Skip to main content
SpringerLink
Log in

DNase activity in murine lenses: Implications for cataractogenesis

  • Laboratory investigations
  • Published:
Graefe's Archive for Clinical and Experimental Ophthalmology Aims and scope Submit manuscript

Abstract

In murine lens extracts a Mg2+-dependent DNase activity was found and characterized with respect to its ionic conditions. The lenticular DNase can be clearly distinguished from DNaseII. Only a moderate DNase activity is detectable in intact nuclei of lens cells from 1-day-old mice, but DNase is obviously present with high activity in lens cell nuclei from 7-day-old mice. During this time, when murine eyes are not yet open, and the fiber cell nuclei including the nuclear membrane remain to be completely digested, only weak activity can be detected in cytosolic lens extracts. In three allelic dominant mice mutants exhibiting hereditary cataracts the DNase activity is inhibited. The decrease of DNase activity follows the same directionality (Cat-2 ns >Cat2 no >Cat-2 t) as the decrease in the relative content of water soluble lens proteins, which might be used as a rough indicator for the severity of cataractogenesis. Both trends are highly significant (P<0.0001).

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Bonner J, Chalkley GR, Dahmus M, Fambrough D, Fujimura F, Huang R-CC, Huberman J, Jense P, Marushiga K, Ohlenbusch H, Olivera B, Widholm J (1968) Isolation and characterization of chromosomal nucleoproteins. Methods Enzymol 1213:3–65

    Google Scholar 

  2. Counis MF, Chaudun E, Courtois Y, Allinquant B (1989) Lens fiber differentiation correlated with activation of two different DNAases in lens embryonic cells. Cell Diff Develop 27:137–146

    Google Scholar 

  3. Counis M-F, Chaudun E, Courtois Y, Allinquant B (1991) DNAase activities in embryonic chicken lens: in epithelial cells or in differentiating fibers where chromatin is progressively cleaved. Biol Cell 72:231–238

    Google Scholar 

  4. Doria R, Graw J, Maier K (1984) Purification and characterization of a y-crystallin from mouse lenses. Curr Eye Res 3:723–728

    Google Scholar 

  5. Fuller JL, Wimer RE (1966) Neural, sensory and motor functions. In: Green EL (ed) Biology of the laboratory mouse, 2nd edn. McGraw-Hill, New York, pp 609–628

    Google Scholar 

  6. Graw J, Liebstein A (1991) Inhibition of lens DNase: an important step towards the understanding of cataractogenesis inCat-2 mutant mice? In: Vrensen GJFM, Clauwaert J (eds) Eye lens membranes and aging. EURAGE, Leiden, pp 363–372

    Google Scholar 

  7. Graw J, Kratochvilova J, Summer K-H (1984) Genetical and biochemical studies of a dominant cataract mutant in mice. Exp Eye Res 39:37–45

    Google Scholar 

  8. Graw J, Gopinath PM, Bors W, Michel C, Summer HK-H (1989) Biochemical analysis of young rats homozygous for the cataract mutationcat. Exp Eye Res 48:1–9

    Google Scholar 

  9. Graw J, Kratochvilova J, Löbke A, Reitmeir P, Schäffer E, Wulff A (1989) Characterization ofScat (Suture Cataract), a dominant cataract mutation in mice. Exp Eye Res 49:469–477

    Google Scholar 

  10. Graw J, Bors W, Gopinath PM, Merkle S, Michel C, Reitmeir P, Schäffer E, Summer K-H, Wulff A (1990) Characterization ofCat-2 t, a radiation-induced dominant cataract mutation in mice. Invest Ophthalmol Vis Sci 31:1353–1361

    Google Scholar 

  11. Graw J, Werner T, Merkle S, Reitmeir P, Schäffer E, Wulff A (1990) Histological and biochemical characterization of the murine cataract mutantNop. Exp Eye Res 50:449–456

    Google Scholar 

  12. Graw J, Coban L, Liebstein A, Werner T (1991) Murine γE-crystallin is distinct from murine γ2-crystallin. Gene 104:265–270

    Google Scholar 

  13. Herve B, Jacquemin E, Lescure B (1983) Endogenous nuclease activity in chick embryo lens cells. Cell Diff 12:265–269

    Google Scholar 

  14. Hewish DR, Burgoyne LA (1973) Chromatin sub-structure. The digestion of chromatin DNA at regularly spaced sites by a nuclear deoxyribonuclease. Biochem Biophys Res Commun 52:504–510

    Google Scholar 

  15. Kratochvilova J, Favor J (1992) Allelism tests of 15 dominant cataract mutations in mice. Genet Res Camb 59:199–203

    Google Scholar 

  16. Kunitz M (1950) Crystalline desoxyribonuclease. II. Digestion of thymus nucleic acid (desoxyribonucleic acid). The kinetics of the reaction. J Gen Physiol 33:363–377

    Google Scholar 

  17. Kuwabara T, Imaizumi M (1974) Denucleation process of the lens. Invest Ophthalmol 13:973–981

    Google Scholar 

  18. Lindblom B, Holmlund G (1988) Rapid DNA purification for restriction fragment length polymorphism analysis. Gene Anal Techn 5:97–101

    Google Scholar 

  19. Maisel H, Harding CV, Alcalá JA, Kuszak J, Bradley R (1981) The morphology of the lens. In: Bloemendal H (ed) Molecular and cellular biology of the eye lens. Wiley, New York, pp 49–84

    Google Scholar 

  20. Maniatis T, Fritsch EF, Sambrook J (1982) Molecular cloning. Cold Spring Harbor Laboratory, Cold Spring Harbor

    Google Scholar 

  21. Muel AS, Chaudun E, Courtois Y, Modak SP, Counis MF (1986) Nuclear endogenous Ca2+-dependent endodeoxyribonuclease in differentiating chick embryonic lens fibers. J Cell Physiol 127:167–174

    Google Scholar 

  22. Nagae S, Ikeda M, Anai M (1983) Endodeoxyribonuclease from nuclei of bovine small intestinal mucosa: further studies on intranuclear localization and cleavage mechanism of the enzyme. Biochem Biophys Res Commun 116:952–958

    Google Scholar 

  23. Oosterhof DK, Hozier JC, Rill RL (1975) Nuclease action on chromatin: evidence for discrete, repeated nucleoprotein units along chromatin fibrils. Proc Natl Acad Sci USA 72:633–637

    Google Scholar 

  24. Oshima RG, Price PA (1973) Alkylation of an essential histidine residue in porcine spleen deoxyribonuclease. J Biol Chem 248:7522–7526

    Google Scholar 

  25. Rosenfeld PJ, Kelly TJ (1986) Purification of nuclear factor I by DNA recognition site affinity chromatography. J Biol Chem 261:1398–1408

    Google Scholar 

  26. Sanwal M, Muel AS, Chaudun E, Courtois Y, Counis MF (1986) Chromatin condensation and terminal differentiation process in embryonic chicken lens in vivo and in vitro. Exp Cell Res 167:429–439

    Google Scholar 

  27. Talwar S, Pocklington MJ, Maclean N (1983) A calcium-activated nuclease endogenous to Xenopus erythrocytes. FEBS Lett 158:349–352

    Google Scholar 

  28. Wyllie AH (1980) Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature 284:555–556

    Google Scholar 

  29. Vrensen GFJM, Graw J, de Wolf A (1991) Nuclear breakdown during terminal differentiation of primary lens fibres in mice: a transmission electron microscopic study. Exp Eye Res 52:647–659

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. GSF-Forschungszentrum für Umwelt und Gesundheit, Institut für Säugetiergenetik, W-8042, Neuherberg, Germany

    Jochen Graw & Alexander Liebstein

Authors
  1. Jochen Graw
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Alexander Liebstein
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Graw, J., Liebstein, A. DNase activity in murine lenses: Implications for cataractogenesis. Graefe's Arch Clin Exp Ophthalmol 231, 354–358 (1993). https://doi.org/10.1007/BF00919034

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00919034

Keywords

Search

Navigation