Multivalent cations and ligand affinity of the type 1 insulin-like growth factor receptor on P2A2-LISN muscle cells

Journal of Cellular Physiology
R H McCuskerR L Sackett

Abstract

Mouse P2A2-LISN myoblasts are transfected cells that overexpress the human type 1 insulin-like growth factor (IGF) receptor. Because the type 1 IGF receptor is the major binding site for both IGF-I and IGF-II, this cell line is an excellent model to determine the effect of multivalent cations on ligand binding specifically to this type of receptor. Competitive binding assays were performed to characterize IGF binding and Scatchard analysis to quantify affinity (Ka). 125I-IGF-I, 125I-IGF-II, and 125I-R3-IGF-I bind only to the type 1 IGF receptor on these cells. Zn2+ increased binding of the three ligands to the type 1 IGF receptor by 17 to 35%. Cd2+ significantly increased binding of 125I-IGF-I, although by only 8%. La3+ and Cr3+ did not effect binding. Au3+ decreased IGF binding by approximately 56%. Scatchard analysis produced nonlinear concave-down plots yielding binding constants for high and low affinity sites. Zn2+ increased the strength of only the high affinity sites. Au3+ decreased the affinity of both high and low affinity sites. Zn2+ increased binding with a half-maximal effect between 40 microM and 60 microM. Half-maximal dose of Au3+ was >130 microM. Zinc, gold, and cadmium bind to similar regions within proteins (a...Continue Reading

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Aug 7, 2003·The Veterinary Journal·Chris E HostetlerMark A Mirando
Jun 19, 2004·International Journal of Environmental Health Research·Francesco TomeiEnrico Tomao
Jun 2, 2011·Disease Models & Mechanisms·Sebastien ElisShoshana Yakar
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Dec 20, 2018·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Michael Francis, Arthur Grider

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