CD28 was identified in early 1980s by Martin and colleagues by monoclonal antibodies recognizing a 44 kDa protein on the surface of human T lymphocytes (Martin et al. 1980). Further experiments from Gmunder and Lessener evidenced the crucial role of this molecule in costimulating T cell responses by synergizing with PHA in inducing T cell proliferation (Gmunder and Lesslauer 1984). Later in 1987, Aruffo and Seed cloned the cDNA of human CD28 and showed that it encodes for a 23 kDa glycosylated type I transmembrane protein expressed as disulfide-linked homodimer on the surface of 80% of human CD4+ T cells and 50% of human CD8+ T cells (Aruffo and Seed 1987). In mouse, CD28 was cloned in 1990 by Gross and colleagues and found to be expressed 100% on both CD4+ and CD8+ T cells (Gross et al. 1990). In the same year, the natural ligands of CD28 were also identified. In...
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- Muscolini M, Camperio C, Porciello N, Caristi S, Capuano C, Viola A, et al. Phosphatidylinositol 4-phosphate 5-kinase alpha and Vav1 mutual cooperation in CD28-mediated actin remodeling and signaling functions. J Immunol. 2015;194:1323–33. https://doi.org/10.4049/jimmunol.1401643.CrossRefPubMedPubMedCentralGoogle Scholar