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Monoclonal antibodies are increasingly becoming a standard part of clinical cancer treatment. Monoclonal antibodies (MoAbs) represent an important part of the targeted therapy approach to treat cancer. The history of monoclonal antibodies as an immunotherapeutic option dates back to the 19th century, when the toxin from diphtheria bacteria was isolated. Improvements in technology have yielded monoclonal antibodies specific to cell surface targets and soluble growth factors.[1-3] In the last decade, the Food and Drug Administration (FDA) has approved several MoAbs for the treatment of cancer, a total of eight as of May 2006 (Table 1). Antibodies are large (180 kDa) Y-shaped molecules containing two antigen binding Fab sites (represented by the arms of the Y and known as the variable region) and an Fc segment (represented by the stem of the Y and known as the constant region) (Figure 1). MoAbs have been used to target host tissues or proteins that support tumor growth, such as growth factors and growth factor receptors. To overcome this deficiency, scientists engineered antibodies to incorporate human antibody elements, particularly in the Fc portion of the antibody. Another type of engineered antibody, the humanized antibody, is mostly human (95%-98%) with only a small portion of the variable region (Fab) containing nonhuman sequences. Examples of unconjugated MoAbs include rituximab, trastuzumab (Herceptin), cetuximab (Erbitux), and bevacizumab (Avastin).
Conjugated monoclonal antibodies have been modified by being physically attached to antitumor agents such as radioisotopes, chemotherapy drugs, toxins, or other biological agents. One of the greatest advantages of delivering therapeutics through the blood stream is that blood goes everywhere. Targeted delivery schemes aims to solve this problem by devising methods that will selectively accumulate the drug at the site of cancer. Eight monoclonal antibodies are approved by the Food and Drug Administration for the treatment of cancer in the United States.


MoAbs specifically target tumor cells and may potentially cause fewer adverse effects on normal cells.
This article reviews six of the approved anti-cancer monoclonal antibodies, their side-effect profiles, and symptom management strategies. Depending on the particular class and subtype, an antibody can interact with other serum proteins, such as the complement system, or Fc-receptors on cells to activate normal immune functions that selectively eliminate the antigen or totally eliminate the target cell expressing that antigen. Much larger chemical structures than drugs such as doxorubicin, MoAbs have very different properties and pharmacology. Monoclonal antibodies may also inhibit the binding of growth factors to their respective receptors on the cell surface and shut off downstream signaling that stimulates tumor cell growth. One type of engineered antibody, known as a chimeric antibody, is part mouse and part human.
Unconjugated monoclonal antibodies are unmodified and do not have cytotoxic agents or radioisotopes attached to them.
After targeting specific antigens, conjugated MoAbs attack tumors by releasing the attached antitumor agents into the cells or by or attracting and concentrating high levels of local radioactive emissions to the site. Another example of a conjugated MoAb is gemtuzumab ozogamicin (Mylotarg), with the anti-CD33 MoAb conjugated to the cytotoxic antibiotic g1-calecheamicin. Therefore, the medicine will reach the entire body, carried by blood through the circulation system. This will have a variety of benefits including more effective treatment, decreased side-effects and lowered dosage. The first method is to target cancer specific markers that are displayed on cancer and cancer-related cells. Oncology nurses are expected to be familiar with these agents, their indications, and their adverse effects, to provide appropriate care and symptom management to patients receiving these agents, and to adequately educate patients and families about these treatments and their specific and overlapping side effects.


The side effects of MoAbs depend on the specific target (or antigen) of the antibody, the type of cell where the antigen is expressed, and sometimes the tumor burden.
Known as complement, these serum proteins assemble into large macromolecular structures that lyse the membrane of cells that bind to the antibody. For example, doxorubicin is metabolized and excreted in 72 hours, while it is still possible to measure blood levels of the monoclonal antibody rituximab (Rituxan) 6 months after the last dose.
MoAbs with this mechanism of action are bevacizumab (Avastin), cetuximab (Erbitux), and trastuzumab (Herceptin)[1,2,6] and will be described in more detail later. The variable (Fab) portion of the mouse antibody is joined to the constant (Fc) portion of the human antibody. However, cancer therapeutics are often toxic agents that are designed to disrupt cellular processes in order to kill cancer cells. Monoclonal antibody mechanisms of action and indications, infusion guidelines, and symptom management are outlined in this article. In addition, the Fc portion of the antibody may bind to receptors on immune cells and engulf or attack the targeted cell, a phenomenon termed antibody dependent cellular cytotoxicity (ADCC).
Antigens are cell surface proteins that function as targets for binding monoclonal antibodies.
The biologic activities generated by unconjugated monoclonal antibodies are outlined in Table 2. In fact, much of the side-effects of chemotherapy are due to the cancer medication affecting the body’s normal functions.



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