Proteomics analysis of a novel compound: cyclic RGD in breast carcinoma cell line MCF-7

Proteomics
Hsueh-Fen JuanHsuan-Cheng Huang

Abstract

In studies of cell adhesion, migration, growth, differentiation, and apoptosis, synthetic peptides containing the RGD (Arg-Gly-Asp) motif have been extensively used as the inhibitors of integrin-ligand interactions. The RGD motif is an integrin-recognition motif found in many ligands, so that the RGD-containing peptides can be used to probe integrin functions in various biological systems. A linear RGD is a tripeptide consisting of a flexible structure that makes the motif bind to its receptor with inefficient chelating affinity. Therefore, we designed a cyclic-RGD peptide (Tpa-RGDWPC, cRGD) with rigid skeleton to closely bind with its receptor. The cRGD was obtained by solid-phase peptide synthesis method using Rink amide resin. We showed that the cRGD exerts more potency than linear RGD on inhibiting cell growth of MCF-7 breast carcinoma cells. This stimulated us to question how cRGD inhibits cell growth of MCF-7 cells. Moreover, understanding what molecular mechanism underlies the effect that RGD motif exerts on MCF-7 cells is also of considerable importance. We used proteomics and bioinformatics to survey the global changes in proteins after cRGD treatment in MCF-7 cells. The classification of these proteins is shown accord...Continue Reading

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Citations

Feb 23, 2008·Journal of Proteome Research·Shui-Tein ChenChun-Ming Huang
Mar 4, 2008·Biochemical and Biophysical Research Communications·Yi-Ling Lin, Yi-Ping Hsueh
Aug 4, 2006·American Journal of Physiology. Cell Physiology·Rebecca R QuesnellBruce D Schultz
Feb 16, 2008·Journal of Proteome Research·Tsui-Chin HuangHsueh-Fen Juan

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