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Article: Effect of surface-adsorbed proteins and phosphorylation inhibitor AG18 on intracellular protein expression in adherent macrophages

TitleEffect of surface-adsorbed proteins and phosphorylation inhibitor AG18 on intracellular protein expression in adherent macrophages
Authors
KeywordsInflammation
U937
Tyrosine phosphorylation
Proteomics
LC/MS
Fibronectin
Issue Date2006
Citation
Biomaterials, 2006, v. 27, n. 20, p. 3745-3757 How to Cite?
AbstractMacrophages are believed to play an important role in the host inflammatory response to implanted biomaterials. However, the mechanism of macrophage adhesion to protein-adsorbed substrates and the subsequent activation and inflammation is unresolved. Previously the effect of various surface-adsorbed proteins and increasing concentrations of phosphorylation inhibitor AG18 on intracellular protein expression levels in adherent human monocytic cell line U937 was identified using SDS-PAGE and densitometry. The protein ligands and AG18 concentrations up or down regulated the expression of a set of proteins ranging from ∼200 to ∼23 kDa. In the present work, HPLC coupled tandem mass spectroscopy (LC/MS) was used to identify proteins in these bands. We hypothesized that key proteins in macrophage adhesion and activation could be identified by observing protein expression resulting from various surface-adsorbed ligands and AG18 concentrations. Increasing concentrations of AG18 down or up regulate protein expression in adherent U937 on PBS-adsorbed TCPS at ∼52, ∼42 and ∼23 kDa. AG18 concentrations had no effect on cells on albumin (Alb)-adsorbed surfaces but regulated different protein expression in adherent U937 on fibronectin (FN)-adsorbed TCPS at 40 and 80 μm AG18. Both Alb and FN regulate distinct sets of proteins in adherent cells as surface-adsorbed ligands. Based on the data from LC/MS, both surface associated ligand and increasing concentrations of AG18 modulate shifts in intracellular signaling. © 2006 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/216183
ISSN
2015 Impact Factor: 8.387
2015 SCImago Journal Rankings: 3.565

 

DC FieldValueLanguage
dc.contributor.authorZuckerman, Sean T.-
dc.contributor.authorKao, Weiyuan John-
dc.date.accessioned2015-08-25T10:22:15Z-
dc.date.available2015-08-25T10:22:15Z-
dc.date.issued2006-
dc.identifier.citationBiomaterials, 2006, v. 27, n. 20, p. 3745-3757-
dc.identifier.issn0142-9612-
dc.identifier.urihttp://hdl.handle.net/10722/216183-
dc.description.abstractMacrophages are believed to play an important role in the host inflammatory response to implanted biomaterials. However, the mechanism of macrophage adhesion to protein-adsorbed substrates and the subsequent activation and inflammation is unresolved. Previously the effect of various surface-adsorbed proteins and increasing concentrations of phosphorylation inhibitor AG18 on intracellular protein expression levels in adherent human monocytic cell line U937 was identified using SDS-PAGE and densitometry. The protein ligands and AG18 concentrations up or down regulated the expression of a set of proteins ranging from ∼200 to ∼23 kDa. In the present work, HPLC coupled tandem mass spectroscopy (LC/MS) was used to identify proteins in these bands. We hypothesized that key proteins in macrophage adhesion and activation could be identified by observing protein expression resulting from various surface-adsorbed ligands and AG18 concentrations. Increasing concentrations of AG18 down or up regulate protein expression in adherent U937 on PBS-adsorbed TCPS at ∼52, ∼42 and ∼23 kDa. AG18 concentrations had no effect on cells on albumin (Alb)-adsorbed surfaces but regulated different protein expression in adherent U937 on fibronectin (FN)-adsorbed TCPS at 40 and 80 μm AG18. Both Alb and FN regulate distinct sets of proteins in adherent cells as surface-adsorbed ligands. Based on the data from LC/MS, both surface associated ligand and increasing concentrations of AG18 modulate shifts in intracellular signaling. © 2006 Elsevier Ltd. All rights reserved.-
dc.languageeng-
dc.relation.ispartofBiomaterials-
dc.subjectInflammation-
dc.subjectU937-
dc.subjectTyrosine phosphorylation-
dc.subjectProteomics-
dc.subjectLC/MS-
dc.subjectFibronectin-
dc.titleEffect of surface-adsorbed proteins and phosphorylation inhibitor AG18 on intracellular protein expression in adherent macrophages-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.biomaterials.2006.02.028-
dc.identifier.pmid16530822-
dc.identifier.scopuseid_2-s2.0-33645960432-
dc.identifier.volume27-
dc.identifier.issue20-
dc.identifier.spage3745-
dc.identifier.epage3757-

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