retinol-binding protein

Retinol (Alphalin) and derivatives of retinol that play an essential role in metabolic functioning of the retina, the growth of and differentiation of epithelial tissue, the growth of bone, reproduction, and the immune response. Dietary vitamin A is derived from a variety of CAROTENOIDS found in plants. It is enriched in the liver, egg yolks, and the fat component of dairy products.

BPN-14136 is a potent antagonist of retinol-binding protein 4 (RBP4), utilized in mechanistic studies of retinoid transport, metabolic disorders BPN-14136 is used in the research for RBP4-driven pathophysiology, particularly in the context of insulin resistance and metabolic disease models.

A 1120 is a nonretinoid retinol-binding protein 4 (RBP4) antagonist (Ki: 8.3 nM), which disrupts the interaction between RBP4 and its binding partner transthyretin.

9-cis-Retinal is a retinoid with Kd of 8 nM and 5 nM for cellular retinol binding protein-I (CRBP-1) and CRBP-II, respectively. 9-cis-Retinal accelerates the differentiation and maturation of rod photoreceptors in retinal organoids, reduces the toxicity of unliganded opsins, and can be used to study congenital stationary night blindness caused by G90D rhodopsin.

STG-001 is an antagonist of retinol-binding protein 4 (RBP4). By inhibiting RBP4, STG-001 reduces the synthesis of retinaldehyde and bis-retinoids, thereby preventing photoreceptor degeneration. This compound is applicable in studies related to sex-linked hereditary retinopathies such as Stargardt disease (STGD).

RBP4 inhibitor 1 (compound 43b) is an orally active and potent inhibitor of retinol-binding protein 4 (RBP4) with IC50 values of 28 nM and 110 nM for human and mouse RBP4, respectively. It effectively reduces blood RBP4 levels in mice, providing a long-lasting effect [1].

RBP4 ligand-1 is a non-retinoid ligand for retinol-binding protein 4 (RBP4). It exhibits hRBP4SPA IC50 and RBP4-TTR FRET IC50 values of 0.23±0.11 μM and 0.13±0.12 μM, respectively, in radioligand binding and FRET assays. The measured concentration was 0.12 μM.

Interphotoreceptor retinoid-binding protein (1-20) (IRBP1-20), a dodecapeptide fragment of retinoid-binding protein 3, plays a crucial role in pigment regeneration by facilitating the transport of retinol and retinal between photoreceptor cells and the retinal pigment epithelium. It has been utilized to provoke autoimmune uveoretinitis in C57BL/6 mice, possessing the H-2b haplotype. Furthermore, IRBP1-20 at a concentration of 3 µM enhances the secretion of IL-4, IL-5, and IL-6 from primary mouse spleen lymphocytes. Immunization and subsequent rechallenge with IRBP1-20 lead to increased ear swelling, inflammation of ocular blood vessels, infiltration by immune cells, damage to the photoreceptor layer, and retinal detachment in IFN-γ-deficient mice.

Interphotoreceptor retinoid-binding protein (651-670) (IRBP651-670), a peptide fragment of retinoid-binding protein 3 (also known as IRBP), plays a crucial role in the visual cycle by facilitating the transport of retinol and retinal between photoreceptor cells and the retinal pigment epithelium. This transport is essential for the regeneration of pigments necessary for vision. When administered at a dose of 300 µg/animal, IRBP651-670 induces autoimmune uveoretinitis in C57BL/6 mice, a model possessing the H-2b haplotype. This immunization leads to increased levels of ocular cytokines including IL-1β, IL-6, IL-17, TNF-α, and IFN-γ, promotes immune cell infiltration into the eye, and results in photoreceptor cell damage.