Monoclonal antibody alpha-chain

Clinical pharmacology Basiliximab is a chimeric (mouse/human) interleukin-2 receptor antagonist. It is directed against the interleukin-2 receptor-alpha chain (CD25) on activated T-lymphocytes, and is a potent inhibitor of interleukin-2-mediated activation of lymphocytes, a critical pathway in the cellular immune response involved in allograft rejection. Another anti-CD25 monoclonal antibody, dacUzumab (Zenapax), has the same indication as basiliximab. 

Class Immunosuppressive chimeric monoclonal antibody, specifically binds to and blocks the interleukin-2 receptor alpha chain on the surface of activated T- lymphocytes... 

Altieri DC, Edgington TS. The saturable high affinity association of factor X to ADP-stimulated monocytes defines a novel function of the Mac-1 receptor. J. Biol. Chem. 1988 263 7007-7015. Keizer GD, Visser W, Vliem M, Figdor CG. A monoclonal antibody (NKI-L16) directed against a unique epitope on the alpha-chain of human leukoc)4e function-associated antigen 1 induces homotypic ceU-ceU interactions. J. Immunol. 1988 140 1393-1400. 

Basiliximab is a chimeric (human/mouse) anti-inter-leukin-2 receptor monoclonal antibody used in the prophylaxis of acute renal transplant rejection. It acts by binding the alpha chain of interleukin-2 receptors on activated T lymphocytes. Initially positive results in phase III trials have not been generally confirmed (1,2). 

While lipoproteins are the products of many different genes, the major apolipoproteins share properties distinguishing them from most lipid-free and membrane-associated proteins. For example, apolipoproteins consist of a single polypeptide chain that has relatively little tertiary structure. Most apolipoproteins contain stretches of amphipathic alpha-helix, whose hydrophobic face can be turned to the lipid surface of the particle. The apolipoproteins are flexible, as is reflected in their unusually small free energy of unfolding. As these apolipoproteins expand and contract at the cell surface, different protein domains are exposed that are detectable with monoclonal antibodies. These properties reflect the role of apolipoproteins at the surface of lipoprotein particles whose size changes as they circulate. 

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