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Volume 271, Number 18, Issue of May 3, 1996 pp. 10437-10440
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Vitamin A Bound to Cellular Retinol-binding Protein as Ultraviolet Filter in the Eye Lens of the Gecko Lygodactylus picturatus

(Received for publication, February 13, 1996)

Beate Röll ,  Reinout Amons ,  Wilfried W. de Jong

The yellow eye lenses of the diurnal gecko Lygodactylus picturatus contain, in addition to the usual crystallins, a monomeric protein with a molecular mass of 16 kDa. It comprises 6-8% of the total water-soluble lens proteins. We here identify it as a novel type of crystallin, most closely related with cellular retinol-binding protein I (CRBP I). Because of its tiny size, we designate it as -crystallin. The typical endogenous ligand of CRBP is all-trans-retinol. In the gecko lens, however, the ligand of -crystallin turns out to be 3-dehydroretinol (vitamin A(2)), which causes the yellow color of this lens. The -crystallinbullet3-dehydroretinol complex absorbs shortwave radiation, supposedly improving the optical quality of the dioptric apparatus and protecting the retina against ultraviolet damage. Whereas other crystallins have been recruited from stress proteins and metabolic enzymes, -crystallin represents a completely new class of taxon-specific lens proteins. Also, its ligand 3-dehydroretinol represents a novel type of lens pigment.



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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.