Proteomic Analysis of Palmitoylated Proteins in Human Colon Carcinoma Tissues

Protein palmitoylation plays important roles in the occurrence,development and metastasis of colon cancer. In this study,acyl biotinyl exchange (ABE)method was improved and used to enrich palmitoylated proteins in colorectal cancer tissues. The enriched proteins were identified by proteomics approaches. A total of 213 highly reliable palmitoylated proteins(+HA/-HA >3)were identified,including enolase 1,peroxide oxidoreductase,vimentin,mitochondrial malate dehydrogenase,nuclear heterogeneous ribonucleoprotein K, and chaperone complex protein 1. The palmitoylation modification of enolase 1 was verified by Western blot analysis. The present study improved the classical ABE method to reduce its non-specific background. The detection results of palmitoylated proteins in colon cancer tissues could provide a new idea for further studying the molecular mechanism of palmitoylation of specific tumor related proteins and accurately discovering tumor markers or molecular targets of colon cancer.