Fibronectin in cell adhesion and migration via N-glycosylation

// Cheng-Te Hsiao 1, 2, * , Hung-Wei Cheng 3, * , Chi-Ming Huang 3 , Hao-Ru Li 3 , Meng-Hsin Ou 3 , Jie-Rong Huang 3 , Kay-Hooi Khoo 1, 2 , Helen Wenshin Yu 4 , Yin-Quan Chen 4 , Yang-Kao Wang 5 , Arthur Chiou 4, 6 and Jean-Cheng Kuo 3, 4, 7 1 Institute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan 2 Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan 3 Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan 4 Biophotonics and Molecular Imaging Research Center, National Yang-Ming University, Taipei 11221, Taiwan 5 Department of Cell Biology and Anatomy, National Cheng Kung University, Tainan 70101, Taiwan 6 Institute of Biophotonics, National Yang-Ming University, Taipei 11221, Taiwan 7 Proteomics Research Center, National Yang-Ming University, Taipei 11221, Taiwan * These authors have contributed equally to this work Correspondence to: Jean-Cheng Kuo, email: jckuo@ym.edu.tw Keywords: fibronectin, glycoproteomics, N-glycans, integrin signals, cell migration Received: November 04, 2016     Accepted: July 18, 2017     Published: August 07, 2017 ABSTRACT Directed cell migration is an important step in effective wound healing and requires the dynamic control of the formation of cell-extracellular matrix interactions. Plasma fibronectin is an extracellular matrix glycoprotein present in blood plasma that plays crucial roles in modulating cellular adhesion and migration and thereby helping to mediate all steps of wound healing. In order to seek safe sources of plasma fibronectin for its practical use in wound dressing, we isolated fibronectin from human (homo) and porcine plasma and demonstrated that both have a similar ability as a suitable substrate for the stimulation of cell adhesion and for directing cell migration. In addition, we also defined the N-glycosylation sites and N-glycans present on homo and porcine plasma fibronectin. These N-glycosylation modifications of the plasma fibronectin synergistically support the integrin-mediated signals to bring about mediating cellular adhesion and directed cell migration. This study not only determines the important function of N-glycans in both homo and porcine plasma fibronectin-mediated cell adhesion and directed cell migration, but also reveals the potential applications of porcine plasma fibronectin if it was applied as a material for clinical wound healing and tissue repair.