CD28 is a 44 kD disulfide-linked homodimeric type I glycoprotein. It is a member of the immunoglobulin superfamily and is also known as T44 or Tp44. CD28 is expressed on most T lineage cells, NK cell subsets, and plasma cells. CD28 binds both CD80 and CD86 using a highly conserved motif MYPPY in the CDR3-like loop. CD28 is considered a major co-stimulatory molecule, inducing T lymphocyte activation and IL-2 synthesis, and preventing cell death. In vitro studies indicate that ligation of CD28 on T cells by CD80 and CD86 on antigen presenting cells provides a costimulatory signal required for T cell activation and proliferation.
CD29 is a 130 kD single chain type I glycoprotein also known as integrin β1, VLA-β chain, or gpIIa. It is broadly expressed on a majority of hematopoietic and non-hematopoietic cells, including leukocytes (although at low level on granulocytes), platelets, fibroblasts, endothelial cells, epithelial cells, and mast cells. CD29 is a member of the integrin family. It is non-covalently associated with integrin α1-α6 chains to form VLA-1 to VLA-6 molecules, respectively. Integrins, which include CD29, bind to several cell surface (e.g. VCAM-1, MadCAM-1) and extracellular matrix molecules. CD29 acts as a fibronectin receptor and is involved in a variety of cell-cell and cell-matrix interactions.
CD32 is a 40 kD polymorphic transmembrane glycoprotein also known as FcγRII and FCRII. It is an immunoglobulin superfamily member expressed on monocytes/macrophages, granulocytes, platelets and B cells. There are at least 6 isoforms of CD32 resulting from alternative mRNA splicing. CD32 mediates phagocytosis and oxidative burst in granulocytes, as well as platelet aggregation and immunomodulation. The extracellular domain of CD32 binds to polymeric and aggregated IgG and immune complexes, while the intracellular domain has been reported to associate with SHP-1 (B1 isoform).
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