TAILIEUCHUNG - Báo cáo khoa học: A novel retinol-binding protein in the retina of the swallowtail butterfly, Papilio xuthus

Retinoid-binding proteins are indispensable for visual cycles in both vertebrate and invertebrate retinas. These proteins stabilize and transport hydrophobic retinoids in the hydro-philic environment of plasma and cytoplasm, and allow regeneration of visual pigments. Here, we identified a novel retinol-binding protein in the eye of a butterfly, Papilio xuthus. The protein that we term Papilioretinol-binding protein (PapilioRBP) is a major component of retinal soluble proteins and exclusively binds 3-hydroxyretinol, and emits fluorescencepeakingat 480 nmunder ultraviolet (UV) illumination. . | Eur. J. Biochem. 270 2436-2445 2003 FEBS 2003 doi A novel retinol-binding protein in the retina of the swallowtail butterfly Papilio xuthus Motohiro Wakakuwa1 Kentaro Arikawa1 and Koichi Ozaki2 1Graduate School of Integrated Science Yokohama City University Yokohama Kanagawa 2Graduate School of Frontier Biosciences Osaka University Toyonaka Osaka Japan Retinoid-binding proteins are indispensable for visual cycles in both vertebrate and invertebrate retinas. These proteins stabilize and transport hydrophobic retinoids in the hydrophilic environment of plasma and cytoplasm and allow regeneration of visual pigments. Here we identified a novel retinol-binding protein in the eye of a butterfly Papilio xuthus. The protein that we term Papilio retinol-binding protein Papilio RBP is a major component of retinal soluble proteins and exclusively binds 3-hydroxyretinol and emits fluorescence peaking at 480 nm under ultraviolet UV illumination. The primary structure deduced from the nucleotide sequence of the cDNA shows no similarity to any other lipophilic ligand-binding proteins. The molecular mass and isoelectric point of the protein estimated from the amino-acid sequence are kDa and respectively. The absence of any signal sequence for secretion in the N-terminus suggests that the protein exists in the cytoplasmic matrix. All-trans 3-hydroxyretinol is the major ligand of the Papilio RBP in dark-adapted eyes. Light illumination of the eyes increases the 11-cis isomer of the ligand and induces redistribution of the Papilio RBP from the proximal to the distal part of the photoreceptor layer. These results suggest that the Papilio RBP is involved in visual pigment turnover. Keywords retinol-binding protein rhodopsin visual pigment visual cycle. Retinalaldehyde retinal plays an essential role in animal vision as the chromophore of visual pigments that are generically called rhodopsins. In the rhodopsin molecule retinal is bound to the .

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