![]() ![]() 19, May 6, 1996, Columbus, Ohio, abstract No. Miura et al., “Different effects on mitogensis and transformation of a mutation at tyrosine 1251 of the insulin-like growth factor I receptor”, Journal of Biological Chemistry., vol. Miura et al, Biochemical and Biophysical Research Communications 239: 182-185, 1997.* Ngo et al, 1994, The Protein Folding Problem and Tertiary Structure Prediction, pp. The compositions and methods of the invention are useful for modulating apoptosis in vertebrate cells. Surprisingly, receptors truncated at the C-terminus had enhanced anti-apoptotic function. In the C-terminus of the IGF-IR, mutation at tyrosine 1251 and at histidine 1293 and lysine 1294 abolished apoptotic function, whereas mutation of the four scrines at 1280-1283 did not affect survival. However, mutations at tyrosine residue 950 or in the tyrosine cluster (1131, 1135, and 1136) in the kinase domain resulted in receptors that retained survival function. ![]() An IGF-I receptor with a mutation at the ATP-binding site did not provide protection from apoptosis. Under the same conditions, IGF-I did not have a significant mitogenic effect on FL5.12 cells expressing IGF-I receptors. In FL5.12 cells transfected with wild type IGF-I receptors, IGF-I provided protection from IL-3 withdrawal analogous to the protection afforded by expression of Bcl-2. ![]() Active Survival Domains in the Insulin-like Growth Factor-I Receptor (IGF-IR) required for transmitting the survival signal in vertebrate cells have been identified. ![]()
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