This project started out as an academic collaboration between my laboratory in the Department of Pathology and Prof Sirpa Jalkanen's laboratory in the University of Turku, Finland. During this collaboration an engineered antibody with novel Fc receptor (FcR) and complement binding properties, and with specificity for the activation antigen VAP-1 was produced. This antibody, called HuVAP, is now in commercial development with a Finnish biotech company, BioTie Therapies Inc, Turku, Finland (see link below).
Work from Prof Jalkanen's laboratory demonstrated that VAP-1 antigen is expressed on activated vascular endothelial cells and is involved in leukocyte adhesion and migration out of the circulation and into peripheral tissues (reviewed Salmi and Jalkanen 2001). The antigen seems to be upregulated during inflammation. Antibodies which block the antigen can effectively interfere with the leukocyte adhesion and migration and thus inhibit the cycle of inflammation (Jaakkola et al 2000).
The engineered HuVAP antibody is designed to block the VAP-1 antigen and hence inhibit leukocyte migration and inhibition. We hope that then special design of the antibody Fc will retain the long biological half-life of human IgG but that it will not cause activation of human effector mechanisms normally associated with IgG binding to FcR and to complement. The antibody does still retain some binding to the inhibitory receptor called Fc-gamma-RIIb which may add additional beneficial properties to this antibody and thus make it safer in use.