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Retinoids: in vitro interaction with retinol‐binding protein and influence on plasma retinol
The FASEB Journal, 1993Studies have been conducted to investigate the structure‐function relationships of retinoids in their in vitro interaction with plasma retinol‐binding protein (RBP) and in their influence on plasma retinol concentration. Two classes of retinoids, one bearing modifications in the area of the retinol hydroxyl end group (fenretinide ...
BERNI, Rodolfo +4 more
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The transthyretin-retinol-binding protein complex
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000Transthyretin (TTR, formerly called prealbumin), one of the transporters of the hormone thyroxine and the lipocalin retinol-binding protein (RBP), the specific carrier of the vitamin, are known to form, under physiological conditions, a macromolecular complex that is believed to play an important physiological role: prevention of glomerular filtration ...
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Archives of Biochemistry and Biophysics, 1985
Retinol (vitamin A alcohol), which plays an important role in the differentiation of epithelia, can be transferred to chromatin in vitro. Rat liver chromatin can accept retinol in a specific and saturable manner only when the retinol is presented as a complex with cellular retinol-binding protein (CRBP).
G, Liau, D E, Ong, F, Chytil
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Retinol (vitamin A alcohol), which plays an important role in the differentiation of epithelia, can be transferred to chromatin in vitro. Rat liver chromatin can accept retinol in a specific and saturable manner only when the retinol is presented as a complex with cellular retinol-binding protein (CRBP).
G, Liau, D E, Ong, F, Chytil
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1995
Retinol binding protein is a single chain polypeptide of 21 000 Da without associated carbohydrate. It is the sole transport protein for vitamin A, and exists in the serum as an equimolar complex with prealbumin (trans-thyretin). Free retinol binding protein is rapidly excreted by the kidney, the function of the prealbumin-RBP complex appearing to be a
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Retinol binding protein is a single chain polypeptide of 21 000 Da without associated carbohydrate. It is the sole transport protein for vitamin A, and exists in the serum as an equimolar complex with prealbumin (trans-thyretin). Free retinol binding protein is rapidly excreted by the kidney, the function of the prealbumin-RBP complex appearing to be a
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Retinol and retinol-binding protein in neonates with Bronchopulmonary Dysplasia
Nutrition Research, 1999Abstract The incidence of Bronchopulmonary Dysplasia (BPD) is high in preterm very-low-birth-weight infants, and prematurity is one the main causes of neonatal and infant morbidity and mortality in Mexico. The objective of the study was to evaluate vitamin A status of infants at risk for BPD.
Roxana Valdés-Ramos +4 more
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Thermodynamic parameters of the binding of retinol to binding proteins and to membranes
Biochemistry, 1990Retinol (vitamin A alcohol) is a hydrophobic compound and distributes in vivo mainly between binding proteins and cellular membranes. To better clarify the nature of the interactions of retinol with these phases which have a high affinity for it, the thermodynamic parameters of these interactions were studied. The temperature-dependence profiles of the
N, Noy, Z J, Xu
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Characterization of retinol-binding protein in familial hypo-retinol-binding proteinemia.
Japanese journal of ophthalmology, 1989We reported previously familial hypo-retinol-binding proteinemia in a child who developed keratomalacia during measles infection. In the present study, we characterized serum retinol-binding proteins (RBPs) in the affected family members and compared these RBPs with those in the unaffected family members. Immunoblotting following SDS-polyacrylamide gel
T, Matsuo, N, Matsuo
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RETINOL-BINDING PROTEIN IN MALNUTRITION
The Lancet, 1979W A, Coward, P G, Lunn
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2013
Vitamin A (retinol) is essential for life; however, little is known about how it is transported into cells. Ninety-five percent of retinol found in blood is bound to Serum Retinol Binding Protein (RBP4), suggesting that RBP4 is important for transport of retinol.
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Vitamin A (retinol) is essential for life; however, little is known about how it is transported into cells. Ninety-five percent of retinol found in blood is bound to Serum Retinol Binding Protein (RBP4), suggesting that RBP4 is important for transport of retinol.
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Retinol and retinol-binding protein in lung cancer screening.
Cancer detection and prevention, 1992Human epidemiology studies demonstrate an inverse correlation between serum levels of vitamin A and the incidence of lung cancer. While such studies suggest that vitamin A may have a role in cancer prevention, the intent of this study was to investigate the use of vitamin A status parameters as markers for detection of occult lung cancer.
T E, Edes, P S, McDonald
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