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    Extracellular Matrix Elasticity Gives Integrin a Sweet Change via a p53/miRNA-532/atp2c1 Axis

    Yan Zu1,2, Qiang Li1, Chun Yang2,*

    Molecular & Cellular Biomechanics, Vol.16, Suppl.2, pp. 106-106, 2019, DOI:10.32604/mcb.2019.07132

    Abstract Extracellular matrix (ECM) elasticity affects the function of a variety of cells. Integrins are transmembrane receptors that considered to be a sensor of cellular mechanical stimulation. The activity of integrins is strongly influenced by glycans through glycosylation events and the establishment of glycan-mediated interactions. Our study found that the level of β1 integrin N-linked glycosylation was significantly down-regulated on softer ECM. Further, sialic acid is a common monosaccharide modified at the end of the sugar chain during N-glycosylation. We subjected the enriched sialylated glycoproteins to gel-based proteomic identification by tandem mass spectrometry and found that… More >

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