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Polysialic acid (PSA) is a glycosaminoglycan (GAG) found on the surface of embryonic and cancer cells. It is a strong ligand for vascular cell adhesion molecule-1 (VCAM-1), a receptor on endothelial cells that binds lymphocytes in inflammatory lesions and in secondary lymphoid organs. PSA is synthesized by polysialyltransferases, EC 5.4.99.9, that mediate the addition of alpha2-8 or alpha2-9 sialic acid residues to the glycoprotein acceptor substrate. A combination of mutagenesis, peptide inhibition, and biochemical assays of recombinant enzymes have demonstrated that the enzymes undergo a self-consistent cycling mechanism of activity that produces alternating alpha2-8 and alpha2-9 sialyltransferase activities on the enzymes. This property is conserved in all homologues of polysialyltransferases that have been identified in various species including man, dog, mouse, and rat. Inhibition of the polysialyltransferase enzymes by the glycosylation inhibitor benzoyl per-O-acetyl-beta-D-glucosaminide is the basis for an effective strategy for the selective inhibition of PSA synthesis. PSA has been shown to block the interaction of alpha2-8(poly)-alpha2-9(poly)-linked sialo-oligosaccharides with VCAM-1. Thus, PSA functions as an inhibitor of immune cell adhesion and as a negative regulator of the inflammatory response. In humans, the expression of PSA is increased in multiple types of cancers in association with their metastatic potential, and PSA is an antigen in a vaccine that may enhance therapeutic immunity against cancer. In recent years, our knowledge of the synthesis and biological function of PSA has expanded beyond the original model of embryonic and cancer cell proliferation, and it is now clear that PSA is a normal component of the developing brain, a mediator of social behavior in the rodent, and a regulator of cell growth and differentiation
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