Daniel Rydberg

Session
Session 1
Board Number
33

Myosin and Cancer: Motor Proteins’ Correlation with Tumor Invasiveness

Several biological pathways are manipulated by cancer cells, particularly those relating to cell migration and proliferation. A key protein family in both processes is myosin proteins. Through analyzing abundances in myosin proteins across tumors, the identification of potential impacts of myosin proteins in cancer cells can be discerned. Differential myosin protein abundance patterns in relation to tumor invasiveness may indicate the manipulation of specific pathways to facilitate tumor growth and migration. Here, we perform a cross cancer proteome analysis using publicly available data from the Clinical Proteome Tumor Analysis Consortium (CPTAC) investigating the relationship between tumor invasiveness, as measured by tumor grade and cancer prognostic biomarkers, and myosin protein abundance. Five cancer types were explored for relation between invasiveness and myosin protein abundance: Clear Cell Renal Cell Carcinoma (CCRCC), Lung Squamous Cell Carcinoma (LSCC), Glioblastoma (GBM), Pancreatic Ductal Adenocarcinoma (PDA), and Breast Cancer. Key findings include the downregulation of MYO1C in CCRCC and GBM and the downregulation of MYO1D in CCRCC, PDA, and GBM as invasiveness increases. Both upregulation of MYO1C due to its function in the PI3K signaling pathway and the upregulation of MYO1D used in regulation of EGFR activity may indicate prognostic benefits for patients as shown by these findings. This study highlights proteins of interest specific to each cancer type for investigation of potential future diagnostic and therapeutic treatments in a clinical setting.