CD30/TNFRSF8 Fc Chimera Protein, Human

CD30, a 120 kDa cytokine receptor and transmem-brane glycoprotein, is a member of the tumor necrosis factor (TNF) receptor superfamily. The protein is comprised of an extracellular domain, a transmembrane region and a cytoplasmic domain. The majority of antibodies against human CD30 recognize epitopes within the extracellular domain. The soluble form of CD30 has a molecular weight (85 kDa) produced through proteolytic cleavage releasing the extracellular domain. Binding of CD30 with its receptor ligand activates TNF receptor-associated factor (TRAF)2 and TRAF5, initiating signal transduction pathways that can lead either to proliferation or apoptosis; CD30 induced apoptosis may lead to the self-regression seen in lymphomatoid papulosis lesions, whereas proliferation may result in anaplastic large-cell lymphoma (ALCL). The expression of CD30 by malignant lymphocytes affords an opportunity as a therapeutic target. Because CD30 is not found in most normal tissues outside of the immune system or on resting monocytes or lymphocytes, it provides an ideal target for immunotherapy. While it has been demonstrated that anti-CD30 antibodies alone display therapeutic efficacy, newer agents markedly enhance antibody effectiveness through their conjugation with various cytotoxic agents. Therefore, CD30 can serve both as a diagnostic marker for lymphocyte malignancies and as a target for therapy.