Retinoic acid receptor responder protein 2(RARRES2) is a secreted protein that in humans is encoded by the RARRES2 gene. It is highly expressed in skin, also found in pancreas, liver, spleen, prostate, ovary, small intestine and colon. It is a chemoattractant protein that acts as a ligand for the G protein-coupled receptor CMKLR1. RARRES2 is secreted in an inactive form as prochemerin and is activated through cleavage of the C-terminus by inflammatory and coagulation serine proteases. It is thought to act as a cell surface receptor, found to stimulate chemotaxis of dendritic cells and macrophages to the site of inflammation. RARRES2 is inhibited in psoriatic lesions,it is activated by tazarotene in skin rafts and in the epidermis of psoriatic lesions.
RAB14 is a member of Rab GTPases that regulate the roles and identity of endosomes. Rab14 collaborates with FAM116 in regulating proteolytic cleavage of N-cadherin, and modulation of cell-cell adhesion and cell motility. Rab14 mediates the endocytic transport of GLUT4 from cytoplasmic compartments to cell surface.
Histone-binding protein RBBP4, also known as Retinoblastoma-binding protein 4, Retinoblastoma-binding protein p48, Chromatin assembly factor 1 subunit C, Chromatin assembly factor I p48 subunit, Nucleosome-remodeling factor subunit RBAP48 and RBBP4, is a nucleus protein which belongs to theWD repeat RBAP46/RBAP48/MSI1 family. RBBP4 is a core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. RBBP4 is a component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair, the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression, the nucleosome remodeling and histone deacetylase complex, which promotes transcriptional repression by histone deacetylation and nucleosome remodeling and the NURF complex. Researchers at the CUMC in New York City have found RbAp48 is responsible for age-related memory problems. By replenishing RbAp48 in the brains of mice, the researchers were able to undo existing age-related memory damage. After studying eight healthy brains donated to science by people between the ages of 33 and 88, they found that RbAp48 was reduced by nearly 50 percent in the older brains. When turned off RbAp48 in younger mice, they became more forgetful, while increasing RbAp48 in older mice restored memory.
Retinol-binding proteins (RBP) are a family of proteins with diverse functions. They are carrier proteins that bind retinol. 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.
Retinol Binding Protein 4 (RBP4) is a member of the Lipocalin family and in the blood. RBP4 is the specific vector for retinol. RBP4 is expressed and secreted by adipose tissue; and is associated with insulin resistance. RBP4 delivers retinol from the liver stores to the peripheral tissues. In plasma; the RBP-retinol complex interacts with transthyretin to prevents its loss by filtration through the kidney glomeruli. Defects in RBP4 cause retinol-binding protein deficiency and can cause night vision problems.
Retinol-binding protein 4 (RBP4) is the specific carrier for retinol (also known as vitamin A); and is responsible for the conversion of unstable and insoluble retinol in aqueous solution into stable and soluble complex in plasma through their tight interaction. As a member of the lipocalin superfamily; RBP4 containing a β-barrel structure with a well-defined cavity is secreted from the liver; and in turn delivers retinol from the liver stores to the peripheral tissues. In plasma; the RBP4-retinol complex interacts with transthyretin (TTR); and this binding is crucial for preventing RBP4 excretion through the kidney glomeruli. RBP4 expressed from an ectopic source efficiently delivers retinol to the eyes; and its deficiency affects night vision largely. Recently; RBP4 as an adipokine; is found to be expressed in adipose tissue and correlated with obesity; insulin resistance (IR) and type 2 diabetes (T2DM).
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