Nov 15, 1989

Identification of immunodominant regions of transforming growth factor alpha. Implications of structure and function

The Journal of Biological Chemistry
P D HoeprichJ P Tam

Abstract

Human transforming growth factor alpha (TGF alpha) is a 50-residue mitogenic peptide with a compact structure restrained by three disulfide bonds. Sequential and overlapping synthetic peptides were made to identify epitopes of TGF alpha using a panel of murine monoclonal antibodies and rabbit polyclonal antibodies. Antibodies were raised against human TGF alpha from different preparations obtained from either chemical synthesis or recombinant DNA techniques. Two related methodologies were used in these experiments. In the first method, probes were synthesized as peptides immobilized on polyethylene pins by the method of Geysen et al. (Geysen, H. M., Meloen, R. H., and Barteling, S. J. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 3998-4002). Three sets of sequentially overlapping tetrapeptides, hexapeptides, and octapeptides covering the entire length of the human TGF alpha sequence were synthesized. In the second method, a set of overlapping 8-residue synthetic peptides, freely soluble in solution, were used as probes. By both methods, the nonneutralizing monoclonal antibodies, i.e. those that did not inhibit TGF alpha in mitogenic assays, recognized two immunodominant regions represented by the NH2-terminal segment (residues 1-9) ...Continue Reading

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Mentioned in this Paper

Monoclonal Antibodies
Monoclonal antibodies, antineoplastic
Activated T Cell Autonomous Cell Death
Transforming Growth Factor Alpha Activity
Murine
Antigenic Specificity
Polyethylenes
Soluble
Recombinant DNA
Protein Conformation

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