Abstract
The pseudobranch in rainbow trout was investigated in order to clarify its metabolic and physiological function. Contents of lactate, glycogen, and glycerides and activities of carbonic anhydrase (CA), lactate dehydrogenase (LDH), and 3-hydroxy-acyl CoA dehydrogenase (HAD) were measured and compared with those in the gills and liver. Contents of lactate and glycerides, and activities of CA and HAD were higher in the pseudobranch than in the gills and liver. The results show that the pseudobranch is well equipped with enzymes (HAD and CA) suggested to be coupled to fatty acids breakdown and synthesis respectively. Lactic acid, possibly formed from glycogen and the glycerol component in glycerides, may be involved in the increase in blood P0 2 (Root effect) that is necessary to meet the oxygen needs of the eye. Pseudobranch carbonic anhydrase is probably involved in this process.
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References cited
Bass, A., Bridzka, D., Eyer, P., Hofer, S. and Pette, D. 1969. Metabolic differentiation of distinct muscle types at the level of enzymatic organization. Eur. J. Biochem. 10: 198–206.
Bradford, M.M. 1976. A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248–254.
Broussonet, P.M.A. 1785. Mémoire pour servir à l'histoire de la respiration des Poissons. Mem. Acad. R. Sci. Paris: 174–196.
Dimberg, K. and Höglund, L.B. 1987. Carbonic anhydrase activity in the blood and the gills of rainbow trout during longterm hypercapnia in hard, bicarbonate-rich freshwater. J. Comp. Physiol. B. 157: 405–412.
Dimberg, K. 1988. Inhibition of carbonic anhydrase in vivo in the freshwater-adapted rainbow trout: differential effects of acetazolamide and metazolamide on blood CO2 levels. Comp. Biochem. Physiol. 91A: 253–258.
Dimberg, K. 1994. The carbonic anhydrase inhibitor in trout plasma: purification and its effect on carbonic anhydrase activity and the Root effect. Fish Physiol. Biochem. 12: 381–386.
Hansen, P. and Magid, E. 1966. Studies on a method of measuring carbonic anhydrase activity. Scand. J. Clin. Lab. Invest. 18: 21–32.
Herbert, J.D. and Coulson, R.A. 1983. A role for carbonic anhydrase in de novo fatty acid synthesis in liver. Ann. N. Y. Acad. Sci. 429: 525–527.
Laurent, P., Dunel-Erb, S. and Barets, A. 1969. Localisation histochimique de l'anhydrase carbonique au niveau des chemorécepteurs artériels des Mammifères, des Batraciens et des Poissons. Histochemie 17: 99–107.
Laurent, P. and Dunel-Erb, S. 1984. The pseudobranch: morphology and function. In Fish Physiology. Vol. XB, pp. 285–323. Edited by W.S. Hoar and D.J. Randall. Academic Press, New York.
Maetz, J. 1956. Le role biologique de l'anhydrase carbonique chez quelques Téléostéens. Bull. Biol. Fr. Belg. 40: 1–129.
Norton, W.N., Mattie, D.R. and Kearns, C.L. 1985. The cytopathologic effects of specific aromatic hydrocarbons. Am. J. Pathol. 118: 387–397.
Pelster, B. and Scheid, P. 1991. Activities of enzymes for glucose catabolism in the swimbladder of the European eel Anguilla anguilla. J. Exp. Biol. 156: 207–213.
Pelster, B. and Scheid, P. 1992. Countercurrent concentration and gas secretion in the fish swim bladder. Physiol. Zool. 65: 1–16.
Pinter, J.K., Hayashi, J.A. and Watson, J.A. 1967. Enzymatic assay of glycerol, dihydroxyacetone and glyceraldehyde. Arch. Biochem. Biophys. 121: 404.
Somdal, O. and Schram, T.A. 1992. Ectoparasites on Northeast Atlantic mackerel (Scomber scombrus L.) from western and North Sea stocks. Sarsia. 77: 19–31.
Walsh, J.P. and Milligan, C.L. 1993. Roles of buffering capacity and pentose phosphate pathway in the gas gland of the gulf toadfish Opsanus beta. J. Exp. Biol. 176: 311–316.
Wittenberg, J.B. and Haedrich, R.L. 1974. The choroid rete mirabile of the fish eye. II. Distribution and relation to the pseudobranch and to the swimbladder rete mirabile. Biol. Bull. 146: 137–156.
Wolf, K. 1963. Physiological salines for freshwater teleosts. Progr. Fish.-Cult. 25: 135–140.
Wright, P.A., Perry, S.F. and Moon, T.W. 1989. Regulation of hepatic gluconeogenesis and glycogenolysis by catecholamines in rainbow trout during environmental hypoxia. J. Exp. Biol. 47: 169–188.
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Dimberg, K. Investigation of the pseudobranch organ in rainbow trout (Oncorhyncus mykiss): endogenous substrates and activities of carbonic anhydrase, lactate dehydrogenase, and 3-hydroxy-acyl CoA dehydrogenase. Fish Physiol Biochem 14, 323–327 (1995). http://doi.org/10.1007/BF00004070
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DOI: http://doi.org/10.1007/BF00004070