SDF1/CXCL12 [C3]

The C-X-C or α chemokine family is characterized by a pair of cysteine residues separated by a single amino acid and primarily functions as chemoattractants for neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. The C-X-C family includes IL-8, NAP-2, MSGA and stromal cell-derived factor-1, or SDF1. SDF1 was originally described as a pre-B cell stimulatory factor, but has now been shown to function as a potent chemoattractant for T cells and monocytes, but not neutrophils. Chemoattractant active on T-lymphocytes, monocytes, but not neutrophils. SDF1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins.