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Binding of 3,5,3'-Triiodothyronine (T₃) and its Analogs to the in Vitro Translational Products of c-erbA Protooncogenes: Differences in the Affinity of the - and β-Forms for the Acetic Acid Analog and Failure of the Human Testis and Kidney -2 Products to Bind T₃

Department of Medicine, Division of Endocrinology, University of Minnesota Minneapolis, Minnesota 55455

Address requests for reprints to: Dr. Jack H. Oppenheimer, University of Minnesota, Division of Endocrinology, Department of Medicine, Box 91 UMHC, 515 Delaware Street, Southeast, Minneapolis, Minnesota 55455.

Abstract

We have compared the affinities for T₃ and the T₃ analog binding characteristics of the in vitro translational products of seven c-erbA cDNAs (chicken cerbA human placental c-erbA β rat c-erbA β-1; rat c-erbA -1; rat c-erbA -2; human testis c-erbA -2; and human kidney c-erbA -2). Four of these (chicken c-erbA , human placental c-erbA β, rat cerbA β-1, rat c-erbA -1) bound T₃with high affinity as previously described. When compared under identical conditions of synthesis and [¹²⁵I]T₃ binding, there was no significant difference between the affinity of the chicken c-erb A-1 and the human cerbA β but in a more limited series the affinity of rat c-erbA β-1 for T₃ was 4.6-fold higher than that of the rat c-erbA -1. In vitro translational products of the β-probes showed a characteristic 2.2-fold higher triiodothyroacetic acid/T₃ ratio than did the products of the -probes, regardless of the species of origin of the probe. As previously established, the rat cerbA -2 product did not bind T₃. However, in contrast to two published reports, the human testis and kidney -2 probe products also failed to bind T₃. These findings indicate that highly conserved Cterminal 37-40 residues are important for high affinity T₃ binding by proteins encoded by the c-erb A family of genes.

FOOTNOTES

This work was supported by: NIH RO1-DK19812 (to J.H.O.); NIH T32-DKO7203 (to J.H.O.); and NIH RO1-DK32885 (to C.N.M.).

Received for publication July 19, 1989. Revision received September 28, 1989. Accepted for publication October 11, 1989.

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