Skip to main content
Log in

Enzyme activity levels associated with the production of glycerol as an antifreeze in liver of rainbow smelt (Osmerus mordax)

  • Published:
Fish Physiology and Biochemistry Aims and scope Submit manuscript

Abstract

Rainbow smelt (Osmerus mordax) tolerate temperatures close to the freezing point of sea water, in part, through the use of glycerol as an antifreeze. Potential mechanisms for glycerol production by liver were assessed by comparing activities of key enzym es of carbohydrate and amino acid metabolism in rainbow smelt to those in Atlantic tomcod (Microgadus tomcod) and smooth flounder (Liopsetta putmani). The latter two species inhabit the same environment but do not maintain high levels of blood glycerol. The enzyme profile of liver from rainbow smelt is substantially different from those of the other species and is poised for glycerol production. With respect to carbohydrate metabolism, glycerol-3-phosphate dehydrogenase activity in rainbow smelt liver was 156 µmoles min-1 g-1, a level which was 28 and 12-fold higher than activities in tomcod and flounder liver, respectively. Glycerol-3-phosphatase activity in smelt liver was 1.95 µmol min-1 g-1. This activity was 2.7 and 5.4-fold higher than those in tomcod and flounder liver, respectively. As such, the production of glycerol appears to be dependent upon the concerted action of glycerol-3-phosphate dehydrogenase and glycerol-3-phosphatase. The enzyme profile also suggests that amino acids are a potential source of carbon for glycerol. Aspartate aminotransferase activity in rainbow smelt was 7 to 14-fold higher in comparison to tomcod and flounder liver, respectively. Activities of alanine aminotransferase and glutamate dehydrogenase in liver were between 2 and 3-fold higher in rainbow smelt than in the other two species. Finally, it is shown that in vitro preparations of smelt liver sections produce glycerol at 0°C lending support to the concept that liver is a site of glycerol synthesis in vivo.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References cited

  • Chamberlain, M.E., Glemet H.C. and Ballantyne, J.S. 1991. Glutamine metabolism in a holostean (Amia calva) and teleost fish (Salvelinus namaycush). Am. J. Physiol. 260 (Regulatory Integrative Comp. Physiol. 29): R159–R166.

    Google Scholar 

  • Davies, P.L., Hew, C.L. and Fletcher, G.L. 1988. Fish antifreeze proteins: physiology and evolutionary biology. Can. J. Zool. 66: 2611–2617.

    Google Scholar 

  • Duman, J.G. and DeVries, A.L. 1975. The role of macro-molecular antifreezes in cold water fishes. Comp. Biochem. Physiol. 52A: 193–199.

    Google Scholar 

  • Eastman, J.T., Boyd, R.B. and DeVries, A.L. 1987. Renal corpuscle development in boreal fishes with and without antifreezes. Fish Physiol. Biochem. 4: 89–100.

    Google Scholar 

  • Ewart, K.V. and Fletcher, G.L. 1990. Isolation and characterization of antifreeze proteins from smelt (Osmerus mordax) and Atlantic herring (Clupea harengus harengus). Can. J. Zool. 68: 1652–1658.

    Google Scholar 

  • Fletcher, G.L., Hew, C.L. and Joshi, S.D. 1982. Isolation and characterization of the antifreeze glycoproteins from the frostfish Microgadus tomcod. Can. J. Zool. 60: 348–355.

    Google Scholar 

  • French, C.J., Mommsen, T.P. and Hochachka, P.W. 1981. Amino acid utilization in isolated hepatocytes from rainbow trout. Eur. J. Biochem. 113: 311–317.

    Google Scholar 

  • Joanisse, D.R., and K.B. Storey 1994. Enzyme activity profiles in an overwintering population of freeze-tolerant larvae of the gall fly, Eurosta solidaginis. J. Comp. Physiol. B 164: 247–255.

    Google Scholar 

  • Moon, T.W. and Mommsen, T.P. 1987. Enzymes of intermediary metabolism in tissues of the little skate, Raja erinacea. J. Exp. Zool. 244: 9–15.

    Google Scholar 

  • Moon, T.W., Walsh, P.J. and Mommsen, T.P. 1985. Fish hepatocytes: a model metabolic system. Can. J. Fish. Aquat. Sci. 42: 1772–1782.

    Google Scholar 

  • O'Grady, S.M., Schrag, J.D., Raymond, J.A. and DeVries, A.L. 1982. Comparison of antifreeze glycoprotein from Arctic and Antarctic fishes. J. Exp. Zool. 224: 177–185.

    Google Scholar 

  • Opie, L.H. and Newsholme, E.A. 1967. The activities of fructose 1,6-diphosphatase, phosphofructokinase and phosphoenolpyruvate carboxykinase in white muscle and red muscle. Biochem. J. 103: 391–399.

    Google Scholar 

  • Pereira, C., Vijayan, M.M. and Moon, T.W. 1995. In vitro hepatocyte metabolism of alanine and glucose and the response to insulin in fed and fasted rainbow trout. J. Exp. Zool. 271: 425–431.

    Google Scholar 

  • Raymond, J.A. 1992. Glycerol is a colligative antifreeze in some northern fishes. J. Exp. Zool. 262: 347–352.

    Google Scholar 

  • Raymond, J.A. 1993. Glycerol and water balance in a near-isosmotic teleost, winter-acclimatized rainbow smelt. Can. J. Zool. 71: 1849–1854.

    Google Scholar 

  • Raymond, J.A. 1994. Seasonal variations of trimethylamine oxide and urea in the blood of a cold-adapted marine teleost, the rainbow smelt. Fish Physiol. Biochem. 13: 13–22.

    Google Scholar 

  • Raymond, J.A. 1995. Glycerol synthesis in the rainbow smelt Osmerus mordax. J. Exp. Biol. 198: 2569–2573.

    Google Scholar 

  • Raymond, J.A. and Driedzic, W.R. 1997. Amino acids are a source of glycerol in cold-acclimated rainbow smelt. Comp. Biochem. Physiol. 118B: (In press).

  • Raymond, J.A., Hattori, H. and Tsumura, K. 1966. Metabolic responses of glycerol-producing osmerid fishes to cold temperature. Fish. Sci. 62: 257–260.

    Google Scholar 

  • Singer, T.D. and Ballantyne, J.S. 1989. Absence of extrahepatic lipid oxidation in a freshwater elasmobranch, the dwarf stingray Potamotrygon magdalenae: evidence from enzyme activities. J. Exp. Zool. 251: 355–360.

    Google Scholar 

  • Sephton, D., Bailey, J. and Driedzic, W.R. 1990. Impact of acute temperature transition on enzyme activity levels, oxygen consumption and exogenous fuel utilization in sea raven (Hemitripterus americanus). J. Comp. Physiol. 160B: 511–518.

    Google Scholar 

  • Storey, K.B. and Storey, J.M. 1988. Freeze tolerance in animals. Physiol. Rev. 68: 27–84.

    Google Scholar 

  • Walaas, O. and Walaas, E. 1950. Effect of epinephrine on rat diaphragm. J. Biol. Chem. 187: 769–776.

    Google Scholar 

  • Walsh, P.J., Moon, T.W. and Mommsen, T.P. 1985. Interactive effects of acute changes in temperature and pH on metabolism in hepatocytes from the sea raven Hemitripterus americanus. Physiol. Zool. 58: 727–735.

    Google Scholar 

  • Zammit, V.A. and Newsholme, E.A. 1976. The maximum activities of hexokinase, phosphorylase, phosphofructokinase, glycerol phosphate dehydrogenase, lactate dehydrogenase, octopine dehydrogenase, phosphoenolpyruvate carboxykinase, nucleoside diphosphatekinase, glutamate-oxaloacetate transaminase and arginine kinase in relation to carbohydrate utilization in muscles from marine invertebrates. Biochem. J. 160: 447–462.

    Google Scholar 

Download references

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Driedzic, W., West, J., Sephton, D. et al. Enzyme activity levels associated with the production of glycerol as an antifreeze in liver of rainbow smelt (Osmerus mordax). Fish Physiology and Biochemistry 18, 125–134 (1998). https://doi.org/10.1023/A:1007777501093

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1007777501093

Navigation