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Receptor-mediated effects on ligand availability influence relative mitogenic potencies of epidermal growth factor and transforming growth factor α

✍ Scribed by Cartikeya C. Reddy; Alan Wells; Douglas A. Lauffenburger

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
639 KB
Volume
166
Category
Article
ISSN
0021-9541

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✦ Synopsis

formed cells, it is also produced by a variety of normal cells in mammals, suggesting an important physiological role for TGFa (reviewed by Derynck, 1992). Human EGF and TGFa share 42% amino acid sequence homol-0 1996 WILEY-LISS, INC. ogy (Carpenter and Wahl, 1990) and are believed to exhibit similar three-dimensional configurations based on N M R studies in solution (Montelione e t al., 1989; Campbell e t al., 1990). They readily compete with each other for binding to the epidermal growth factor recept o r (EGFR), and it i s generally believed that they transmit their actions through this common receptor (Carpenter e t al., 1983; Massague, 1983; Ebner and Derynck, 1991). The EGFR i s a 170 kD transmembrane tyrosine kinase which gets activated upon growth factor binding and initiates intracellular signaling cascades (Carpenter and Wahl, 1990). While EGF and TGFa have been reported t o elicit

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