File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Either integrin subunit β1 or β3 is involved in mediating monocyte adhesion, IL-1β protein and mRNA expression in response to surfaces functionalized with fibronectin-derived peptides

TitleEither integrin subunit β1 or β3 is involved in mediating monocyte adhesion, IL-1β protein and mRNA expression in response to surfaces functionalized with fibronectin-derived peptides
Authors
KeywordsArginine-glycine-aspartic acid (RGD)
Integrin
Interleukin-1β (IL-1β)
Interpenetrating network (IPN)
Polyethylene glycol (PEG)
Issue Date2007
Citation
Journal of Biomaterials Science, Polymer Edition, 2007, v. 18, n. 6, p. 713-729 How to Cite?
AbstractWe synthesized gelatin-based, interpenetrating network (IPN) scaffolds immobilized with fibronectin (FN)-derived peptides to assess monocyte-biomaterial interaction. Human primary monocytes were seeded onto peptide-grafted IPN or tissue-culture polystyrene (TCPS) pre-adsorbed with FN or FN-derived peptides. Monocyte cell density on both TCPS and IPN surfaces was higher in the presence of the arginine-glycine-aspartic acid (RGD) peptide. Pretreatment with anti-integrin β1 or β3 antibody decreased monocyte density on all ligand-modified TCPS and IPN. Interleukin-1 β (IL-1β) protein levels of cells on modified TCPS decreased over time. IL-1β expression of monocytes in the presence of IPNs peaked at 24 h and then decreased through 168 h. Ligand identity did not affect IL-1β expression in either TCPS or IPN samples. Pretreatment with anti-integrin β1 or β3 antibody reduced IL-1β levels from both TCPS and IPN samples in a ligand-independent manner, particularly at 24 h. Monocytic IL-1β mRNA expression in IPN samples without antibody pretreatment was highest at 2 h and decreased over time. IL-1β mRNA expression in cells with anti-integrin β1 or β3 antibody pretreatment was similar to those without antibody pretreatment, except for methoxygrafted IPN samples. The change in IL-1β mRNA expression did not correlate with changes in protein expression. The results indicate that monocyte adhesion was affected by the substrate and the RGD sequence and β1 or β3 containing integrin receptors. β1- or β3-containing integrin receptors were also involved in IL-1β gene and protein expression in monocytes adhered to gelatin-based biomaterial surfaces. © 2007 VSP.
Persistent Identifierhttp://hdl.handle.net/10722/216188
ISSN
2015 Impact Factor: 1.733
2015 SCImago Journal Rankings: 0.482

 

DC FieldValueLanguage
dc.contributor.authorChung, Amy S.-
dc.contributor.authorGao, Qiang-
dc.contributor.authorKao, Weiyuan John-
dc.date.accessioned2015-08-25T10:22:18Z-
dc.date.available2015-08-25T10:22:18Z-
dc.date.issued2007-
dc.identifier.citationJournal of Biomaterials Science, Polymer Edition, 2007, v. 18, n. 6, p. 713-729-
dc.identifier.issn0920-5063-
dc.identifier.urihttp://hdl.handle.net/10722/216188-
dc.description.abstractWe synthesized gelatin-based, interpenetrating network (IPN) scaffolds immobilized with fibronectin (FN)-derived peptides to assess monocyte-biomaterial interaction. Human primary monocytes were seeded onto peptide-grafted IPN or tissue-culture polystyrene (TCPS) pre-adsorbed with FN or FN-derived peptides. Monocyte cell density on both TCPS and IPN surfaces was higher in the presence of the arginine-glycine-aspartic acid (RGD) peptide. Pretreatment with anti-integrin β1 or β3 antibody decreased monocyte density on all ligand-modified TCPS and IPN. Interleukin-1 β (IL-1β) protein levels of cells on modified TCPS decreased over time. IL-1β expression of monocytes in the presence of IPNs peaked at 24 h and then decreased through 168 h. Ligand identity did not affect IL-1β expression in either TCPS or IPN samples. Pretreatment with anti-integrin β1 or β3 antibody reduced IL-1β levels from both TCPS and IPN samples in a ligand-independent manner, particularly at 24 h. Monocytic IL-1β mRNA expression in IPN samples without antibody pretreatment was highest at 2 h and decreased over time. IL-1β mRNA expression in cells with anti-integrin β1 or β3 antibody pretreatment was similar to those without antibody pretreatment, except for methoxygrafted IPN samples. The change in IL-1β mRNA expression did not correlate with changes in protein expression. The results indicate that monocyte adhesion was affected by the substrate and the RGD sequence and β1 or β3 containing integrin receptors. β1- or β3-containing integrin receptors were also involved in IL-1β gene and protein expression in monocytes adhered to gelatin-based biomaterial surfaces. © 2007 VSP.-
dc.languageeng-
dc.relation.ispartofJournal of Biomaterials Science, Polymer Edition-
dc.subjectArginine-glycine-aspartic acid (RGD)-
dc.subjectIntegrin-
dc.subjectInterleukin-1β (IL-1β)-
dc.subjectInterpenetrating network (IPN)-
dc.subjectPolyethylene glycol (PEG)-
dc.titleEither integrin subunit β1 or β3 is involved in mediating monocyte adhesion, IL-1β protein and mRNA expression in response to surfaces functionalized with fibronectin-derived peptides-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1163/156856207781034179-
dc.identifier.scopuseid_2-s2.0-34547146840-
dc.identifier.volume18-
dc.identifier.issue6-
dc.identifier.spage713-
dc.identifier.epage729-
dc.identifier.eissn1568-5616-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats