CXCL6

CXCL6 (also known as granulocyte chemotactic protein-2, GCP-2), a member of the ELR+ CXC chemokine family, is a chemoattractant for neutrophilic granulocytes and initiates chemotaxis through the chemokine receptors CXCR1 and CXCR2^[1][2]. CXCL6 exerts neutrophil-activating and angiogenic activities, and has antibacterial action against Gram-negative and Gram-positive bacteria^[3].
CXCL6 is an ELR-positive CXC chemokine with a length of 77 amino acids. The NH2-terminal glutamic acid-leucine-arginine (ELR) motif is characteristic of CXC chemokines interacting with the G-protein-coupled receptors CXCR1 and CXCR2. The ELR+ CXC family which includes IL-8, the growth-regulated oncogenes (GRO-α,-β-γ), and ENA-78. The structure of CXCL6 is >75% homologous to ENA-78, but is unique in that it binds with high-affinity to both CXCR1 and CXCR2. GCP-2, similar to IL-8, activates target cells by binding to CXCR-1 and CXCR-2. Both receptors are expressed by neutrophil granulocytes, but not by other blood-derived cells, such as lymphocytes or monocytes. Activation of endothelial cells by CXCL6 causes a mitogenic response, resulting in angiogenesis. CXCL2 is expressed by epithelial cells of the airways, eyes, gastrointestinal tract, mammary glands, tonsils, macrophages, and mesenchymal cells, in particular during inflammation. Lipopolysaccharides (LPS) and the proinflammatory cytokines TNF-α and IL-1β up-regulate the expression of CXCL6, while gamma interferon has a down-regulating effect^[1][2][3].

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