1. A synthetic fragment of rat transforming growth factor alpha with receptor binding and antigenic properties.
- Author
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Nestor JJ Jr, Newman SR, DeLustro B, Todaro GJ, and Schreiber AB
- Subjects
- Amino Acid Sequence, Animals, Chromatography, High Pressure Liquid, Cross Reactions, Epidermal Growth Factor metabolism, ErbB Receptors, Mice, Peptide Fragments chemical synthesis, Peptides immunology, Submandibular Gland analysis, Transforming Growth Factors, Epitopes immunology, Peptide Fragments metabolism, Peptides chemical synthesis, Receptors, Cell Surface metabolism
- Abstract
A fragment of rat transforming growth factor alpha (TGF alpha) comprising the third disulfide loop (residues 34-43) was selected as a potential antigenic and receptor binding region. Immunization of rabbits with a peptide conjugate resulted in antibodies which were specific for both the peptide and rat TGF alpha, but not for the homologous epidermal growth factor (EGF). The synthetic decapeptide exhibited low affinity for EGF receptors on human cells. Affinity was increased 100x to 0.2% of EGF or TGF alpha binding by blocking the peptide ends. The blocked decapeptide had no mitogenic activity but prevented the mitogenic effect of EGF and TGF alpha on fibroblasts. This decapeptide is an antagonist and contains an important receptor binding region of TGF alpha.
- Published
- 1985
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