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Immunohistochemical Recognition of the Epidermal Growth Factor Receptor by the h-R3 Antibody in the Skin of Experimental Animals

Maceira, Maura BSc*; Rengifo, Enrique PhD*; Cedeño, Mercedes BSc*; Merino, Nelson VMD, PhD; Parada, Angel Casacó MD, PhD*

Applied Immunohistochemistry & Molecular Morphology: December 2004 - Volume 12 - Issue 4 - p 360-363
Research Articles: Research
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The h-R3 is a humanized monoclonal antibody (Mab) that binds to the external domain of the human epidermal growth factor receptor (EGF-R). It has being used for the treatment of head and neck tumors. Since it is known that different animal species have different EGF-R amino acid sequences, it raises the handicap that, a priori, the animal species relevant for the pharmacodynamic, pharmacokinetic, and toxicologic studies of this Mab are unknown. To elucidate relevant laboratory animal species, the authors investigated the immunohistochemical recognition by h-R3 Mab of EGF-R in small skin biopsy samples obtained from NMRI nu/nu, C57Bl/6, and OF-1 mice; Sprague-Dawley rats; Hartley guinea pigs; New Zealand rabbits; and Cercopithecus aethiops and Macaca fascicularis monkeys. Additionally, three human skin biopsies were obtained from trauma victims. The immunolocalization of EGF-R in different tissue sections was performed using the avidin-biotin peroxidase complex (ABC) technique. The skin sections from different tissues were tested with the biotinylated h-R3 Mab or with a biotinylated irrelevant Mab, used as negative control. The staining intensity was qualified as:−, no staining; +, weak staining; ++, moderate staining; +++, strong staining. Macaca fascicularis monkey, New Zealand rabbit, and OF-1 mouse skins had a strong staining intensity; Cercopithecus aethiops monkey and Sprague-Dawley rat skins showed a moderate to strong staining intensity; C57Bl/6 mouse skins showed a moderate staining intensity. No staining was observed in the skins from Hartley guinea pigs and MNRI nu/nu mice. The fact that h-R3 Mab recognizes other animal EGF receptors in addition to the human EGF-R makes it possible to perform relevant pharmacodynamic, pharmacokinetic, and toxicologic studies in some laboratory animals.

From the *Center for Molecular Immunology, Havana, Cuba; and the †Institute of Pharmacy and Foods, Havana, Cuba.

Manuscript received August 26, 2003; accepted March 16, 2004.

Reprints: Angel Casacó Parada, MD, PhD, Division of Immunopharmacol-ogy, Center of Molecular Immunology, 216 Esq. a 15, Siboney, Playa, A. Postal 16040, Habana 11600, Cuba (e-mail: casaco@ict.cim.sld.cu).

© 2004 Lippincott Williams & Wilkins, Inc.