Đang chuẩn bị nút TẢI XUỐNG, xin hãy chờ
Tải xuống
Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học General Psychiatry cung cấp cho các bạn kiến thức về ngành y đề tài: Antibody engineering to develop new antirheumatic therapies. | Available online http arthritis-research.eom content 11 3 225 Review Antibody engineering to develop new antirheumatic therapies John D Isaacs Wilson Horne Immunotherapy Centre and Musculoskeletal Research Group Institute of Cellular Medicine Newcastle University Framlington Place Newcastle-Upon-Tyne NE2 4HH UK Corresponding author John D Isaacs j.d.isaacs@ncl.ac.uk Published 19 May 2009 This article is online at http arthritis-research.com content 11 3 225 2009 BioMed Central Ltd Arthritis Research Therapy 2009 11 225 doi 10.1186 ar2594 Abstract There has been a therapeutic revolution in rheumatology over the past 15 years characterised by a move away from oral immunosuppressive drugs toward parenteral targeted biological therapies. The potency and relative safety of the newer agents has facilitated a more aggressive approach to treatment with many more patients achieving disease remission. There is even a prevailing sense that disease cure may be a realistic goal in the future. These developments were underpinned by an earlier revolution in molecular biology and protein engineering as well as key advances in our understanding of rheumatoid arthritis pathogenesis. This review will focus on antibody engineering as the key driver behind our current and developing range of antirheumatic treatments. Antibody structure function and molecular genetics a primer The biological therapy revolution was made possible by elucidation of the fine detail of the structure-function relationship in immunoglobulin molecules and the modular organisation of the underlying genes. Antibodies are essentially multidomain adapter molecules used by the immune system to neutralise and or destroy invading microorganisms and their products antigens . They do this by connecting the antigen with various effector mechanisms. At one end of the antibody molecule Figure 1 two identical variable V regions have a molecular structure that in three dimensions is highly complementary to the target .
