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Article: Intracellular protein tyrosine phosphorylation of adherent human macrophages on adsorbed fibronectin

TitleIntracellular protein tyrosine phosphorylation of adherent human macrophages on adsorbed fibronectin
Authors
KeywordsPHSRN
Peptides
Biomaterials
RGD
Polyethylene glycol
PKC
Issue Date2003
Citation
Biomaterials, 2003, v. 24, n. 7, p. 1183-1191 How to Cite?
AbstractFibronectin (FN) was pre-adsorbed onto physicochemically distinct substrates: polyethyleneglycol-based networks or tissue culture polystyrene (TCPS). The role of these substrates in modulating FN-mediated intracellular protein tyrosine phosphorylation and cell adhesion was analyzed with human primary blood derived macrophages. Although macrophage adhesion on both FN-pre-adsorbed TCPS and networks was similarly dependent on protein tyrosine kinase (PTK) and protein serine/threonine kinase (PSK), the compensation between PTK and PSK, and the involvement of signaling molecules (such as protein kinase C (PKC) isoforms) were distinct between the substrates. The pattern and the extent of tyrosine phosphorylation of several proteins (i.e. ∼70, ∼44, ∼30kDa) were differentially regulated by PKCs. FN-derived peptides were employed to probe this material-dependency in macrophage adhesion and tyrosine phosphorylation. The PHSRN domain in the peptide sequence was predominant in mediating this substrate-dependent FN signaling event. We conclude that the tyrosine phosphorylation and the cross talk between PTK and PSK are modulated by FN and the substrate onto which the protein is adsorbed. © 2002 Elsevier Science Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/216166
ISSN
2015 Impact Factor: 8.387
2015 SCImago Journal Rankings: 3.565

 

DC FieldValueLanguage
dc.contributor.authorKao, Weiyuan John-
dc.contributor.authorLiu, Yiping-
dc.date.accessioned2015-08-25T10:22:07Z-
dc.date.available2015-08-25T10:22:07Z-
dc.date.issued2003-
dc.identifier.citationBiomaterials, 2003, v. 24, n. 7, p. 1183-1191-
dc.identifier.issn0142-9612-
dc.identifier.urihttp://hdl.handle.net/10722/216166-
dc.description.abstractFibronectin (FN) was pre-adsorbed onto physicochemically distinct substrates: polyethyleneglycol-based networks or tissue culture polystyrene (TCPS). The role of these substrates in modulating FN-mediated intracellular protein tyrosine phosphorylation and cell adhesion was analyzed with human primary blood derived macrophages. Although macrophage adhesion on both FN-pre-adsorbed TCPS and networks was similarly dependent on protein tyrosine kinase (PTK) and protein serine/threonine kinase (PSK), the compensation between PTK and PSK, and the involvement of signaling molecules (such as protein kinase C (PKC) isoforms) were distinct between the substrates. The pattern and the extent of tyrosine phosphorylation of several proteins (i.e. ∼70, ∼44, ∼30kDa) were differentially regulated by PKCs. FN-derived peptides were employed to probe this material-dependency in macrophage adhesion and tyrosine phosphorylation. The PHSRN domain in the peptide sequence was predominant in mediating this substrate-dependent FN signaling event. We conclude that the tyrosine phosphorylation and the cross talk between PTK and PSK are modulated by FN and the substrate onto which the protein is adsorbed. © 2002 Elsevier Science Ltd. All rights reserved.-
dc.languageeng-
dc.relation.ispartofBiomaterials-
dc.subjectPHSRN-
dc.subjectPeptides-
dc.subjectBiomaterials-
dc.subjectRGD-
dc.subjectPolyethylene glycol-
dc.subjectPKC-
dc.titleIntracellular protein tyrosine phosphorylation of adherent human macrophages on adsorbed fibronectin-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0142-9612(02)00489-1-
dc.identifier.pmid12527259-
dc.identifier.scopuseid_2-s2.0-0037342816-
dc.identifier.volume24-
dc.identifier.issue7-
dc.identifier.spage1183-
dc.identifier.epage1191-

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