Trastuzumab, cancer monoclonal antibody therapy

While no biopharmaceutical is approved with the requirement of genotyping as a part of its therapeutic indication, a recently approved monoclonal antibody therapy against breast cancer, trastuzumab (Herceptin), is indicated only for those tumors measurably expressing the protein expressed by the gene erbB-2. Because the oncogene product of erbB-2 is elevated... 

Trastuzumab exemplifies a growing number of monoclonal antibodies that have become available for antineoplastic therapy. These are directed against cell surface proteins that are strongly expressed by cancer cells. Trastuzumab binds to HER2, the recep-Luellmann, Color Atlas of Pharmacology All rights reserved. Usage subject to terms... 

Trastuzumab (Herceptin) is a humanized monoclonal antibody against the HER2/neu (ErbB-2) member of the epidermal growth factor family of cellular receptors. The internal domain of the HER2/neu glycoprotein encodes a tyrosine kinase that activates downstream signals and enhances metastatic potential and inhibits apoptosis. HER2/neu is overexpressed in up to 30% of breast cancers and is associated with clinical resistance to cytotoxic and hormone therapy. A number of mechanisms of action have... 

Another case of already practical use of pharmacogenetic methods is the test for mutations in tumors that overexpress the human EGFR, HER2. Trastuzumab, a humanized monoclonal antibody, is effective in only 10-15% of breast cancer patients whose tumors overexpress HER2 [67]. Therefore, the pretreatment detection of HER2 is essential for the trastuzumab therapy. 

Trastuzumab (Herceptin , Genentech) is a monoclonal antibody that binds the cell surface HER2/neu (erbB2) receptor and is used in the therapy of erbB2 + breast cancer. 

Over the past decade, a wide variety of antibody-based targeting molecules have been assessed for their potential application in cancer therapy [200]. Monoclonal antibodies (mAb) were the first and are still the preferred class of targeting molecules. Current developments of antibodies have been focused on chimeric, humanized, and fully humanized derivatives to decrease their immunogenicity. Some of these antibody-based drugs have already undergone clinical development and have been successfully translated into the clinical environment. Such examples include rituximab (Rituxan ), trastuzumab (Herceptin ), cetuximab (Erbitux ), and bevacizumab (Avastin ). Rituximab was approved by the FDA for treating B-cell lymphoma in 1997. 

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