Proteomic analysis of differentially expressed proteins in endothelial cells under low shear stress

Abstract Background: Shear stress (SS) affects the morphology, proliferation, differentiation and migration of endothelial cells, and regulates protein expression.Methods: This study aims to conduct a proteomic analysis of human umbilical vein endothelial cells (HUVECs) under low SS. HUVECs were cultured on glass slides (test group n=30; control group n=30) and transferred to parallel-plate flow chamber. The test group was subjected to low SS at 4.58 dyne/cm2 for 2 hours, and the control group was maintained under static conditions. Approximately 2´107 cells were collected from each group and analyzed by two-dimensional electrophoresis. The protein from each spot were identified by mass spectrometry. The biological functions and processes associated with the identified proteins were evaluated using the NCBInr, SwissProt, and DAVID databases. The protein expression of 14-3-3 proteins, annexin I, annexin II, zyxin, filamin A, filamin B, Ras-related nuclear protein (Ran), and talin were assessed by Western blotting.Results: A total of 234 proteins were analyzed; 14 proteins were upregulated and 78 were downregulated in the test group compared with the control group. The expression of 14-3-3 proteins, annexin I, annexin II, zyxin, filamin A, and filamin B was significantly decreased, whereas the expression of Ran and talin was significantly increased in the test group.Conclusion: The current results provide evidence that SS changes the protein profile of HUVECs.