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Conference Paper: Surface properties of a fibronectin derived peptide that regulates tyrosine phosphorylation

TitleSurface properties of a fibronectin derived peptide that regulates tyrosine phosphorylation
Authors
Issue Date2004
Citation
Transactions - 7th World Biomaterials Congress, 2004, p. 1321 How to Cite?
AbstractThe role of fibronectin (FN) and substrates, created from FN-derived peptides, in cell-surface interaction was examined. A relationship between substrate mediated intracellular protein tyrosine phosphorylation and cell adhesion was also found using human primary blood derived macrophages. Using western blot analysis, it was found that ∼30 kDa proteins from these macrophages were influenced by surface-bound G3PHSRNG resulting in a reduced tyrosine phosphorylation in the presence of protein kinase C9PKC) inhibitor. The substrate association was shown to allow subsequent interactions that are likely related to its unique ability to influence tyrosine phosphorylation in the presence of PKC inhibitor.
Persistent Identifierhttp://hdl.handle.net/10722/216173

 

DC FieldValueLanguage
dc.contributor.authorOlivieri, M. P.-
dc.contributor.authorMaine, R. F.-
dc.contributor.authorLink, P. A.-
dc.contributor.authorWollman, R. M.-
dc.contributor.authorKao, W. J.-
dc.contributor.authorLi, J.-
dc.date.accessioned2015-08-25T10:22:11Z-
dc.date.available2015-08-25T10:22:11Z-
dc.date.issued2004-
dc.identifier.citationTransactions - 7th World Biomaterials Congress, 2004, p. 1321-
dc.identifier.urihttp://hdl.handle.net/10722/216173-
dc.description.abstractThe role of fibronectin (FN) and substrates, created from FN-derived peptides, in cell-surface interaction was examined. A relationship between substrate mediated intracellular protein tyrosine phosphorylation and cell adhesion was also found using human primary blood derived macrophages. Using western blot analysis, it was found that ∼30 kDa proteins from these macrophages were influenced by surface-bound G3PHSRNG resulting in a reduced tyrosine phosphorylation in the presence of protein kinase C9PKC) inhibitor. The substrate association was shown to allow subsequent interactions that are likely related to its unique ability to influence tyrosine phosphorylation in the presence of PKC inhibitor.-
dc.languageeng-
dc.relation.ispartofTransactions - 7th World Biomaterials Congress-
dc.titleSurface properties of a fibronectin derived peptide that regulates tyrosine phosphorylation-
dc.typeConference_Paper-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.scopuseid_2-s2.0-13844256453-
dc.identifier.spage1321-

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