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Retinol-binding Protein
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 and retinoic acid play crucial roles in the modulation of gene expression and overall development of an embryo. However, deficit or excess of either one of these substances can cause early embryo mortality or developmental malformations. Regulation of transport and metabolism of retinol necessary for a successful pregnancy is accomplished via RBP. Retinol-binding proteins have been identified within the uterus, embryo, and extraembryonic tissue of the bovine, ovine, and porcine, clearly indicating that RBP plays a role in proper retinol exposure to the embryo and successful transport at the maternal-fetal interface. Further research is necessary to determine the exact effects of poor RBP expression on pregnancy and threshold levels f ...
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RNA-binding Protein
RNA-binding proteins (often abbreviated as RBPs) are proteins that bind to the double or single stranded RNA in cells and participate in forming ribonucleoprotein complexes. RBPs contain various structural motifs, such as RNA recognition motif (RRM), dsRNA binding domain, zinc finger and others. They are cytoplasmic and nuclear proteins. However, since most mature RNA is exported from the nucleus relatively quickly, most RBPs in the nucleus exist as complexes of protein and pre-mRNA called heterogeneous ribonucleoprotein particles (hnRNPs). RBPs have crucial roles in various cellular processes such as: cellular function, transport and localization. They especially play a major role in post-transcriptional control of RNAs, such as: splicing, polyadenylation, mRNA stabilization, mRNA localization and translation. Eukaryotic cells express diverse RBPs with unique RNA-binding activity and protein–protein interaction. According to the Eukaryotic RBP Database (EuRBPDB), there are 2 ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ...
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Carrier Protein
A membrane transport protein (or simply transporter) is a membrane protein involved in the movement of ions, small molecules, and macromolecules, such as another protein, across a biological membrane. Transport proteins are integral transmembrane proteins; that is they exist permanently within and span the membrane across which they transport substances. The proteins may assist in the movement of substances by facilitated diffusion or active transport. The two main types of proteins involved in such transport are broadly categorized as either ''channels'' or ''carriers''. The solute carriers and atypical SLCs are secondary active or facilitative transporters in humans. Collectively membrane transporters and channels are known as the transportome. Transportomes govern cellular influx and efflux of not only ions and nutrients but drugs as well. Difference between channels and carriers A carrier is not open simultaneously to both the extracellular and intracellular environments. Ei ...
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Retinol
Retinol, also called vitamin A1, is a fat-soluble vitamin in the vitamin A family found in food and used as a dietary supplement. As a supplement it is used to treat and prevent vitamin A deficiency, especially that which results in xerophthalmia. In regions where deficiency is common, a single large dose is recommended to those at high risk twice a year. It is also used to reduce the risk of complications in measles patients. It is taken by mouth or by injection into a muscle. Retinol at normal doses is well tolerated. High doses may cause enlargement of the liver, dry skin, and hypervitaminosis A. High doses during pregnancy may harm the fetus. The body converts retinol to retinal and retinoic acid, through which it acts. Dietary sources include fish, dairy products, and meat. Retinol was discovered in 1909, isolated in 1931, and first made in 1947. It is on the World Health Organization's List of Essential Medicines. Retinol is available as a generic medication and over ...
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RBP1
Retinol binding protein 1, cellular, also known as RBP1, is a protein that in humans is encoded by the ''RBP1'' gene. Function 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. The second intervening sequence alone occupies 19 kb of the 21 kb of the gene. Clinical significance Cellular retinol-binding protein-1 (CRBP-1) contributes to the maintenance of the differentiative state of endometrial cells through the regulation of bioavailability of retinol. On the converse, loss of CRBP-1 is associated with development of endometrial cancer Endometrial cancer is a cancer that arises from the endometrium (the lining of the uterus or womb). It is the result of the abnormal growth of ...
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RBP2
Retinol-binding protein 2 (RBP2) is a protein that in humans is encoded by the ''RBP2'' gene. Function RBP2 is an abundant protein present in the small intestinal epithelium. It is thought to participate in the uptake and/or intracellular metabolism of vitamin A Vitamin A is a fat-soluble vitamin and an essential nutrient for humans. It is a group of organic compounds that includes retinol, retinal (also known as retinaldehyde), retinoic acid, and several provitamin A carotenoids (most notably .... Vitamin A is a fat-soluble vitamin necessary for growth, reproduction, differentiation of epithelial tissues, and vision. RBP2 may also modulate the supply of retinoic acid to the nuclei of endometrial cells during the menstrual cycle. References Further reading * * * * * * * * External links PDBe-KBprovides an overview of all the structure information available in the PDB for Human Retinol-binding protein 2 (RBP2) {{gene-3-stub Lipocalins
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RBP3
Retinol-binding protein 3, interstitial (RBP3), also known as IRBP is a protein that in humans is encoded by the ''RBP3'' gene. RBP3 orthologs have been identified in most eutherians except tenrecs and armadillos. Function The inter- photoreceptor retinoid-binding protein is a large glycoprotein known to bind retinoids and found primarily in the interphotoreceptor matrix of the retina between the retinal pigment epithelium and the photoreceptor cells. It is thought to transport retinoids between the retinal pigment epithelium and the photoreceptors, a critical role in the visual process. Gene The human IRBP gene is approximately 9.5 kbp in length and consists of four exons separated by three introns. The introns are 1.6-1.9 kbp long. The gene is transcribed by photoreceptor and retinoblastoma cells into an approximately 4.3-kilobase mRNA that is translated and processed into a glycosylated protein of 135,000 Da. Structure The amino acid sequence of human IRBP can ...
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Retinol Binding Protein 4
Retinol binding protein 4, also known as RBP4, is a transporter protein for retinol (vitamin A alcohol). RBP4 has a molecular weight of approximately 21 kDa and is encoded by the ''RBP4'' gene in humans. It is mainly, though not exclusively, synthesized in the liver and circulates in the bloodstream as a hepatokine bound to retinol in a complex with transthyretin. RBP4 has been a drug target for ophthalmology research due to its role in vision. RBP4 may also be involved in metabolic diseases as suggested by recent studies. Function This protein belongs to the lipocalin family and is the specific carrier for retinol (vitamin A) in the blood. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, which prevents its loss by filtration through the kidney glomeruli. A deficiency of vitamin A blocks secretion of the binding protein posttranslationally and results in defective delivery and supply to the epi ...
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Extraembryonic Membrane
The extraembryonic membranes are four membranes which assist in the development of an animal's embryo. Such membranes occur in a range of animals from humans to insects. They originate from the embryo, but are not considered part of it. They typically perform roles in nutrition, gas exchange, and waste removal. There are four standard extraembryonic membranes in birds, reptiles, and mammals: the yolk sac which surrounds the yolk, the amnion which surrounds and cushions the embryo, the allantois which among avians stores embryonic waste and assists with the exchange of carbon dioxide with oxygen as well as the resorption of calcium from the shell, and the chorion which surrounds all of these and in avians successively merges with the allantois in the later stages of egg development to form a combined respiratory and excretory organ called the chorioallantois. The extraembryonic membranes in insects include a serous membrane originating from blastoderm cells, an amnion or amniot ...
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STRA6
Vitamin A receptor, Stimulated by retinoic acid 6 or STRA6 protein was originally discovered as a transmembrane cell-surface receptor for retinol-binding protein. STRA6 is unique as it functions both as a membrane transporter and a cell surface receptor, particularly as a cytokine receptor. In fact, STRA6 may be the first of a whole new class of proteins that might be known as "cytokine signaling transporters." STRA6 is primarily known as the receptor for retinol binding protein and for its relevance in the transport of retinol to specific sites such as the eye (Vitamin A). It does this through the removal of retinol (ROH) from the holo-Retinol Binding Protein (RBP) and transports it into the cell to be metabolized into retinoids and/or kept as a retinylester. As a receptor, after holo-RBP is bound, STRA6 activates the JAK/STAT pathway, resulting in the activation of transcription factor, STAT5. These two functions—retinol transporter and cytokine receptor—while using d ...
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Proteins
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues ...
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