Recombinant Human RBP1 protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Retinol binding protein 1 (RBP1) also known as cellular retinol-binding protein 1 (CRBP1) plays a critical role in the regulation and transportation of retinol a form of vitamin A within cells. RBP1 has a molecular mass of approximately 15 kDa and localizes predominantly in the cytoplasm. It is expressed in multiple tissues including the liver kidney and adipose tissue where it helps in regulating retinoid metabolism. The presence of RBP1 in these tissues is essential for maintaining physiological retinol levels.

Biological function summary

RBP1 assists in the cellular uptake storage and metabolism of retinol facilitating its conversion into retinal and retinoic acid. Although it is not part of a well-defined complex RBP1 works closely with enzymes involved in retinol metabolism such as lecithin retinol acyltransferase (LRAT) and retinal dehydrogenases. This process is important for maintaining visual function immune response and cellular differentiation which all rely on proper retinol metabolism and activity.

Pathways

RBP1 plays a significant role in the retinoic acid signaling pathway affecting gene expression regulation by modulating retinoid concentrations. It interacts with retinoic acid receptor (RAR) and retinoid X receptor (RXR) pathways influencing transcriptional activities related to development and differentiation. Connections between RBP1 and LRAT are important for the retinol esterification process integrating into broader retinoid metabolism and signaling pathways that govern cellular functions.

Dysregulation of RBP1 can contribute to conditions such as age-related macular degeneration (AMD) and metabolic syndrome. In AMD impaired retinol transport and metabolism lead to retinal damage and vision loss. In metabolic syndrome altered retinoid homeostasis involving RBP1 may exacerbate insulin resistance and obesity. Relationships with proteins like LRAT and retinaldehyde dehydrogenase (RALDH) highlight its involvement in disease mechanisms related to retinol dysfunction.