Summary
The antioxidant enzymes superoxide dismutase, glutathione peroxidase, and catalase were measured in the rete mirabile and gas gland epithelium area of the swim bladder of the toadfish Opsanus tau. When the concentration of enzyme in the swim bladder was compared with the concentration in other organs (kidney, heart, gills) of the same fish, the swim bladder was found to have the highest concentration of superoxide dismutase but relatively low levels of glutathione peroxidase and catalase.
Cytochemical assay for the peroxidatic activity of catalase confirmed that virtually no catalase is present in epithelial cells of the gas gland. A similar assay for peroxidase revealed a cyanide-sensitive peroxidase in the multilamellar bodies of these cells. Most of the catalase and peroxidase in the rete mirabile appears to be confined to the granules of neutrophils and the cytoplasm of erythrocytes. Enzyme activity in the neutrophils is not inhibited by 10-1 M KCN. Cyanide does appear to inhibit the peroxidase activity in erythrocytes but has little effect on catalase in these cells.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Adamson IYR, Bowden JP, Wyatt JP (1970) Oxygen poisoning in mice. Ultrastructural and surfactant studies during exposure and recovery. Arch Pathol 90:463–472
Beers RF, Sizer IW (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 195:133–140
Black VS (1946) Chloride, carbonic anhydrase, and catalase in the tissues of the perch, Percaflavescens. (Mitchill) Rev Can Biol 5:311–318
Breton-Gorius J, Coquin Y, Guichard J (1978) Cytochemical distinction between azurophils and catalase-containing granules in leukocytes. 1. Studies in developing neutrophils and monocytes from patients with myeloperoxidase deficiency: comparison with peroxidase-deficient chicken heterophils. Lab Invest 38:21–31
Cannon MS, Mollenhauer HH, Cannon AM, Eurell TE, Lewis DH (1980) Ultrastructural localization of peroxidase activity in neutrophil leukocytes of letalurus punctatus. Can J Zool 58:1139–1143
Crapo J, Tierney DF (1974) Superoxide dismutase and pulmonary oxygen toxicity. Am J Physiol 226:1401–1407
D'Aoust BG (1969) Hyperbaric oxygen toxicity to fish at pressures present in their swim bladders. Science 163:576–578
Fänge R (1966) Physiology of the swim bladder. Physiol Rev 46:299–322
Fänge R, Wittenberg JB (1958) The swim bladder of the toadfish (Opsanus tauL.) Biol Bull 115:172–179
Feigl F (1958) Spot tests in inorganic analysis. Elsevier Publishing Co., Inc., New York, p 210
Franks L, Bucher JR, Roberts RJ (1978) Oxygen toxicity in neonatal and adult animals of various species. J Appl Physiol 45:699–704
Goldfischer S, Villaverde H, Forschirm R (1966) The demonstration of acid hydrolase, thermostable reduced diphosphopyridine nucleotide tetrazolium reductase and peroxidase activities in human lipofuscin pigment granules. J Histochem Cytochem 14:641–652
Gould VE, Tosco R, Wheelis RF, Gould NS, Kapanci Y (1972) Oxygen pneumonitis in man. Ultrastructural observations on the development of alveolar lesions. Lab Invest 26:499–508
Hall FG (1924) The functions of the swim bladder of fishes. Biol Bull 47:79–127
Herzog V, Fahimi HD (1976) Intracellular distinction between peroxidase and catalase in exocrine cells of rat lacrimal gland: A biochemical and cytochemical study. Histochem 46:273–286
Holmes B, Park BH, Malawista SE, Quie PG, Nelson DL, Good RA (1970) Chronic granulomatous disease in females. A deficiency of leukocyte glutathione peroxidase. N Engl J Med 283:217–221
Hüfner G (1892) Zur physikalischen Chemie der Schwimmblasengase. Arch Anat Physiol, Physiol Abt Lpz 54–80
Jacobs W (1930) Untersuchungen zur Physiologie der Schwimmblase der Fische. I. Über die Gassekretion in der Schwimmblase von Physoklisten. Z Vergleich Physiol 11:565–629
Kaplan HP, Robinson FR, Kapanci Y, Weibel ER (1969) Pathogenesis and reversibility of the pulmonary lesions of oxygen toxicity in monkeys. I. Clinical and light microscopic studies. Lab Invest 20:94–100
Kimball RE, Reddy K, Pierce TH, Schwartz LW, Mustafa MG, Cross CE (1976) Oxygen toxicity: augmentation of antioxidant defense mechanisms in rat lung. Am J Physiol 230:1425–1431
Kistler GS, Caldwell PRB, Weibel ER (1967) Development of fine structural damage to alveolar and capillary lining cells in oxygen-poisoned rat lungs. J Cell Biol 32:605–628
Kuhn W, Kuhn HJ (1961) Multiplikation von Aussalz- und anderen Einzeleffekten für die Bereitung höher Gasdrucke in der Schwimmblase. Z Elektrochem 65:426–439
Kuhn W, Ramel A, Kuhn HJ, Marti E (1963) The filling mechanism of the swimbladder. Generation of high gas pressures through hairpin countercurrent multiplication. Experentia 19:497–552
Little C, O'Brien PJ (1968) An intracellular GSH-peroxidase with a lipid peroxide substrate. Biochem Biophys Res Comm 31:145–150
Litwin JA (1979) Histochemistry and cytochemistry of 3,3′-diaminobenzidine. A review. Folia Histochem Cytochem (Krakow) 17:3–28
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275
Maral J, Puget K, Michelson AM (1977) Comparative study of superoxide dismutase, catalase, and glutathione peroxidase levels in erythrocytes of different animals. Biochem Biophys Res Comm 77:1525–1535
Matkovics B, Novak R, DucHanh H, Szabó L, Varga I, Zalesna G (1977) A comparative study of some more important experimental animal peroxide metabolism enzymes. Comp Biochem Physiol 56B:31–34
Mazeaud F, Maral J, Michelson AM (1979) Distribution of superoxide dismutase and glutathione peroxidase in the carp: erythrocyte manganese SOD. Biochem Biophys Res Comm 86:1161–1168
McCord JM, Fridovich I (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244:6049–6055
Nishimura ET, Whest GM, Yang H-Y (1976) Ultrastructural localization of peroxidatic catalase in human peripheral blood leukocytes. Lab Invest 34:60–68
Paglia DE, Valentine WN (1967) Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70:158–169
Reynolds ES (1963) The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol 17:208–212
Rister M, Baehner RL (1976) The alteration of superoxide dismutase, catalase, glutathione peroxidase, and NAD(P)H cytochrome c reductase in guinea pig polymorphonuclear leukocytes and alveolar macrophages during hyperoxia. J Clin Invest 58:1174–1184
Schaffner F, Feiig P, Trachtenberg E (1967) Structure of rat lung after protracted oxygen breathing. Arch Pathol Lab Med 83:99–107
Sterba G (1967) Descriptions of families and species. In: Freshwater fishes of the world. Studio Vista, LTD. London, pp. 38–39
Tsuchihashi M (1923) Zur Kenntnis der Blutkatalase. Biochem Z 140:63–112
Wittenberg JB, Copeland DE, Haedrich RL, Child JS (1980) The swimbladder of deep-sea fish: The swimbladder wall is a lipid-rich barrier to oxygen diffusion. J Mar Biol Ass U.K. 60:263–276
Yamamoto E, Wittner M, Rosenbaum RM (1970) Resistance and susceptibility to oxygen toxicity by cell types of the blood-gas barrier of the rat lung. Am J Pathol 59:409–435
Author information
Authors and Affiliations
Additional information
Supported by grant No. HL23338 from the National Institutes of Health
Rights and permissions
About this article
Cite this article
Morris, S.M., Albright, J.T. Superoxide dismutase, catalase, and glutathione peroxidase in the swim bladder of the physoclistous fish, Opsanus tau L. Cell Tissue Res. 220, 739–752 (1981). https://doi.org/10.1007/BF00210458
Accepted:
Issue date:
DOI: https://doi.org/10.1007/BF00210458