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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Preferential binding of insulin-like growth factors to a binding protein rather than to receptors on chicken hepatoma cell (LMH) membranes.

[125I]IGF-I binding to chicken hepatoma cell (LMH) membranes was displaced by unlabelled IGF-I or IGF-II, but not by insulin. Cross-linking revealed specific binding sites of 128 and 28-31 kDa, which following solubilization could be separated by wheat germ agglutinin (WGA) chromatography. [125I]IGF-I binding to the WGA eluate (128 kDa) could be displaced by insulin although with a 30-fold lower potency than IGF-I. Binding to the WGA flow-through (28-31 kDa) was not inhibited by insulin. This suggested that IGF binding to LMH was due mainly to membrane bound IGFBP rather than to type 1 IGF receptors. A reverse proportion was observed in normal chicken liver. A predominant 28 kDa IGFBP was synthesized and secreted by LMH cells, together with an unusual 60 kDa IGF binding entity which only bound [125I]IGF-II (with weak affinity). This process was not affected by the presence or absence of glucose, dexamethasone, glucagon, insulin or IGF-I.[1]

References

  1. Preferential binding of insulin-like growth factors to a binding protein rather than to receptors on chicken hepatoma cell (LMH) membranes. Duclos, M.J., Chevalier, B., Simon, J. Growth Regul. (1994) [Pubmed]
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