Lactate Dehydrogenase Like Crystallin: A Potentially Protective Shield for Indian Spiny-Tailed Lizard (Uromastyx hardwickii) Lens Against Environmental Stress?
- 207 Downloads
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.
Keywordsε-Crystallin Gene recruitment Gene sharing Lactate dehydrogenase Reptilian lens Taxon specific crystallin
Reverse phase-high performance liquid chromatography
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.
- 1.Bloemendal H (1981) In: Bloemendal H (ed) Molecular and cellular biology of the eye lens. Wiley, New YorkGoogle Scholar
- 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
- 7.Piatigorsky J (1992) Lens crystallins. Innovation associated with changes in gene regulation. J Biol Chem 267(7):4277–4280Google Scholar
- 9.Metzler DE (1977) Biochemistry: the chemical reactions of living cells. Academic Press, New YorkGoogle Scholar
- 11.Keeton WT (1972) Biological science, 2nd edn. W. W. Norton, New YorkGoogle Scholar
- 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
- 14.Zain-Ul-Abedin M, Barbara KZ (1977) Characterization, biochemistry of the lizard Uromastyx hardwickii. University of Karachi, PakistanGoogle Scholar
- 15.Weisshaar HD, Prasad MC, Parker RS (1975) Estimation of lactate dehydrogenase in serum/plasma. Med Welt 26:387–391Google Scholar
- 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
- 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.Wistow G (1995) Molecular biology and evolution of crystallins: gene recruitment and multifunctional proteins in eye lens. RG Landes, USAGoogle Scholar
- 26.Lehringer-Albert L, Nelson-David L, Cox-Michael M (1993) Principles of biochemistry, 2nd edn. Worth, New YorkGoogle Scholar
- 27.Bennett AF, Dawson WR (1976) In: Gans C, Dawson WR (eds) Biology of reptilian-physiology, 4th edn. Academic Press, EnglandGoogle Scholar