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Chemokines are a class of small chemotactic proteins with cytokine-like functions
They are secreted by cells and induce directed chemotaxis in nearby responsive cells. Proteins are classified as chemokines based on their structural characteristics: A small size with a molecular mass of between 8-10 kDa, shared gene and amino acid sequence homology, and the presence of four cysteine residues in conserved locations.
Members of the chemokine family are divided into four groups depending on the spacing of their first two cysteine residues. The CC chemokine proteins (β-chemokines) have two adjacent cysteines near their amino terminus. The two N-terminal cysteines of CXC chemokines (α-chemokines) are separated by one amino acid. The third group, the C chemokines (γ-chemokines), is unlike all other chemokines in that it has only two cysteines; one N-terminal cysteine and one cysteine downstream. A fourth group is characterized through three amino acids between the two cysteines and is termed CX3C chemokines (δ-chemokines).
The major role of chemokines is to act as a chemoattractant to guide the migration of cells. Cells that are attracted by chemokines follow a signal of increasing chemokine concentration towards the source of the chemokine. Some chemokines are considered pro-inflammatory and can be induced during an immune response to promote cells of the immune system to a site of infection, while others are considered homeostatic and are involved in controlling the migration of cells during normal processes of tissue maintenance or development.
Chemokines are found in all vertebrates, some viruses and some bacteria, but none have been described for other invertebrates. These proteins exert their biological effects by interacting with G protein-linked transmembrane receptors called chemokine receptors that are selectively found on the surfaces of their target cells.