Cargando…
Fibronectin in cell adhesion and migration via N-glycosylation
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 adhe...
Autores principales: | , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Impact Journals LLC
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5642584/ https://www.ncbi.nlm.nih.gov/pubmed/29050309 http://dx.doi.org/10.18632/oncotarget.19969 |
_version_ | 1783271396752752640 |
---|---|
author | Hsiao, Cheng-Te Cheng, Hung-Wei Huang, Chi-Ming Li, Hao-Ru Ou, Meng-Hsin Huang, Jie-Rong Khoo, Kay-Hooi Yu, Helen Wenshin Chen, Yin-Quan Wang, Yang-Kao Chiou, Arthur Kuo, Jean-Cheng |
author_facet | Hsiao, Cheng-Te Cheng, Hung-Wei Huang, Chi-Ming Li, Hao-Ru Ou, Meng-Hsin Huang, Jie-Rong Khoo, Kay-Hooi Yu, Helen Wenshin Chen, Yin-Quan Wang, Yang-Kao Chiou, Arthur Kuo, Jean-Cheng |
author_sort | Hsiao, Cheng-Te |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5642584 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Impact Journals LLC |
record_format | MEDLINE/PubMed |
spelling | pubmed-56425842017-10-18 Fibronectin in cell adhesion and migration via N-glycosylation Hsiao, Cheng-Te Cheng, Hung-Wei Huang, Chi-Ming Li, Hao-Ru Ou, Meng-Hsin Huang, Jie-Rong Khoo, Kay-Hooi Yu, Helen Wenshin Chen, Yin-Quan Wang, Yang-Kao Chiou, Arthur Kuo, Jean-Cheng Oncotarget Research Paper 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. Impact Journals LLC 2017-08-07 /pmc/articles/PMC5642584/ /pubmed/29050309 http://dx.doi.org/10.18632/oncotarget.19969 Text en Copyright: © 2017 Hsiao et al. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/) 3.0 (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Paper Hsiao, Cheng-Te Cheng, Hung-Wei Huang, Chi-Ming Li, Hao-Ru Ou, Meng-Hsin Huang, Jie-Rong Khoo, Kay-Hooi Yu, Helen Wenshin Chen, Yin-Quan Wang, Yang-Kao Chiou, Arthur Kuo, Jean-Cheng Fibronectin in cell adhesion and migration via N-glycosylation |
title | Fibronectin in cell adhesion and migration via N-glycosylation |
title_full | Fibronectin in cell adhesion and migration via N-glycosylation |
title_fullStr | Fibronectin in cell adhesion and migration via N-glycosylation |
title_full_unstemmed | Fibronectin in cell adhesion and migration via N-glycosylation |
title_short | Fibronectin in cell adhesion and migration via N-glycosylation |
title_sort | fibronectin in cell adhesion and migration via n-glycosylation |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5642584/ https://www.ncbi.nlm.nih.gov/pubmed/29050309 http://dx.doi.org/10.18632/oncotarget.19969 |
work_keys_str_mv | AT hsiaochengte fibronectinincelladhesionandmigrationvianglycosylation AT chenghungwei fibronectinincelladhesionandmigrationvianglycosylation AT huangchiming fibronectinincelladhesionandmigrationvianglycosylation AT lihaoru fibronectinincelladhesionandmigrationvianglycosylation AT oumenghsin fibronectinincelladhesionandmigrationvianglycosylation AT huangjierong fibronectinincelladhesionandmigrationvianglycosylation AT khookayhooi fibronectinincelladhesionandmigrationvianglycosylation AT yuhelenwenshin fibronectinincelladhesionandmigrationvianglycosylation AT chenyinquan fibronectinincelladhesionandmigrationvianglycosylation AT wangyangkao fibronectinincelladhesionandmigrationvianglycosylation AT chiouarthur fibronectinincelladhesionandmigrationvianglycosylation AT kuojeancheng fibronectinincelladhesionandmigrationvianglycosylation |