Advertisement

The Protein Journal

, Volume 33, Issue 2, pp 128–134 | Cite as

Lactate Dehydrogenase Like Crystallin: A Potentially Protective Shield for Indian Spiny-Tailed Lizard (Uromastyx hardwickii) Lens Against Environmental Stress?

  • Ambreen Atta
  • Amber Ilyas
  • Zehra Hashim
  • Aftab Ahmed
  • Shamshad Zarina
Article

Abstract

Taxon specific lens crystallins in vertebrates are either similar or identical with various metabolic enzymes. These bifunctional crystallins serve as structural protein in lens along with their catalytic role. In the present study, we have partially purified and characterized lens crystallin from Indian spiny-tailed lizard (Uromastyx hardwickii). We have found lactate dehydrogenase (LDH) activity in lens indicating presence of an enzyme crystallin with dual functions. Taxon specific lens crystallins are product of gene sharing or gene duplication phenomenon where a pre-existing enzyme is recruited as lens crystallin in addition to structural role. In lens, same gene adopts refractive role in lens without modification or loss of pre-existing function during gene sharing phenomenon. Apart from conventional role of structural protein, LDH activity containing crystallin in U. hardwickii lens is likely to have adaptive characteristics to offer protection against toxic effects of oxidative stress and ultraviolet light, hence justifying its recruitment. Taxon specific crystallins may serve as good models to understand structure–function relationship of these proteins.

Keywords

ε-Crystallin Gene recruitment Gene sharing Lactate dehydrogenase Reptilian lens Taxon specific crystallin 

Abbreviations

LDH

Lactate dehydrogenase

PVDF

Polyvinylidene difluoride

RP-HPLC

Reverse phase-high performance liquid chromatography

UV

Ultra-violet

Notes

Acknowledgments

DNA sequencing analysis and N-terminal protein sequencing were provided by Centralized Science Laboratory, University of Karachi, Pakistan and RI-INBRE Centralized Core Facility, University of Rhode Island, USA, supported by Grant # 5P20GM103430-13 from the National Institute of General Medical Sciences of the National Institute of Health.

References

  1. 1.
    Bloemendal H (1981) In: Bloemendal H (ed) Molecular and cellular biology of the eye lens. Wiley, New YorkGoogle Scholar
  2. 2.
    Wistow G, Piatigosky J (1988) Lens crystallins evolution and expression of proteins for a highly specialized tissue. Annu Rev Biochem 57:479–504CrossRefGoogle Scholar
  3. 3.
    Barbosa P, Wistow GJ, Cialkowski M, Piatigorsky J, O’brien WE (1991) Expression of duck lens delta-crystallin cDNAs in yeast and bacterial hosts. Delta 2-crystallin is an active argininosuccinate lyase. J Biol Chem 266(33):22319–22322Google Scholar
  4. 4.
    Wistow G, Richardson J, Jaworski C, Graham C, Sharon-Friling R, Segovia L (1994) Crystallins: the over expression of functional enzymes and stress proteins in the eye lens. Biotechnol Genet Eng Rev 12:1–38CrossRefGoogle Scholar
  5. 5.
    Piatigorsky J, Wistow G (1991) The recruitment of crystallins: new function precedes gene duplication. Science 252:1078–1079CrossRefGoogle Scholar
  6. 6.
    Agrawal R, Chandrashekhar R, Mishra AK, Ramadevi J, Sharma Y, Aggarwal RK (2002) Cloning and sequencing of complete tau-crystallin cDNA from embryonic lens of Crocodylus palustris. J Biosci 27(3):251–259CrossRefGoogle Scholar
  7. 7.
    Piatigorsky J (1992) Lens crystallins. Innovation associated with changes in gene regulation. J Biol Chem 267(7):4277–4280Google Scholar
  8. 8.
    Stapel SO, Zweers A, Dodemont HJ, Kan JH, De Jong WW (1985) epsilon-Crystallin, a novel avian and reptilian eye lens protein. Eur J Biochem 147(1):129–136CrossRefGoogle Scholar
  9. 9.
    Metzler DE (1977) Biochemistry: the chemical reactions of living cells. Academic Press, New YorkGoogle Scholar
  10. 10.
    Cahn RD, Kaplan NO, Zwilling E, Levine L (1962) Nature and development of lactic dehydrogenases: the two major types of this enzyme form molecular hybrids which change in makeup during development. Science 136:962–969CrossRefGoogle Scholar
  11. 11.
    Keeton WT (1972) Biological science, 2nd edn. W. W. Norton, New YorkGoogle Scholar
  12. 12.
    De Jong WW, Stapel SO, Zweers A (1981) ɛ-Crystallin, a novel avian and reptilian eye lens protein. Comp Biochem Physiol 69:593–598Google Scholar
  13. 13.
    Roll B, Amons R, De Jong WW (1996) Vitamin A2 bound to cellular retinol-binding protein as ultraviolet filter in the eye lens of the gecko Lygodactylus picturatus. J Biol Chem 271:10437–10440CrossRefGoogle Scholar
  14. 14.
    Zain-Ul-Abedin M, Barbara KZ (1977) Characterization, biochemistry of the lizard Uromastyx hardwickii. University of Karachi, PakistanGoogle Scholar
  15. 15.
    Weisshaar HD, Prasad MC, Parker RS (1975) Estimation of lactate dehydrogenase in serum/plasma. Med Welt 26:387–391Google Scholar
  16. 16.
    Laemmli UK (1970) Cleavage of structural proteins during assembly of the head of bacteriophage. Nature 227:680–685CrossRefGoogle Scholar
  17. 17.
    Piatigorsky J (1993) Puzzle of crystallin diversity in eye lenses. Dev Dyn 196:267–272CrossRefGoogle Scholar
  18. 18.
    Wistow G, Wyatt K, David L, Gao C, Bateman O, Bernstein S, Tomarev S, Segovia L, Slingsby C, Vihtelic T (2005) Gamma N-crystallin and evolution of the beta gamma-crystallin super family in vertebrates. FEBS J 272(9):2276–2291CrossRefGoogle Scholar
  19. 19.
    Ryan LD, Vestling CS (1974) Rapid purification of lactate dehydrogenase from rat liver and hepatoma: a new approach. Arch Biochem Biophys 160(1):279–284CrossRefGoogle Scholar
  20. 20.
    Kopperschlager G, Diezel W, Freyer R, Liebe S, Hofmann E (1971) Reciprocity of yeast-phosphofructokinase with dextran blue 2000. Eur J Biochem 22(1):40–45CrossRefGoogle Scholar
  21. 21.
    Akatsuka I, Bando M, Obazawa H, Oka M, Takehana M, Kobayashi S (2001) NADH-dependent dehydroascorbate reductase in the rabbit lens. Tokai J Exp Clin Med 26:25–32Google Scholar
  22. 22.
    Ya-Huei C, Ming-Ting L, Yu-Wen C, Wei-Yuan C, Chung-Ming Y, Hwei-Jen L (2011) Distinct interactions of αA-crystallin with homologous substrate proteins, δ-crystallin and argininosuccinate lyase, under thermal stress. Biochimie 93:314–320CrossRefGoogle Scholar
  23. 23.
    Zigler JS Jr, Rao PV (1991) Enzyme/crystallins and extremely high pyridine nucleotide levels in the eye lens. FASEB J 5:223–225Google Scholar
  24. 24.
    Wistow G (1995) Molecular biology and evolution of crystallins: gene recruitment and multifunctional proteins in eye lens. RG Landes, USAGoogle Scholar
  25. 25.
    Wistow G, Mulders JWM, de Jong WW (1987) The enzyme lactate dehydrogenase as a structural protein in avian and crocodile lens. Nature 326:622–624CrossRefGoogle Scholar
  26. 26.
    Lehringer-Albert L, Nelson-David L, Cox-Michael M (1993) Principles of biochemistry, 2nd edn. Worth, New YorkGoogle Scholar
  27. 27.
    Bennett AF, Dawson WR (1976) In: Gans C, Dawson WR (eds) Biology of reptilian-physiology, 4th edn. Academic Press, EnglandGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  • Ambreen Atta
    • 1
  • Amber Ilyas
    • 1
  • Zehra Hashim
    • 1
  • Aftab Ahmed
    • 2
  • Shamshad Zarina
    • 1
  1. 1.National Center for ProteomicsUniversity of KarachiKarachiPakistan
  2. 2.Biomedical and Pharmaceutical SciencesUniversity of Rhode IslandKingstonUSA

Personalised recommendations