Skip to main content
Log in

Polyamines in liver and their influence on chromatin condensation after 17-β estradiol treatment of Atlantic salmon

  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Abstract

Atlantic salmon (Salmo salar) were treated with 17-β estradiol to induce vitellogenin synthesis in liver. This led to an increase in liver wet weight and total DNA. After incubation with micrococcal nuclease (EC 3.1.31.1) less soluble chromatin was obtained from nuclei of the estradiol treated than the control fish, but active gene regions were solubilized by the nuclease. Thus, in the estradiol treated fish soluble mononucleosomes contained hybridizable vitellogenin gene sequences. As a result of estradiol treatment the content in total liver of putrescine rose 3-fold, that of spermidine 2-fold, while spermine was unchanged. In muscle no significant changes were observed. The regulatory functions of polyamines during gene expression were investigated by binding (14C)spermine to isolated liver nuclei depleted of endogenous polyamines. The number of binding sites was higher in nuclei of estradiol treated than control fish. (14C)spermine associated preferentially with micrococcal nuclease insensitive chromatin. Thus, the high content of putrescine and spermidine in liver supported the view of polyamine accumulation in proliferating tissues. The preferential binding to condensed chromatin indicated a stabilizing effect of polyamines on the organization of inactive chromatin structures.

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

Abbreviations

MNase:

micrococcal nuclease

PMSF:

phenylmethylsulfonylfluoride

References

  1. Ng TB, Idler DR: Yolk formation and differentiation in teleost fishes. In: WS Hoar, DJ Randall and EM Donaldson (eds.) Fish Physiology, Vol. 9A. Academic Press, New York, 1983, pp 373–404

    Google Scholar 

  2. Waters S, von der Decken A: Characterization of liver chromatin proteins after induction of vitellogenin synthesis in salmon (Salmo salar). Int J Biochem 21: 383–389, 1989

    Google Scholar 

  3. Emmersen J, Korsgaard B, Petersen I: Dose response kinetics of serum vitellogenin, liver DNA, RNA, protein and lipid after induction by estradiol-17β in male flounders (Platichthys flesus L.). Comp Biochem Physiol 63B: 1–6, 1979

    Google Scholar 

  4. Tabor CW, Tabor H: Polyamines. Ann Rev Biochem 53: 749–790, 1984

    Google Scholar 

  5. Pegg AE: Recent advances in the biochemistry of polyamines in eukaryotes. Biochem J 234: 249–262, 1986

    CAS  PubMed  Google Scholar 

  6. Snyder RD: Polyamine depletion is associated with altered chromatin structure in Hela cells. Biochem J 260: 697–704, 1989

    Google Scholar 

  7. Morgan JE, Blankenship JW, Matthews HR: Polyamines and acetylpolyamines increase the stability and alter the conformation of nucleosome core particles. Biochemistry 26: 3643–3649, 1987

    Google Scholar 

  8. Marx KA, Reynolds TC: Ion competition and micrococcal nuclease digestion studies of spermidine-condensed calf thymus DNA. Evidence for torus organization by circumferential DNA wrapping. Biochim Biophys Acta 741: 279–287, 1983

    Google Scholar 

  9. Colson P, Houssier C: Polyamine addition to preparation media induces chromatin condensation, irreversibly at low ionic strength. FEBS Letters 257: 141–144, 1989

    Google Scholar 

  10. Waters S, von der Decken A: A 21 KDa protein resides in the nucleosomes of micrococcal nuclease sensitive liver chromatin of Atlantic salmon treated with estradiol. Cell Mol Biol 36: 197–204, 1990

    Google Scholar 

  11. Giles KW, Myers A: An improved diphenylamine method for the estimation of deoxyribonucleic acid. Nature (London) 206: 93, 1965

    Google Scholar 

  12. Maniatis T, Fritsch EF, Sambrock J: Molecular Cloning. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1982

    Google Scholar 

  13. Maitre J-L, Mercier L, Dolo L, Valotaire Y: Caractérisation de récepteurs spécifiques à l'oestradiol, induction de la vitellogenine et de son mRNA dans le foie de truite arc-en-ciel (Salmo gairdnerii). Biochimie 67: 215–225, 1985

    Google Scholar 

  14. Anderson MLM, Young BD: Quantitative filter hybridisation. In: BD Hames and SJ Higgins (eds.) Nucleic Acid Hybridisation. IRL Press, Oxford, U.K., 1985, pp 71–111

    Google Scholar 

  15. Kanda S, Takahashi M, Nagase S: Fluorometric assay for polyamines in urine and tissues using electrophoresis on titan III cellulose acetate. Anal Biochem 180: 307–310, 1989

    Google Scholar 

  16. Snedecor GW, Cochran WG: Statistical Methods, 7th Edition, Iowa State University Press, Ames, IA, 1980

    Google Scholar 

  17. Morgan DML: Polyamines. Essays Biochem 23: 82–115, 1987

    Google Scholar 

  18. Morgan DML: Polyamines and regulation: perspectives. Biochem Soc Trans 18: 1080–1084, 1990

    Google Scholar 

  19. Andersson GM, von der Decken A: Deoxyribonucleic acid-dependent ribonucleic acid polymerase activity in rat liver after protein restriction. Biochem J 148: 49–56, 1975

    Google Scholar 

  20. Mach M, Ebert P, Popp R, Ogilvie A: Compartmentalization of polyamines in mammalian cells. Biochem Biophys Res Comm 104: 1327–1334, 1982

    Google Scholar 

  21. Olin T, Westman A, von der Decken A: Time- and temperature-dependent appearance of vitellogenin in Golgi vesicles and serum after estrogen treatment of salmon (Salmo salar). J Expt Zool 249: 213–220, 1989

    Google Scholar 

  22. von der Decken A, Olin T, Waters S, Nazar DS, Persson G, Westman A: Response of hepatic and skeletal muscle proteins to the onset of vitellogenesis induced by estradiol. In: M Takada and T Watanaba (eds.) Proc 3rd Int Symp on Feeding and Nutr of Fish. Japan Translation Center, Ltd, Tokyo, pp 443–450

  23. Smith TK: Effect of dietary putrescine on whole body growth and polyamine metabolism. Proc Soc Expt Biol Med 194: 332–336, 1990

    Google Scholar 

  24. Nazar DS, Persson G, Olin T, Waters S, von der Decken A: Sarcoplasmic and myofibrillar proteins in white trunk muscle of salmon (Salmo salar) after estradiol treatment. Comp Biochem Physiol 98B: 109–114, 1991

    Google Scholar 

  25. Olin T, Nazar DS, von der Decken A: Response of epaxial muscle and liver to 17-β estradiol in fed and starved Atlantic salmon (Salmo salar). Aquaculture 1991, in press

  26. Jackson DA: Structure-function relationships in eukaryotic nuclei. BioEssays 13: 1–10, 1991

    Google Scholar 

  27. Marquet R, Colson P, Houssier C: The condensation of chromatin and histone H1- depleted chromatin by spermine. J Biomol Struct Dyn 4: 205–218, 1986

    Google Scholar 

  28. Koch MH, Sayers Z, Michon AM, Marquet R, Houssier C, Willfuehr J: The superstructure of chromatin and its condensation mechanism. V. Effects of linker length, condensation by multivalent cations, solubility and electric dichroism properties. Eur Biophys J 16: 177–185, 1988

    Google Scholar 

  29. Smirnov IV, Dimitrov SI, Makarov VL: Polyamine-DNA interactions. Condensation of chromatin and naked DNA. J Biomol Struct Dyn 5: 1149–1161, 1988

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Waters, S., Khamis, M. & von der Decken, A. Polyamines in liver and their influence on chromatin condensation after 17-β estradiol treatment of Atlantic salmon. Mol Cell Biochem 109, 17–24 (1992). https://doi.org/10.1007/BF00230869

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00230869

Key words

Navigation