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Department of Developmental Biology, Genentech, Inc. South San Francisco, California 94080
Department of Cell Biology, Vanderbilt University School of Medicine Nashville, Tennessee 37232
Address requests for reprints to: Dr. Rik Derynck, Genentech, Inc., Department of Developmental Biology, 460 Port San Bruno Boulevard, South San Francisco, California 94080.
Abstract
Recent cDNA characterization has predicted the existence of a new member of the transforming growth factor family, transforming growth factor-β3 (TGFβ3). However, nothing is known about the biological activities of the TGFβ3 protein, since it has not been purified from any natural sources. We report here the recombinant expression in mammalian cells and the purification to apparent homogeneity of human TGFβ3. The TGFβ3 was evaluated in comparison with purified TGFβ1 and TGFβ2 in several assays for its effects on stimulation or inhibition of proliferation of mammalian cells. These analyses revealed that TGFβ3 exerts activities similar to the two other TGFβ species, but that there are distinct differences in potencies between the different TGFβ forms depending on the cell type and assay used.
INTRODUCTION: Transforming growth factor-β (TGFβ) was first identified as a factor that could stimulate some rodent fibroblast cell lines to grow in soft agar (1, 2). Subsequently, it became clear that TGFβ has a variety of biological activities in many distinct cell systems. While it can induce the proliferation of fibroblasts in monolayer, it is also a potent inhibitor of cell growth for many cell types, a modulator of differentiation, and a stimulator of extracellular matrix production and deposition (3–5). A vast majority of the biological and structural characterization studies have been performed using TGFβ purified from human platelets (6, 7).
FOOTNOTES
This work was supported in part by NIH Grant CA-42572.
Received for publication August 2, 1989. Revision received September 12, 1989. Accepted for publication September 12, 1989.
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