Retinoic Acid Receptor Responder 2 (Chemerin) (RARRES2)

Retinoic Acid Receptor Responder 2 (RARRES2), commonly known as Chemerin, is a secreted protein that functions as a potent chemoattractant and adipokine (UniProt P51460). It is synthesized as an inactive precursor, prochemerin, which requires C-terminal proteolytic cleavage by inflammatory or coagulation-related proteases to become biologically active (NCBI Gene 5919). Once activated, Chemerin serves as a high-affinity ligand for the G protein-coupled receptors CMKLR1, GPR1, and CCRL2, mediating the recruitment of immune cells like macrophages and dendritic cells to sites of inflammation (Bondue et al., 2011). Beyond its role in the immune system, Chemerin is a key regulator of adipogenesis and glucose metabolism, with high expression levels found in adipose tissue and the liver. In clinical contexts, elevated circulating levels of Chemerin are strongly associated with obesity, insulin resistance, and chronic inflammatory conditions such as psoriasis and rheumatoid arthritis (Mattern et al., 2014). Its role in oncology is complex and context-dependent; it can act as a tumor suppressor by recruiting natural killer cells or as a pro-tumorigenic factor by promoting angiogenesis and cell migration (Rourke et al., 2013). Because of its central role in linking inflammation and metabolic dysfunction, the Chemerin/CMKLR1 signaling axis is a significant target for therapeutic intervention. Current drug development efforts focus on small molecule antagonists and neutralizing antibodies to mitigate its pro-inflammatory and metabolic effects.

Other names

ChemerinTazarotene-induced gene 2 proteinTIG2HP10433Retinoic acid receptor responder protein 2

Antagonism of the Chemerin/CMKLR1 signaling pathway via ligand neutralization or receptor blockade