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Article: LC/MS identification of 12 intracellular cytoskeletal and inflammatory proteins from monocytes adherent on surface-adsorbed fibronectin-derived peptides

TitleLC/MS identification of 12 intracellular cytoskeletal and inflammatory proteins from monocytes adherent on surface-adsorbed fibronectin-derived peptides
Authors
KeywordsRGD
U937
PHSRN
Phorbol myristate acetate
Inflammation
Host response
AG18
Issue Date2008
Citation
Journal of Biomedical Materials Research - Part A, 2008, v. 85, n. 2, p. 513-529 How to Cite?
AbstractThe extent and duration of the host response determines device efficacy, yet the mechanism is poorly understood. U937 promonocytic cells were cultured on peptide-adsorbed tissue-culture polystyrene to better understand surface-modulated intracellular events. Phosphotyrosine proteins were enriched by immunoprecipitation and analyzed by nanospray HPLC-coupled tandem mass spectrometry (LC/MS). Tyrosine-phosphorylated proteins were chosen based on physiological significance and previous densitometry results, which identified a set of proteins ranging from ∼200 to ∼23 kDa showing altered phosphorylation levels in response to various surface-adsorbed ligands and phosphorylation inhibitor AG18. Although LC/MS has been used for nearly a decade, its application to the field of biomaterials is relatively novel. Twelve intracellular proteins identified by nanospray LC/MS are potentially related to the host response. Eight of the twelve proteins are related to the cytoskeleton including: moesin, heat shock protein 90β, α-tubulin, elongation factor 1α, β actin, vimentin, plasminogen activator inhibitor 2, and heterogeneous ribonuclear protein A2. The remaining four proteins: high mobility group box 1, caspase recruitment domain 5, glycoprotein 96, and heterogeneous nuclear ribonucleoprotein D0 modulate inflammation. The specific effect each peptide has upon modulating the phosphorylation state of these proteins cannot be determined from this work; however, 12 viable targets have been identified for further investigation into the role each plays in the surface-mediated monocyte response. © 2007 Wiley Periodicals, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/216193
ISSN
2015 Impact Factor: 3.263
2015 SCImago Journal Rankings: 0.979

 

DC FieldValueLanguage
dc.contributor.authorZuckerman, Sean T.-
dc.contributor.authorKao, Weiyuan John-
dc.date.accessioned2015-08-25T10:22:20Z-
dc.date.available2015-08-25T10:22:20Z-
dc.date.issued2008-
dc.identifier.citationJournal of Biomedical Materials Research - Part A, 2008, v. 85, n. 2, p. 513-529-
dc.identifier.issn1549-3296-
dc.identifier.urihttp://hdl.handle.net/10722/216193-
dc.description.abstractThe extent and duration of the host response determines device efficacy, yet the mechanism is poorly understood. U937 promonocytic cells were cultured on peptide-adsorbed tissue-culture polystyrene to better understand surface-modulated intracellular events. Phosphotyrosine proteins were enriched by immunoprecipitation and analyzed by nanospray HPLC-coupled tandem mass spectrometry (LC/MS). Tyrosine-phosphorylated proteins were chosen based on physiological significance and previous densitometry results, which identified a set of proteins ranging from ∼200 to ∼23 kDa showing altered phosphorylation levels in response to various surface-adsorbed ligands and phosphorylation inhibitor AG18. Although LC/MS has been used for nearly a decade, its application to the field of biomaterials is relatively novel. Twelve intracellular proteins identified by nanospray LC/MS are potentially related to the host response. Eight of the twelve proteins are related to the cytoskeleton including: moesin, heat shock protein 90β, α-tubulin, elongation factor 1α, β actin, vimentin, plasminogen activator inhibitor 2, and heterogeneous ribonuclear protein A2. The remaining four proteins: high mobility group box 1, caspase recruitment domain 5, glycoprotein 96, and heterogeneous nuclear ribonucleoprotein D0 modulate inflammation. The specific effect each peptide has upon modulating the phosphorylation state of these proteins cannot be determined from this work; however, 12 viable targets have been identified for further investigation into the role each plays in the surface-mediated monocyte response. © 2007 Wiley Periodicals, Inc.-
dc.languageeng-
dc.relation.ispartofJournal of Biomedical Materials Research - Part A-
dc.subjectRGD-
dc.subjectU937-
dc.subjectPHSRN-
dc.subjectPhorbol myristate acetate-
dc.subjectInflammation-
dc.subjectHost response-
dc.subjectAG18-
dc.titleLC/MS identification of 12 intracellular cytoskeletal and inflammatory proteins from monocytes adherent on surface-adsorbed fibronectin-derived peptides-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1002/jbm.a.31306-
dc.identifier.pmid17729253-
dc.identifier.scopuseid_2-s2.0-42149093968-
dc.identifier.volume85-
dc.identifier.issue2-
dc.identifier.spage513-
dc.identifier.epage529-
dc.identifier.eissn1552-4965-

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