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Antioxidant defences in rat, pig, guinea pig, and human hearts: comparison with xanthine oxidoreductase activity.
Cardiovasc Res. 1993 Nov; 27(11):2052-7.CR

Abstract

OBJECTIVE

Cardiac injury, related to ischaemia and reperfusion, may be caused by the action of oxygen free radicals. Xanthine oxidoreductase activity may be an important free radical source. During cardiac ischaemia, the native dehydrogenase form may be converted to the oxidase form, which uses molecular oxygen to form superoxide radicals. Superoxide dismutase converts the radicals to H2O2, which is detoxified by catalase and glutathione peroxidase. In view of the large differences in xanthine oxidoreductase in various species, the activity of these antioxidant enzymes was investigated.

METHODS

Normal rodent and porcine as well as explanted human hearts were perfused according to Langendorff. After a 30 minute stabilisation period, hypoxanthine was added to the perfusion buffer to estimate xanthine oxidoreductase. Hearts or biopsies were freeze clamped after 90 minutes. Effluent xanthine and urate were assayed with high performance liquid chromatography; tissue reduced glutathione content and the activity of superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase were determined spectrophotometrically. Apparent xanthine oxidoreductase was calculated as xanthine +2 x urate production.

RESULTS

Xanthine oxidoreductase was (mU.g-1 protein, mean(SEM), n = 5-7): rat, 470(40); guinea pig, 270(41); pig < 1.5; and human, 5.4(1.0). Superoxide dismutase activities were (U.g-1 protein): rat, 13,370(1030); guinea pig, 10,100(1110); pig, 12,800(450); and human, 7400(450). Catalase activity (k < or = 10.g-1 protein) was low in all species studied. Glutathione peroxidase activity was 93(7) U.g-1 protein in rat heart, and 10 x lower in the other species. Glutathione reductase activity was (U.g-1 protein): rat, 15.0(1.6); guinea pig, 10.4(1.3); pig, 16.0(1.5); and human, 26.6(2.0). Tissue reduced glutathione concentrations were (mumol.g-1 protein): rat, 13.5(0.8); guinea pig, 18.5(0.9); pig, 11.1(2.9); and human 17.2(1.7).

CONCLUSIONS

Considerable species differences in xanthine oxidoreductase activity exist, contrasting with the smaller variations in antioxidant enzyme activities. In the species examined catalase activities were very low. Rat hearts are far better protected against H2O2 than the other three species. Xanthine oxidoreductase induced free-radical damage probably plays a minor role in pig and human hearts. Human myocardium seems less protected against superoxide radicals.

Authors+Show Affiliations

Cardiochemical Laboratory, Erasmus University Rotterdam, The Netherlands.No affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8287417

Citation

Janssen, M, et al. "Antioxidant Defences in Rat, Pig, Guinea Pig, and Human Hearts: Comparison With Xanthine Oxidoreductase Activity." Cardiovascular Research, vol. 27, no. 11, 1993, pp. 2052-7.
Janssen M, van der Meer P, de Jong JW. Antioxidant defences in rat, pig, guinea pig, and human hearts: comparison with xanthine oxidoreductase activity. Cardiovasc Res. 1993;27(11):2052-7.
Janssen, M., van der Meer, P., & de Jong, J. W. (1993). Antioxidant defences in rat, pig, guinea pig, and human hearts: comparison with xanthine oxidoreductase activity. Cardiovascular Research, 27(11), 2052-7.
Janssen M, van der Meer P, de Jong JW. Antioxidant Defences in Rat, Pig, Guinea Pig, and Human Hearts: Comparison With Xanthine Oxidoreductase Activity. Cardiovasc Res. 1993;27(11):2052-7. PubMed PMID: 8287417.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Antioxidant defences in rat, pig, guinea pig, and human hearts: comparison with xanthine oxidoreductase activity. AU - Janssen,M, AU - van der Meer,P, AU - de Jong,J W, PY - 1993/11/1/pubmed PY - 1993/11/1/medline PY - 1993/11/1/entrez SP - 2052 EP - 7 JF - Cardiovascular research JO - Cardiovasc Res VL - 27 IS - 11 N2 - OBJECTIVE: Cardiac injury, related to ischaemia and reperfusion, may be caused by the action of oxygen free radicals. Xanthine oxidoreductase activity may be an important free radical source. During cardiac ischaemia, the native dehydrogenase form may be converted to the oxidase form, which uses molecular oxygen to form superoxide radicals. Superoxide dismutase converts the radicals to H2O2, which is detoxified by catalase and glutathione peroxidase. In view of the large differences in xanthine oxidoreductase in various species, the activity of these antioxidant enzymes was investigated. METHODS: Normal rodent and porcine as well as explanted human hearts were perfused according to Langendorff. After a 30 minute stabilisation period, hypoxanthine was added to the perfusion buffer to estimate xanthine oxidoreductase. Hearts or biopsies were freeze clamped after 90 minutes. Effluent xanthine and urate were assayed with high performance liquid chromatography; tissue reduced glutathione content and the activity of superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase were determined spectrophotometrically. Apparent xanthine oxidoreductase was calculated as xanthine +2 x urate production. RESULTS: Xanthine oxidoreductase was (mU.g-1 protein, mean(SEM), n = 5-7): rat, 470(40); guinea pig, 270(41); pig < 1.5; and human, 5.4(1.0). Superoxide dismutase activities were (U.g-1 protein): rat, 13,370(1030); guinea pig, 10,100(1110); pig, 12,800(450); and human, 7400(450). Catalase activity (k < or = 10.g-1 protein) was low in all species studied. Glutathione peroxidase activity was 93(7) U.g-1 protein in rat heart, and 10 x lower in the other species. Glutathione reductase activity was (U.g-1 protein): rat, 15.0(1.6); guinea pig, 10.4(1.3); pig, 16.0(1.5); and human, 26.6(2.0). Tissue reduced glutathione concentrations were (mumol.g-1 protein): rat, 13.5(0.8); guinea pig, 18.5(0.9); pig, 11.1(2.9); and human 17.2(1.7). CONCLUSIONS: Considerable species differences in xanthine oxidoreductase activity exist, contrasting with the smaller variations in antioxidant enzyme activities. In the species examined catalase activities were very low. Rat hearts are far better protected against H2O2 than the other three species. Xanthine oxidoreductase induced free-radical damage probably plays a minor role in pig and human hearts. Human myocardium seems less protected against superoxide radicals. SN - 0008-6363 UR - https://www.unboundmedicine.com/medline/citation/8287417/Antioxidant_defences_in_rat_pig_guinea_pig_and_human_hearts:_comparison_with_xanthine_oxidoreductase_activity_ L2 - https://academic.oup.com/cardiovascres/article-lookup/doi/10.1093/cvr/27.11.2052 DB - PRIME DP - Unbound Medicine ER -