title: Vitamin A2 bound to cellular retinol-binding protein as ultraviolet filter in the eye lens of the gecko Lygodactylus picturatus.
abstract: 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 16kDa. 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 iota-crystallin. The typical endogenous ligand of CRBP is all-trans-retinol. In the gecko lens, however, the ligand of iota-crystallin turns out to be 3-dehydroretinol (vitamin A2), which causes the yellow color of this lens. The iota-crystallin.3-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, iota-crystallin represents a completely new class of taxon-specific lens proteins. Also, its ligand 3-dehydroretinol represents a novel type of lens pigment.
authors.affiliation: Lehrstuhl für Tierphysiologie, Fakultät für Biologie, Ruhr-Universität Bochum, Germany.
authors.forename: B
authors.initials: B
authors.lastname: Röll
authors.forename: R
authors.initials: R
authors.lastname: Amons
authors.forename: W W
authors.initials: WW
authors.lastname: de Jong
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D007908:Lens, Crystalline / Q000378:metabolism* / Q000528:radiation effects; D008116:Lizards; D008969:Molecular Sequence Data; D011485:Protein Binding; D018168:Receptors, Retinoic Acid / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014466:Ultraviolet Rays; D014801:Vitamin A / Q000031:analogs & derivatives* / Q000378:metabolism
chemical_list: D018168:Receptors, Retinoic Acid; C082927:retinoic acid binding protein I, cellular; C024366:vitamin A2; D014801:Vitamin A