Proteomic profile of cultured human endothelial cells after exposition to simulated microgravity

• Published in: Acta astronautica Vol. 179; pp. 11 - 19
• Main Authors: Kashirina, Daria N., Kononikhin, Alexey S., Ratushnyy, Andrey Yu, Nikolaev, Evgeny N., Larina, Irina M., Buravkova, Ludmila B.
• Format: Journal Article
• Language: English
• Published: Elmsford Elsevier Ltd 01.02.2021; Elsevier BV
• Subjects: Adhesion; Alanine; Apoptosis; Catabolism; Chromatography; Chromatography-mass spectrometry; Cytoskeleton; Endoplasmic reticulum; Endothelial cells; Fibers; Filaments; Gravitational effects; Intercellular adhesion; Kinases; Mass spectrometry; Microgravity; Myosin; Polypeptides; Positioning devices (machinery); Proteins; Proteome; Ribosome; Substrates; Proteome; Cytoskeleton; Ribosome; Intercellular adhesion; Endothelial cells; Chromatography-mass spectrometry
• ISSN: 0094-5765; 1879-2030
• DOI: 10.1016/j.actaastro.2020.10.014

The proteome of human umbilical vein endothelial cells (HUVEC) cultured under static conditions and simulated microgravity (sμG) using Random Positioning Machine (RPM) for 24 h was studied by chromatography-mass spectrometry. It was revealed that the percentage of ribosomal proteins and proteins involved in intercellular adhesion, regulation of actin cytoskeleton, various pathways of cell signaling mediated by G-proteins, apoptosis and ubiquitin-dependent protein catabolism increased under sμG. At the same time the number of proteins associated with cell growth reduced. A significant increase in the peak intensities of proteins associated with maintaining the cytoskeleton and stress fibers (myristoylated alanine-rich C-kinase substrate, filamin-A, alpha-actinin-1 and myosin light polypeptide 6) and proteins involved in response to unfolded protein (serpin H1, 78 kDa glucose-regulated protein, transitional endoplasmic reticulum ATPase) was shown. At the same time, a significant decrease in the peak intensity of cofilin 1, which is capable of breaking actin filaments, was revealed. Thus, the most pronounced effect of microgravity is on the proteins associated with the actin cytoskeleton, as well as on adhesion proteins, whose properties also depend on the structure of the cytoskeleton. At the same time, the number of proteins which prevent improper protein folding increases, and the translation apparatus is rearranged under sμG. •HUVEC proteins of cytoskeleton and stress fibers increase in microgravity during 24 h.•Translation apparatus is rearranged in simulated microgravity (μG).•The number of proteins that prevent improper protein folding is increased in μG.