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Article: Human macrophage adhesion on fibronectin: The role of substratum and intracellular signalling kinases

TitleHuman macrophage adhesion on fibronectin: The role of substratum and intracellular signalling kinases
Authors
KeywordsPHSRN
Biomaterials
RGD
Protein kinase
Polyethyleneglycol
Issue Date2002
Citation
Cellular Signalling, 2002, v. 14, n. 2, p. 145-152 How to Cite?
AbstractFibronectin and Arg-Gly-Asp (RGD)- and/or Pro-His-Ser-Arg-Asn (PHSRN)-containing oligopeptides were immobilized onto physicochemically distinct substrata: polyethyleneglycol-based networks or tissue culture polystyrene (TCPS). The role of selected signalling kinases in the adhesion of human primary blood-derived macrophages on these modified substrata was investigated. We demonstrated that the protein tyrosine kinase (PTK) or protein serine/threonine kinase (PSK) dependency and the PTK-PSK cross-talk compensation for macrophage adhesion varied dynamically with the substratum modification and the culture time. The inhibition of MAPK kinase (MAPKK) decreased macrophage adhesion on TCPS, whereas the inhibition of phosphoinositide-3 kinase (PI3 kinase) decreased macrophage adhesion on networks at 24 h. The PI3 kinase-protein kinase C (PKC)-MAPK cascade was involved in macrophage adhesion on fibronectin-preadsorbed TCPS or networks but not on fibronectin-grafted networks. This fibronectin-mediated adhesion signalling involved both RGD and PHSRN sequences in a form of G3RGDG6PHSRNG on TCPS but not on networks. Furthermore, G3RGDG6PHSRNG grafted onto networks evoked unique signalling in macrophage adhesion from that preadsorbed onto networks. Thus, macrophage adhesion and the role of selected signalling kinases were modulated by the substratum and the ligand conjugation method. © 2002 Elsevier Science Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/216161
ISSN
2015 Impact Factor: 4.191
2015 SCImago Journal Rankings: 2.289

 

DC FieldValueLanguage
dc.contributor.authorLiu, Yiping-
dc.contributor.authorKao, Weiyuan John-
dc.date.accessioned2015-08-25T10:22:05Z-
dc.date.available2015-08-25T10:22:05Z-
dc.date.issued2002-
dc.identifier.citationCellular Signalling, 2002, v. 14, n. 2, p. 145-152-
dc.identifier.issn0898-6568-
dc.identifier.urihttp://hdl.handle.net/10722/216161-
dc.description.abstractFibronectin and Arg-Gly-Asp (RGD)- and/or Pro-His-Ser-Arg-Asn (PHSRN)-containing oligopeptides were immobilized onto physicochemically distinct substrata: polyethyleneglycol-based networks or tissue culture polystyrene (TCPS). The role of selected signalling kinases in the adhesion of human primary blood-derived macrophages on these modified substrata was investigated. We demonstrated that the protein tyrosine kinase (PTK) or protein serine/threonine kinase (PSK) dependency and the PTK-PSK cross-talk compensation for macrophage adhesion varied dynamically with the substratum modification and the culture time. The inhibition of MAPK kinase (MAPKK) decreased macrophage adhesion on TCPS, whereas the inhibition of phosphoinositide-3 kinase (PI3 kinase) decreased macrophage adhesion on networks at 24 h. The PI3 kinase-protein kinase C (PKC)-MAPK cascade was involved in macrophage adhesion on fibronectin-preadsorbed TCPS or networks but not on fibronectin-grafted networks. This fibronectin-mediated adhesion signalling involved both RGD and PHSRN sequences in a form of G3RGDG6PHSRNG on TCPS but not on networks. Furthermore, G3RGDG6PHSRNG grafted onto networks evoked unique signalling in macrophage adhesion from that preadsorbed onto networks. Thus, macrophage adhesion and the role of selected signalling kinases were modulated by the substratum and the ligand conjugation method. © 2002 Elsevier Science Inc. All rights reserved.-
dc.languageeng-
dc.relation.ispartofCellular Signalling-
dc.subjectPHSRN-
dc.subjectBiomaterials-
dc.subjectRGD-
dc.subjectProtein kinase-
dc.subjectPolyethyleneglycol-
dc.titleHuman macrophage adhesion on fibronectin: The role of substratum and intracellular signalling kinases-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0898-6568(01)00246-7-
dc.identifier.pmid11781139-
dc.identifier.scopuseid_2-s2.0-0036141244-
dc.identifier.volume14-
dc.identifier.issue2-
dc.identifier.spage145-
dc.identifier.epage152-

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