Abstract
It has long been known that the biological actions of peptide growth factors are mediated by cell surface receptors, but only within the last few years has intimate knowledge of these membrane glycoprotein structures become available. This new insight has been derived from isolated cDNA clones encoding numerous growth factor receptors (Morgan et al. 1987; Ullrich et al. 1984, 1985, 1986; Coussens et al. 1985; Bargmann et al. 1986 a, b; Yarden et al. 1986, 1987; Sherr et al. 1985; Nikaido et al. 1984; MacDonald et al. 1988), in combination with biochemical and immunological approaches toward receptor characterization. Amino acid sequences of growth factor receptors deduced from cDNA isolates have also provided the framework for the development of many important new reagents for their study, as exemplified by antireceptor peptide antibodies. Futhermore, the capability of expressing native and mutant receptor structures at high levels in cultured cells by transfection with plasmids harboring receptor eDNA inserts has led to the generation of excellent new cellular model systems for future studies. Recent success with the production of milligram quantities of receptor proteins that can be isolated from released baculovirus particles has also been achieved (Herrera et al. 1988). Thus, it is now reasonable to expect that major efforts designed to determine three-dimensional structures of the growth factor receptors are in progress. Such detailed information will most probably be available within the next decade.
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Czech, M.P., Clairmont, K.B., Yagaloff, K.A., Corvera, S. (1990). Properties and Regulation of Receptors for Growth Factors. In: Sporn, M.B., Roberts, A.B. (eds) Peptide Growth Factors and Their Receptors I. Handbook of Experimental Pharmacology, vol 95 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-49295-2_3
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