Oxidative cross-linking of fibronectin confers protease resistance and inhibits cellular migration
Morgan L. Locy, Sunad Rangarajan, Yang Sufen, Mark R. Johnson, Karen Bernard, Ashish Kurundkar, Nathaniel B. Bone, Jaroslaw W. Zmijewski, Jaeman Byun, Subramaniam Pennathur, Yong Zhou, Victor J. Thannickal
Abstract
-dityrosine-modified fibronectin was increased in a murine model of lung fibrosis and in human subjects with interstitial lung disease compared to that in control healthy subjects. These studies indicate that tyrosine can undergo stable, covalent linkages in fibrillar fibronectin under inflammatory conditions and that this modification affects the migratory behavior of cells on such modified matrices, suggesting that this modification may play a role in both physiologic and pathophysiologic tissue repair.
Topics & Concepts
FibronectinProteaseCell biologyOxidative phosphorylationOxidative stressChemistryBiologyBiochemistryCellEnzymeProtease and Inhibitor MechanismsCell Adhesion Molecules ResearchS100 Proteins and Annexins