxidative stress byTrichosanthes dioicaroot against Ehrlich ascites carcinoma in mice

Stability of Frozen Serum Levels of Insulin-like Growth Factor-I, Insulin-like Growth Factor-II, Insulin-like Growth Factor Binding Protein-3, Transforming Growth Factorβ, Soluble Fas, and Superoxide Dismutase Activity for the JACC Study

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