CC Chemokines

CC chemokines, a class of soluble proteins with low molecular weight (8-15 kDa) and an N-terminal CC structural domain, were originally identified as mediators of inflammatory processes and regulators of leukocyte transport. All chemokines share the same overall structure: at least three β-folded sheets, an α-helix in the C-terminal domain, and a disulfide bond connecting conserved cysteine residues. Depending on the arrangement of the first two N-terminal cysteine residues in their amino acid sequence, chemokines can be divided into four families: the CXC (or α) family, the CC (or β) family, the CX3C (or δ) family, and the C (or γ) family. Most chemokines exert their biological effects through the activation of G protein-coupled seven transmembrane receptors (GPCR). Chemokines are a class of soluble cytokines that act as chemoattractants to direct the migration of cells (especially immune cells) and are also involved in cell proliferation, differentiation and survival and are associated with a variety of human diseases, including chronic inflammation, immune dysfunction, cancer and metastasis[1][2].