Large-Scale Analysis of Breast Cancer-Related Conformational Changes in Proteins Using Limited Proteolysis.

ABSTRACT: Conformational changes in proteins can lead to disease. Thus, methods for identifying conformational changes in proteins can further improve our understanding and facilitate detection of disease states. Here we combine limited proteolysis (LiP) with Stable Isotope Labeling with Amino Acids in Cell Culture (SILAC) to characterize breast cancer-related conformational changes in proteins on the proteomic scale. Studied here are the conformational properties of proteins in two cell culture models of breast cancer, including the MCF-10A and MCF-7 cell lines. The SILAC-LiP approach described here identified ∼200 proteins with cell-line-dependent conformational changes, as determined by their differential susceptibility to proteolytic digestion using the nonspecific protease, proteinase K. The pr

SUBMITTER: Liu F 

PROVIDER: S-EPMC5270647 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature