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RBP1 is the carrier protein involved in the transport of retinol (vitamin A alcohol) from the liver storage site to peripheral tissue. Vitamin A is a fat-soluble vitamin necessary for growth, reproduction, differentiation of epithelial tissues, and vision. The gene harbors four exons encoding 24, 59, 33, and 16 amino acid residues, respectively.
Retinol is reversibly converted to retinal, then irreversibly to retinoic acid, which activates hundreds of genes. [9] Vitamin A deficiency is common in developing countries, especially in Sub-Saharan Africa and Southeast Asia. Deficiency can occur at any age but is most common in pre-school age children and pregnant women, the latter due to a ...
Retinal was originally called retinene, [3] and was renamed [4] after it was discovered to be vitamin A aldehyde. [5] [6] Vertebrate animals ingest retinal directly from meat, or they produce retinal from carotenoids – either from α-carotene or β-carotene – both of which are carotenes. They also produce it from β-cryptoxanthin, a type of ...
Vitamin A in food exists either as preformed retinol – an active form of vitamin A – found in animal liver, dairy and egg products, and some fortified foods, or as provitamin A carotenoids, which are plant pigments digested into vitamin A after consuming carotenoid-rich plant foods, typically in red, orange, or yellow colors. [27]
Retinol-binding proteins (RBP) are a family of proteins with diverse functions. They are carrier proteins that bind retinol . Assessment of retinol-binding protein is used to determine visceral protein mass in health-related nutritional studies.
Retinol-binding protein 4 has been a drug target for eye diseases as RBP4 is the sole carrier for retinol, which is an essential nutrient for the visual cycle. Animal studies using RBP4-antagonists showed that lowering RBP4 can lead to reduction in the accumulation of lipofuscin that leads to vision loss in eye diseases like Stargardt's disease ...
Vitamin A is necessary for proper functioning of the human eye. The photopigment rhodopsin found in human rod cells is composed of retinal, a form of vitamin A, bound to an opsin protein. [35] Upon the absorption of light rhodopsin was decomposed into retinal and opsin through bleaching. [35]
Retinal is a species of retinoid and the aldehyde form of Vitamin A. Retinal is interconvertible with retinol, the transport and storage form of vitamin A. During the visual cycle, retinal moves between several different isomers and is also converted to retinol and retinyl ester.