Insulin receptor monoclonal antibodies that mimic insulin action without activating tyrosine kinase
HTC rat hepatoma cells were transfected with human insulin receptor cDNA to a level of 40,000 receptors/cell. In these cells, as well as in nontransfected cells, insulin stimulated the uptake of α-aminoisobutyric acid. Two monoclonal antibodies directed against the human insulin receptor α subunit,...
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Veröffentlicht in: | The Journal of biological chemistry 1989-02, Vol.264 (5), p.2438-2444 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | HTC rat hepatoma cells were transfected with human insulin receptor cDNA to a level of 40,000 receptors/cell. In these cells, as well as in nontransfected cells, insulin stimulated the uptake of α-aminoisobutyric acid. Two monoclonal antibodies directed against the human insulin receptor α subunit, like insulin, stimulated amino acid uptake in transfected HTC cells, but not in nontransfected HTC cells. The antibodies, in contrast to insulin, failed to stimulate insulin receptor tyrosine kinase activity, both in intact transfected cells and in cell free extracts prepared from them. These data suggest, therefore, that activation of insulin receptor tyrosine kinase may not be an obligatory step in all of the transmembrane signaling mechanisms of the insulin receptor. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)81632-0 |