Results 151 to 160 of about 15,699 (195)
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Transthyretin: roles in the nervous system beyond thyroxine and retinol transport
Expert Review of Endocrinology and Metabolism, 2012Transthyretin (TTR) is a plasma- and cerebrospinal fluid-circulating protein. Besides the primordially attributed systemic role as a transporter molecule of thyroxine (T4) and retinol (through the binding to retinol-binding protein [RBP]), TTR has been recognized as a protein with important functions in several aspects of the nervous system physiology.
Maria João Saraiva +2 more
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Human Plasma Retinol Transport in Malabsorption.
Annals of Internal Medicine, 1973Excerpt Plasma vitamin A concentrations are widely used to screen for malabsorption. Isolation and characterization of the proteins responsible for plasma vitamin A transport in man—retinol-binding...
Frank Rees Smith, John Lindenbaum
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Retinol-binding protein: the transport protein for vitamin A in human plasma [PDF]
Vitamin A circulates in human plasma as retinol bound to a specific transport protein. This protein differs from the known low and high density plasma lipoproteins and has a hydrated density greater than 1.21. In order to study this protein, volunteers were injected intravenously with retinol-15-(14)C.
Amiram Raz +2 more
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Retinol Transport and Regeneration of Human Cone Photopigment
Nature New Biology, 1972A PUZZLING characteristic of fundus reflectometry data is that cone photopigment regeneration occurs more rapidly after a brief full bleach than after a prolonged full bleach1,2. The hypothesis that the relative slowness of recovery from extended photolysis results from a reduction in the store of 11-cis retinal available for photopigment synthesis1 ...
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Retinol Transport and Metabolism in Transthyretin-“Knockout” Mice
Nutrition Reviews, 2009Mice were made deficient in transthyretin (TTR), the protein that normally transports plasma retinol complexed with retinol-binding protein (RBP), by targeted mutagenesis (TTR-knockout mice). The TTR- mice were healthy and fertile, despite extremely low plasma retinol and RBP levels (6% of wild type).
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Inter- and Intracellular Transport of Retinol in the Liver
1986Following absorption and esterification by enterocytes in the small intestine, retinol is transported in lymph in chylomicrons [1]. In rats, the retinyl esters are relatively nonexchangeable components of the chylomicrons and their remnants [2]. Accordingly, nearly all the retinyl esters follow the chylomicron remnants when they are taken up by the ...
Rune Blomhoff +2 more
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Vitamin A Transport and Retinol-Binding Protein Metabolism
1975Publisher Summary This chapter elaborates the vitamin A transport and retinol-binding protein (RBP) metabolism. Vitamin A is a compound that exerts a number of important biological effects. In general, the vitamin is necessary for the support of growth and life of higher animals, since in the absence of vitamin A higher animals cease to grow, and in ...
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Specificity of the Retinol Transporter of the Rat Small Intestine Brush Border
Biochemistry, 1994The uptake of vitamin A (all-trans-retinol) by the absorptive cell of the small intestine is the necessary first step in its utilization by the organism and appears to involve a specific carrier that operates by facilitated diffusion. We investigated the specificity of that process by determining the absorption of all-trans-, 13-cis-, and 9-cis-retinol,
S E, Dew, D E, Ong
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Transport across liquid membranes containing vitamin A (retinol acetate)
Journal of Colloid and Interface Science, 2004The role of the surface activity of vitamin A has been studied in the light of the liquid membrane hypothesis of drug action. Transport of relevant amino acids such as serine, threonine, arginine, and histidine and various ions such as calcium, sodium, and potassium in the presence of liquid membranes generated by vitamin A has been studied.
A N, Nagappa +5 more
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Retinol-Binding Protein: The Serum Transport Protein for Vitamin A*
Endocrine Reviews, 1989The information available regarding the chemical structure of RBP, the structure of the RBP gene, and the expression of the RBP gene has expanded dramatically in recent years. Still many questions concerning RBP remain to be answered. The longstanding and important questions concerning the possible existence and the biochemical characteristics of the ...
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