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Journal of Comparative Physiology B

, Volume 156, Issue 4, pp 497–502 | Cite as

Features of the lipid transport system of fish as demonstrated by studies on starvation in the rainbow trout

  • Darcey Black
  • E. Roy Skinner
Article

Summary

A comparison was made of the processes involved in the transport and uptake of lipids in starved and fed trout in order to gain a fuller understanding of the underlying mechanisms of these processes and their control in fish. Trout that had been starved for 8 weeks showed significantly lower lipoprotein lipase activities than control fed fish in their adipose tissue (64±45 and 546±205 units±SEM for starved and fed, respectively;P<0.05) and liver (22±6 and 147±56;P<0.05) but no significant difference in red muscle (22±6 and 88±35) or heart (0.53±0.20 and 0.89±0.27). A similar difference in salt-resistant lipase, present in extra-hepatic tissues in trout, was found, i.e. adipose tissue: 200±105 and 1,327±190 (P<0.05); liver: 133±16 and 404±78 (P<0.01); red muscle: 101±32 and 105±20 (n.s.); heart: 2.43±0.38 and 1.92±0.37 (n.s.). The plasma cholesterol esterifying activity of starved trout (1.79±0.36 units) was significantly lower (P<0.001) than the fed fish (3.74±0.65). The concentrations of plasma VLDL and LDL were 67% and 47% lower (P<0.001 andP<0.05, respectively) in the starved than in the fed trout, while the concentration of HDL was the same (163±15 and 165±20 mg cholesterol/100 ml for starved and fed fish, respectively), as was the concentration of nonesterified fatty acids (0.303±0.039 and 0.333±0.035 mEq/l, respectively). These observations demonstrate that, in spite of differences in the distribution of lipases between the various tissues, fish possess systems for the transport and uptake of lipids that broadly parallel those of mammals and are consistent with the greater use of lipid as a major energy source in fish.

Keywords

Lipase Adipose Tissue Rainbow Trout Lipase Activity Lipoprotein Lipase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

VLDL, LDL andHDL

very low density, low density and high density lipoproteins, respectively, isolated from trout plasma by flotation at densities 1.023, 1.086 and 1.21 g/ml

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References

  1. Barker WC, Dayhoff MO (1977) Evolution of lipoproteins deduced from protein sequence data. Comp Biochem Physiol 57B:309–315Google Scholar
  2. Belfrage P, Vaughan M (1969) Simple liquid-liquid partition system for isolation of labelled oleic acid from mixtures with glycerides. J Lipid Res 10:341–344Google Scholar
  3. Black D, Kirkpatrick SA, Skinner ER (1983a) Lipoprotein lipase and salt-resistant lipase activities in the livers of the rainbow trout and cod. Biochem Soc Trans 11:708Google Scholar
  4. Black D, Youssef AM, Skinner ER (1983b) The mechanism of lipid uptake by tissues in the rainbow trout,Salmo gairdneri R. Biochem Soc Trans 11:93–94Google Scholar
  5. Black D, Mackie SG, Skinner ER (1985) A lecithin: cholesterol acyltransferase-like activity in the plasma of the rainbow trout. Biochem Soc Trans 13:143–144Google Scholar
  6. Bligh EH, Dyer WJ (1959) A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37:911–917Google Scholar
  7. Borensztajn J, Robinson DS (1970) The effect of fasting on the utilization of chylomicron triglyceride fatty acids in relation to clearing factor lipase (lipoprotein lipase) releasable by heparin in the perfused rat heart. J Lipid Res 11:111–117Google Scholar
  8. Borensztajn J, Otway S, Robinson DS (1970) Effect of fasting on the clearing factor lipase (lipoprotein lipase) activity of fresh and defatted preparations of rat heart muscle. J Lipid Res 11:102–110Google Scholar
  9. Chapman MJ (1980) Animal lipoproteins: chemistry, structure, and comparative aspects. J Lipid Res 21:789–853Google Scholar
  10. Chapman MJ, Goldstein S, Mills GL, Leger C (1978) Distribution and characterization of the serum lipoproteins and their apoproteins in the rainbow trout (Salmo gairdneri). Biochemistry 17:4455–4464Google Scholar
  11. Cordle SR, Yeaman SJ, Clegg RA (1983) Salt-resistant (hepatic) lipase. Evidence for its presence in bovine liver and adrenal cortex. Biochim Biophys Acta 753:213–219Google Scholar
  12. Cowey CB, Sargent JR (1972) Fish nutrition. In: Russell FS, Yonge M (eds) Advances in marine biology, vol 10. Academic Press, London New York, pp 383–492Google Scholar
  13. Cowey CB, Sargent JR (1979) Nutrition. In: Hoar WS, Randall DJ, Brett JR (eds) Fish physiology, vol VIII. Academic Press, London New York, pp 1–70Google Scholar
  14. Dannevig BH, Norum KR (1982) Cholesterol esterification and lipids in blood plasma of the char (Salmo alpinus L.) during sexual maturation. comp Biochem Physiol 73B:771–777Google Scholar
  15. Fielding CJ, Shore VG, Fielding PE (1972) A protein cofactor of lecithin-cholesterol acyltransferase. Biochem Biophys Res Commun 46:1493–1498Google Scholar
  16. Groot PHE, Scheek LM, Jansen H (1983) Liver lipase and high density lipoprotein. Lipoprotein changes after incubation of human serum with rat liver lipase. Biochim Biophys Acta 751:393–400Google Scholar
  17. Hanson SWF, Olley J (1963) Application of the Bligh and Dyer method of lipid extraction to tissue homogenates. Biochem J 89:101–102PGoogle Scholar
  18. Hernell O, Egelrud T, Olivecrona T (1975) Serum-stimulated lipases (lipoprotein lipases). Immunological crossreaction between the bovine and the human enzymes. Biochem Biophys Acta 381:233–241Google Scholar
  19. Jansen H, Kalkman c, Birkenlager JR, Hülsmann WC (1980) Demonstration of a heparin-releasable liver-lipase-like activity in rat adrenals. FEBS Lett 112:30–34Google Scholar
  20. Jansen H, DeGreef WJ (1981) Heparin-releasable lipase activity of rat adrenals, ovaries and testes. Biochem J 196:739–745Google Scholar
  21. Johnston IA (1981) Structure and function of fish muscles. Symp Zool Soc London 48:71–113Google Scholar
  22. Johnston IA, Goldspink G (1973) Some effects of prolonged starvation on the metabolism of the red and white myotomal muscles of the plaice,Pleuronectes platessa. Mar Biol 19:348–353Google Scholar
  23. Krauss RM, Windmueller HG, Levy RI, Fredrickson DS (1972) Selective measurement of two different triglyceride lipase activities in rat postheparin plasma. J Lipid Res 14:286–295Google Scholar
  24. LaRosa JC, Levy RI, Windmueller HG, Fredrickson DS (1972) Comparison of the triglyceride lipase of liver adipose tissue, and postheparin plasma. J Lipid Res 13:356–363Google Scholar
  25. Love RM (1980) The chemical biology of fishes, vol 2. Academic Press, New York LondonGoogle Scholar
  26. Mills GL, Taylaur CE (1971) The distribution and composition of serum lipoproteins in eighteen animals. Comp Biochem Physiol 40B:489–501Google Scholar
  27. Nagayama F, Oshima H (1974) Studies on the enzyme system of carbohydrate metabolism in fish — 1. Properties of liver hexokinase. Bull Jpn Soc Sci Fish 40:285–290Google Scholar
  28. Palmer TN, Ryman BE (1972) Studies on oral glucose intolerance in fish. J Fish Biol 4:311–319Google Scholar
  29. Patterson S, Goldspink G (1973) The effect of starvation on the ultrastructure of the red and white myotomal muscles of the crucian carp (Carassius carassius). Z Zellforsch Mikrosk Anat 146:375–384Google Scholar
  30. Patterson S, Johnston IA, Goldspink G (1974) The effect of starvation on the chemical composition of red and white muscles in the plaice (Pleuronectes platessa). Experientia 30:892–894Google Scholar
  31. Robinson DS (1963) Changes in the lipolytic activity of the guinea pig mammary gland at parturition. J Lipid Res 4:21–23Google Scholar
  32. Rogie A, Skinner ER (1985) The roles of the intestine and liver in the biosynthesis of plasma lipoproteins in the rainbow trout,Salmo gairdneri Richardson. Comp Biochem Physiol 81B:285–289Google Scholar
  33. Salaman MR, Robinson DS (1961) The effect of fasting on the cleaning factor lipase activity of rat adipose tissue and plasma. In: Desnuelle P (ed) The enzymes of lipid metabolism. Pergamon Press, New York (Proc 6th Int Conf Biochem Lipids, 1961), pp 218–230Google Scholar
  34. Skinner ER, Rogie A (1978b) The isolation and partial characterization of the serum lipoproteins and apolipoproteins of the rainbow trout. Biochem J 173:507–520Google Scholar
  35. Skinner Er, Rogie A (1978b) Trout egg lipoprotein and its relationship to normal serum lipoproteins. Protides Biol Fluids Proc Colloq 25:491–494Google Scholar
  36. Skinner ER, Youssef AM (1982) The characterization of lipoprotein lipase isolated from the post-heparin plasma of the rainbow trout,Salmo gairdneri Richardson. Biochem J 203:727–734Google Scholar
  37. Skinner ER, Youssef AM, Plack PA (1980) Lipoprotein lipase activity in the post-heparin plasma and adipose tissue of the rainbow trout (Salmo gairdnerii). Biochem Soc Trans 8:74Google Scholar
  38. Snedecor GW, Cochran WG (1967) Statistical methods, 6th edn Iowa State University Press, Ames, Iowa, pp 91–119Google Scholar
  39. Stokke KT, Norum KR (1971) Determination of lecithin: cholesterol acyltransferase in human blood plasma. Scand J Clin Lab Invest 27:21–27Google Scholar
  40. Tan MH, Sata T, Havel RJ (1977) The significance of lipoprotein lipase in rat skeletal muscle. J Lipid Res 18:363–370Google Scholar

Copyright information

© Springer-Verlag 1986

Authors and Affiliations

  • Darcey Black
    • 1
  • E. Roy Skinner
    • 1
  1. 1.Department of BiochemistryUniversity of Aberdeen, Marischal CollegeAberdeenScotland UK

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