Summary
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1.
Antiphosphotyrosine antibodies were used to detect phosphotyrosine-containing proteins in immunoblots of bovine chromaffin cell proteins.
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2.
Unstimulated cells exhibited two major phosphotyrosine-containing proteins, which hadM r 's of 121,000 and 70,000. Insulin-like growth factor I (IGF-I) had little effect on the phosphotyrosine content of these two proteins but greatly increased the phosphotyrosine content of three other proteins ofM r 185,000, 170,000, and 96,000. These proteins were found predominantly in the particulate fraction of cell homogenates.
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3.
The effects of the IGF-I were time and concentration dependent, with maximal increases in phosphorylation occurring after 1 min of treatment with 10 nM IGF-I. Na3VO4, an inhibitor of phosphotyrosine phosphatases, potentiated the effects of IGF-I.
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4.
Thus, the IGF-I receptor appears to function as an IGF-I-activated protein tyrosine kinase in chromaffin cells. The tyrosine kinase activity of the IGF-I receptor presumably mediates the effects of IGF-I on chromaffin cell function.
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Cahill, A.L., Perlman, R.L. Phosphotyrosine-containing proteins in bovine chromaffin cells: Effects of insulin-like growth factor I (IGF-I). Cell Mol Neurobiol 11, 387–395 (1991). https://doi.org/10.1007/BF00711420
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DOI: https://doi.org/10.1007/BF00711420