C-X-C motif chemokine ligand 16 (CXCL16)

C-X-C motif chemokine ligand 16 (CXCL16) is an atypical chemokine that exists as both a membrane-bound and a soluble protein, and it uniquely bridges immune and vascular biology. It has a complex structure with a CXC chemokine domain, a heavily glycosylated mucin-like stalk, a transmembrane segment, and a cytoplasmic tail. As a chemokine, CXCL16 is the sole ligand for the chemokine receptor CXCR6, mediating chemotactic recruitment and adhesion of immune cells such as T cells, NK cells, and NKT cells. Membrane-bound CXCL16 also acts as a scavenger receptor for phosphatidylserine and oxidized low-density lipoprotein, facilitating the uptake of apoptotic cells and pathogens by phagocytes[3][4][5][7]. CXCL16 is upregulated by pro-inflammatory cytokines (including IFN-γ and TNF-α) and is involved in disease processes such as inflammation, atherosclerosis, cancer progression, and tissue remodeling. Its serum levels have utility as a biomarker, particularly in cancer, for therapy monitoring and prognostication[2]. CXCL16's dual role as both a chemokine and scavenger receptor highlights its importance in immune cell trafficking, inflammation, and tissue homeostasis[3][4][5][7].

Other names

SCYB16SR-PSOXCXCLG16Scavenger receptor for phosphatidylserine and oxidized low density lipoproteinSmall-inducible cytokine B16Transmembrane chemokine CXCL16

Drugs modulating CXCL16 levels may exert their action by influencing immune cell recruitment, angiogenesis, and tumor microenvironment, as observed with anti-VEGF monoclonal antibodies like bevacizumab[2]. Direct inhibition or modulation of the CXCL16-CXCR6 axis could theoretically affect cell migration, adhesion, and inflammatory responses.