In human blood vessel cells grown in layers, when the ribosomal protein RPL23 moves into the nucleolus, there is an increase in the release of specific inflammatory signaling molecules, and reducing...
Mechanism
Synthesis from 1 study
When artery lining cells pile up, they send a ribosomal protein into a special part of the nucleus, which turns up protein production for inflammation signals. Blocking this protein stops the inflammation signals from being made.
Most probable mechanism
When endothelial cells in the artery wall pile up on top of each other, their internal structure gets disrupted, causing a ribosomal protein called RPL23 to move into a specific region inside the nucleus. This shift boosts the cell’s ability to make proteins, especially those that signal inflammation, leading to higher levels of IL-6, MCP-1, and CXCL8 being released into the surrounding tissue.
Physical stacking of endothelial cells disrupts cytoskeletal organization and causes relocalization of Golgi components and COPII vesicles from the cytoplasm into the nucleus.
Nuclear translocation of Golgi and COPII components facilitates the movement of ribosomal protein RPL23 into the nucleolus.
Accumulation of RPL23 in the nucleolus induces nucleolar stress and enhances ribosomal biogenesis, increasing the translational capacity for inflammatory mediators.
Elevated translational activity in the nucleolus drives increased synthesis of IL-6, MCP-1, and CXCL8 mRNA and protein.
Knockdown of RPL23 or upstream trafficking components reduces nucleolar RPL23 localization and suppresses secretion of IL-6, MCP-1, and CXCL8.
Evidence from Studies
Supporting (1)
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Stacked human aortic endothelial cells induce atherosclerotic fatty streaks and release proinflammatory cytokines and chemokines
Contradicting (0)
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