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Fifteen years ago, a structural analysis of the hormone insulin and theretinoblastoma tumor suppressor protein (RB) revealed that they may physicallyinteract with one another. Subsequently, an RB peptide corresponding to theproposed RB binding site for insulin was found to recognize full-length insulinin vitro. As part of efforts aimed at developing this RB peptide into ananti-cancer drug, this molecule was chemically coupled to a cellularinternalization signal and termed "MCR peptide". Meanwhile, several such MCRpeptide variants have been demonstrated to restrain the proliferation ofdifferent human cancer cells in vitro and in vivo. Moreover, one of the MCRpeptides coined MCR-10 was shown to be capable of interfering with the complexformation between insulin and RB in HepG2 human hepatoma cells, as monitored byimmunofluorescence. This latter result indicating an in vivo associationbetween insulin and RB was confirmed by a follow-up study combining the methodsof co-immunoprecipitation and immunoblotting. Here, we provide evidence for theexistence of the insulin-RB complex in A549 human non-small cell lung cancercells. Specifically, we demonstrate this heterodimer by means of a magneticbeads-based immunoprecipitation approach and equally show that this dimer canbe disrupted by MCR-4 or MCR-10 each of which is known to possessantiproliferative properties, yet to a much lesser extent by a control peptide.Thus, this investigation has yielded another important proof for the occurrenceof the insulin-RB dimer and, furthermore, its validity as a target forantineoplastic MCR peptides.

Antiproliferative MCR peptides block physical interaction of insulin with retinoblastoma protein (RB) in human lung cancer cells