ABSTRACT
This chapter provides a short history of the discovery of the lipocortin family, establish their relationship to other previously described calcium phospholipid-binding proteins, and reviews what is known about six members of this family. Lipocortins were first discovered as potential mediators of steroid action. Anti-inflammatory steroids inhibit the production of eicosanoids by inhibiting the release of arachidonic acid. Primary sequence analysis has revealed that there are at least six distinct lipocortins (I-VI), all of which are calcium phospholipid-binding proteins, inhibit fourfold domain structure, and are between 40 and 50% homologous. The epidermal growth factor receptor is a membrane-associated protein tyrosine kinase, which when activated through the binding of epidermal growth factor, phosphorylates cellular proteins that may have important roles in growth regulation. The discovery of the lipocortin family of calcium phospholipid-binding proteins has established an important link in the signal transduction process.
