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Differential Binding of Transforming Growth Factor-β1, -β2, and -β3 by Fibroblasts and Epithelial Cells Measured by Affinity Cross-Linking of Cell Surface Receptors

Russette M. Lyons^*, Duncan A. Miller, Jeannette L. Graycar, Harold L. Moses and Rik Derynck

Department of Cell Biology, Vanderbilt University School of Medicine Nashville, Tennessee 37232
Department of Developmental Biology, Genentech, Inc. South San Francisco, California 94080

Address requests for reprints to: Dr. Rik Derynck, Departments of Growth, Development, and Anatomy, Program in Cell Biology, University of California, San Francisco, California 94143-0640.

Abstract

A murine fibroblast cell line (AKR-2B clone 84A) and an epithelial cell line (BALB/MK) were compared for their ability to bind different transforming growth factor-β (TGFβ) species. The results of competitive binding assays indicated that the epithelial cells had a higher affinity for TGFβ than the fibroblasts. This difference may be the basis for the sensitivity of epithelial cells to much lower concentrations of TGF/S than fibroblasts. Affinity cross-linking studies showed that both cell types express the three cell surface TGFβ-binding molecules that have been previously described for a variety of cell types. The complexity of these cell surface binding proteins was further evaluated using all possible combinations of radiolabeled ligands in competition with each of the three unlabeled TGFβ species. Differences in the ability of specific TGFβ types to compete with radiolabeled TGFβ2 for binding to the type I and II receptors were observed, with TGFβ1 being more potent for epithelial cells, and TGFβ2 being more potent for fibroblasts. In addition, a difference in the ability of different TGFβ species to compete the [¹²⁵I] TGFβ3 from epithelial cell surface receptors was apparent. TGFβ2 was not able to compete with [¹²⁵I]TGFβ3 for binding to the type II receptor at any concentration tested, while TGFβ1 and TGFβ3 were about equally potent in competition for this receptor type. These differences in cell surface receptor binding of structurally and biologically similar molecules may reflect different functions for these molecules.

FOOTNOTES

This work was supported by Grant CA42572.

^* Present address: Genetic Therapy, Inc., 19 Firstfield Road, Gaithersburg, Maryland 20878.

Present address: Unigene Laboratories, Inc., 110 Little Falls Road, Fairfield, New Jersey 07004.

Received for publication May 30, 1991. Revision received August 7, 1991. Accepted for publication September 6, 1991.

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