Anti-Phosphatidylserine Monoclonal Antibody: Structural Template for Studying Lipid-Protein Interactions and for Identificationo of Phosphatidylserine Binding Proteins

Abstract

Although phosphatidylserine (PS) is an essential component for the formation of membrane bilayers, it has been shown to contribute to many regulatory processes in biological responses (Kaibuchi et al., 1981, Zwaal et al., 1986, Madsen et al., 1989, Inoue et al., 1989). Pharmacological effects of PS have also been reported (Bruni et al., 1976, 1989). Some PS may exhibit biological activity through interacting with specific binding proteins. Some of the proteins were shown to interact with PS in a highly specific manner and precise configurations of PS molecule are required for the interaction. The typical examples are the receptor for lyso-PS on rat mast cells (Horigome et al., 1986, Chang et al., 1988), aminophospholipid translocase (Morrot et al., 1989) and protein kinase C (Lee and Bell, 1989). The PS-binding proteins so far reported are listed in Table 1. Although much effort has been focused on understanding the molecular mechanism involved in the interactions between PS and PS-binding proteins, the difficulties of handling these proteins because of their limited aqueous solubility and scarcity in the biological systems have hampered progress in this area.