Isolation, Characterization, and cDNA Sequence of a Carotenoid Binding Protein from the Silk Gland of Bombyx mori Larvae

Tabunoki, Hiroko; Sugiyama, Hiroshi; Tanaka, Yoshiro; Fujii, Hiroshi; Banno, Yutaka; Jouni, Zeina E.; Kobayashi, Masahiko; Satō, Ryōichi; Maekawa, Hideaki; Tsuchida, Kozo

doi:10.1074/jbc.m204507200

Cited by 92 publications

(97 citation statements)

References 32 publications

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“…For differential uptake, the observed tissue specific carotenoid biodistribution would suggest the presence of selective binding or transport proteins. Lutein, zeaxanthin, and β-carotene reportedly utilize a transport and/or binding protein for specific tissue uptake [28][29][30][31][32][33], yet transport proteins for PE, PF, or LYC have not been identified. In CaCo-2 cells, differential and competitive uptake of α-carotene, β-carotene, lutein, and LYC has been reported [34].…”

Section: Discussionmentioning

confidence: 99%

Phytoene, phytofluene, and lycopene from tomato powder differentially accumulate in tissues of male Fisher 344 rats

Campbell¹,

Engelmann²,

Lila³

et al. 2007

Nutrition Research

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Tomato product consumption is inversely related to prostate cancer incidence, and lycopene (LYC) has been implicated in reduced prostate cancer risk. The contribution of other tomato carotenoids, phytoene (PE) and phytofluene (PF), towards prostate cancer risk has not been adequately studied. The relative uptake and tissue distribution of tomato carotenoids are not known. We hypothesize that PE and PF are bioavailable from a tomato powder diet or from a purified source and accumulate in androgen-sensitive tissues. In this study, 4 wk old male Fisher 344 rats were pre-fed an AIN-93G powder diet composed of 10% tomato powder containing PE, PF, and LYC (0.015, 0.012, and 0.011 g/kg diet, respectively). After 30 d tomato powder feeding, hepatic PF concentrations (168 ± 20 nmol/ g) were higher than PE or LYC (104 ± 13 and 104 ± 13 nmol/g, respectively). In contrast, LYC, followed by PF, had the highest accumulation of the measured carotenoids in the prostate lobes and seminal vesicles. When tomato powder-fed rats received a single oral dose of either ∼2.7 mg PE or PF, an increase in the dosed carotenoid concentration was observed in all measured tissues, except the adrenal. Percent increases of PF were greater than that of PE in liver, serum, and adipose (37, 287 and 49% versus 16, 179 and 23%, respectively). Results indicate that the relative tomato carotenoid biodistribution differs in liver and androgen-sensitive tissues, suggesting that minor changes in the number of sequential double bonds in carotenoid structures alter absorption and/or metabolism of tomato carotenoids.

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Section: Discussionmentioning

confidence: 99%

Phytoene, phytofluene, and lycopene from tomato powder differentially accumulate in tissues of male Fisher 344 rats

Campbell¹,

Engelmann²,

Lila³

et al. 2007

Nutrition Research

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“…In 2002, Tabunoki and colleagues studied a series of mutant silkworms with colorless cocoons, and reported the isolation and cDNA sequence of a 33 kDa lutein-specific carotenoid binding protein (CBP) from the midgut epithelium and silk gland [28]. This protein was a new member of the steroidogenic acute regulatory (StAR) family usually involved in cellular cholesterol transport.…”

Section: Invertebrate Carotenoid-binding Proteinsmentioning

confidence: 99%

Vertebrate and invertebrate carotenoid-binding proteins

Bhosale

Bernstein

2007

Archives of Biochemistry and Biophysics

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In invertebrates and vertebrates, carotenoids are ubiquitous colorants, antioxidants, and provitamin A compounds that must be absorbed from dietary sources and transported to target tissues where they are taken up and stabilized to perform their physiological functions. These processes occur in a specific and regulated manner mediated by high-affinity carotenoid-binding proteins. In this minireview, we examine the published literature on carotenoid-binding proteins in vertebrate and invertebrate systems, and we report our initial purification and characterization of a novel luteinbinding protein isolated from liver of Japanese quail (Coturnix japonica).

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“…These binding proteins may act as cell surface receptors, transmembrane transport proteins, metabolic enzymes, intracellular mediators of the biological actions of the ligand, or sites for the deposition and stabilization of the ligand. Carotenoid-binding proteins have been described in plants (11), microorganisms (12,13), and invertebrates (14,15), but relatively little information has been available about specific carotenoid-binding proteins in any vertebrate system. In 1997, Rao et al (16) reported the existence of a ␤-carotenebinding protein in ferret liver, although no sequence data have been provided yet.…”

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confidence: 99%

Identification and Characterization of a Pi Isoform of Glutathione S-Transferase (GSTP1) as a Zeaxanthin-binding Protein in the Macula of the Human Eye

Bhosale

Larson

Frederick

et al. 2004

Journal of Biological Chemistry

245

211

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Uptake, metabolism, and stabilization of xanthophyll carotenoids in the retina are thought to be mediated by specific xanthophyll-binding proteins (XBPs). A membrane-associated XBP was purified from human macula using ion-exchange chromatography followed by gel-exclusion chromatography. Two-dimensional gel electrophoresis showed a prominent spot of 23 kDa and an isoelectric point of 5.7. Using mass spectral sequencing methods and the public NCBI database, it was identified as a Pi isoform of human glutathione S-transferase (GSTP1). Dietary (3R,3 R)-zeaxanthin displayed the highest affinity with an apparent K d of 0. Other mammalian xanthophyll carrier proteins such as tubulin, high-density lipoprotein, low-density lipoprotein, albumin, and ␤-lactoglobulin did not bind zeaxanthins with high affinity, and they failed to induce or alter xanthophyll CD spectra to any significant extent. Immunocytochemistry with an antibody to GSTP1 on human macula sections showed highest labeling in the outer and inner plexiform layers. These results indicate that GSTP1 is a specific XBP in human macula that interacts with (3R,3 S-meso)-zeaxanthin and dietary (3R,3 R)-zeaxanthin in contrast to apparently weaker interactions with (3R,3 R,6 R)-lutein.

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Isolation, Characterization, and cDNA Sequence of a Carotenoid Binding Protein from the Silk Gland of Bombyx mori Larvae

Cited by 92 publications

References 32 publications

Phytoene, phytofluene, and lycopene from tomato powder differentially accumulate in tissues of male Fisher 344 rats

Phytoene, phytofluene, and lycopene from tomato powder differentially accumulate in tissues of male Fisher 344 rats

Vertebrate and invertebrate carotenoid-binding proteins

Identification and Characterization of a Pi Isoform of Glutathione S-Transferase (GSTP1) as a Zeaxanthin-binding Protein in the Macula of the Human Eye

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