Abstract
Although various mouse anti-rat and rat anti-mouse monoclonal antibodies (mAbs) produce profound immunosuppressive effects, the experience with rodent anti-human mAb has been somewhat disappointing. The impetus for creating chimeric or humanized mAbs or fusion proteins to be used as immunosuppressive agents in allograft recipients stems directly from the clinical experience with rodent antihuman mAbs. With the exception of antibodies directed against proteins of the TCR/CD3 complex, murine mAbs have failed to deliver on their many potential advantages for treating or preventing rejection. The favorable attributes of chimeric or humanized mAbs include: (i) high specificity and affinity; (ii) long circulating half-lives; and (iii) a variety of mechanisms by which they can mediate an immunosuppressive effect. Cytolytic immune effector mechanisms of the host, antibody-mediated cell-mediated cytotoxicity (ADCC), and complement-mediated cytotoxicity (CDC) can theoretically be recruited directed against antibody coated target cells. Moreover, mAbs can interrupt signaling at the cell surface by blocking key receptor sites.
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Strom, T.B. (2001). Targeting the IL-2 receptor with antibodies or chimeric toxins. In: Schuurman, HJ., Feutren, G., Bach, JF. (eds) Modern Immunosuppressives. Milestones in Drug Therapy MDT. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8352-8_7
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DOI: https://doi.org/10.1007/978-3-0348-8352-8_7
Publisher Name: Birkhäuser, Basel
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