File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Extended interaction of β1 integrin subunit-deficient cells (GD25) with surfaces modified with fibronectin-derived peptides: Culture optimization, adhesion and cytokine panel studies

TitleExtended interaction of β1 integrin subunit-deficient cells (GD25) with surfaces modified with fibronectin-derived peptides: Culture optimization, adhesion and cytokine panel studies
Authors
KeywordsCellular growth
Biological response
Tissue engineering
Surface structure
Polymeric biomaterial
Issue Date2008
Citation
Acta Biomaterialia, 2008, v. 4, n. 5, p. 1172-1186 How to Cite?
AbstractThe modification of biomaterials with extracellular matrix-mimicking factors is a common technique used to influence the cellular response through integrin-mediated signaling. The inherent limitations of antibody-inhibition studies necessitate the use of complementary methods to block integrin function to confirm cell-surface interaction. In this study, we employed a β1 integrin-deficient cell line, GD25, to investigate the role of β1 subunit in cell adhesion and subsequent cytokine (granulocyte macrophage colony stimulating factor; interleukin (IL)-1α; IL-1β; IL-6; monocyte chemoattractant protein-1; regulated upon activation, normal T-cell expressed, and secreted; tumor necrosis factor-α) release kinetics in the presence of tissue culture polystyrene (TCPS) and semi-interpenetrating polymer networks (sIPN) modified with fibronectin (FN)-mimic peptides (RGD, PHSRN). Culture conditions (i.e. seeding density, medium, serum supplementation) were optimized for long-term observation. Differences in cell adhesion, cell viability and cytokine release behavior were dependent on the presence of the β1 integrin subunit, FN, sIPN cast method and peptide identity. By comparing two complementary techniques for assaying integrin function, we observed both similarities (i.e. decreased adhesion to FN-absorbed TCPS and increased IL-1β release at 96 h) and differences (i.e. no difference in adhesion or IL-1β release in the presence of different sIPN surfaces) when the function of the β1 subunit was blocked in cell adhesion and signaling in the presence of biomaterials. © 2008 Acta Materialia Inc.
Persistent Identifierhttp://hdl.handle.net/10722/216195
ISSN
2015 Impact Factor: 6.008
2015 SCImago Journal Rankings: 2.020

 

DC FieldValueLanguage
dc.contributor.authorWaldeck, Heather-
dc.contributor.authorKao, Weiyuan John-
dc.date.accessioned2015-08-25T10:22:21Z-
dc.date.available2015-08-25T10:22:21Z-
dc.date.issued2008-
dc.identifier.citationActa Biomaterialia, 2008, v. 4, n. 5, p. 1172-1186-
dc.identifier.issn1742-7061-
dc.identifier.urihttp://hdl.handle.net/10722/216195-
dc.description.abstractThe modification of biomaterials with extracellular matrix-mimicking factors is a common technique used to influence the cellular response through integrin-mediated signaling. The inherent limitations of antibody-inhibition studies necessitate the use of complementary methods to block integrin function to confirm cell-surface interaction. In this study, we employed a β1 integrin-deficient cell line, GD25, to investigate the role of β1 subunit in cell adhesion and subsequent cytokine (granulocyte macrophage colony stimulating factor; interleukin (IL)-1α; IL-1β; IL-6; monocyte chemoattractant protein-1; regulated upon activation, normal T-cell expressed, and secreted; tumor necrosis factor-α) release kinetics in the presence of tissue culture polystyrene (TCPS) and semi-interpenetrating polymer networks (sIPN) modified with fibronectin (FN)-mimic peptides (RGD, PHSRN). Culture conditions (i.e. seeding density, medium, serum supplementation) were optimized for long-term observation. Differences in cell adhesion, cell viability and cytokine release behavior were dependent on the presence of the β1 integrin subunit, FN, sIPN cast method and peptide identity. By comparing two complementary techniques for assaying integrin function, we observed both similarities (i.e. decreased adhesion to FN-absorbed TCPS and increased IL-1β release at 96 h) and differences (i.e. no difference in adhesion or IL-1β release in the presence of different sIPN surfaces) when the function of the β1 subunit was blocked in cell adhesion and signaling in the presence of biomaterials. © 2008 Acta Materialia Inc.-
dc.languageeng-
dc.relation.ispartofActa Biomaterialia-
dc.subjectCellular growth-
dc.subjectBiological response-
dc.subjectTissue engineering-
dc.subjectSurface structure-
dc.subjectPolymeric biomaterial-
dc.titleExtended interaction of β1 integrin subunit-deficient cells (GD25) with surfaces modified with fibronectin-derived peptides: Culture optimization, adhesion and cytokine panel studies-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.actbio.2008.03.020-
dc.identifier.pmid18514047-
dc.identifier.scopuseid_2-s2.0-48449103197-
dc.identifier.volume4-
dc.identifier.issue5-
dc.identifier.spage1172-
dc.identifier.epage1186-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats