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  • Title: Rho B-crystallin, an aldose reductase-like lens protein in the gecko Lepidodactylus lugubris.
    Author: Röll B, van Boekel MA, Amons R, de Jong WW.
    Journal: Biochem Biophys Res Commun; 1995 Dec 14; 217(2):452-8. PubMed ID: 7503721.
    Abstract:
    The ocular lenses of the diurno-nocturnal gecko Lepidodactylus lugubris contain a monomeric 38-kDa protein at a level of 20 to 22% of the total water-soluble protein. Amino acid sequences of peptides from this protein are most similar--up to 72% identity--to mammalian aldose reductase, an NADPH-dependent reductase which normally occurs at house-keeping levels in the eye lens, and which is involved in the development of diabetic cataract. The sequences show 56% identity with rho-crystallin from lenses of the frog genus Rana. It is concluded that different genes from the same superfamily of NADPH-dependent reductases have been recruited to become highly expressed as lens proteins in at least two different evolutionary lineages. To reflect the relationship with frog rho-crystallin, the gecko lens protein is designated as rho B-crystallin. As for frog rho-crystallin, no enzymatic activity could be established for rho B-crystallin in the gecko lens. Up to now, rho B-crystallin has not been detected in lenses of other reptiles or amphibians.
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