File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1016/j.biomaterials.2006.02.028
- Scopus: eid_2-s2.0-33645960432
- PMID: 16530822
- WOS: WOS:000237346000007
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Effect of surface-adsorbed proteins and phosphorylation inhibitor AG18 on intracellular protein expression in adherent macrophages
Title | Effect of surface-adsorbed proteins and phosphorylation inhibitor AG18 on intracellular protein expression in adherent macrophages |
---|---|
Authors | |
Keywords | Inflammation U937 Tyrosine phosphorylation Proteomics LC/MS Fibronectin |
Issue Date | 2006 |
Citation | Biomaterials, 2006, v. 27, n. 20, p. 3745-3757 How to Cite? |
Abstract | Macrophages 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 Identifier | http://hdl.handle.net/10722/216183 |
ISSN | 2023 Impact Factor: 12.8 2023 SCImago Journal Rankings: 3.016 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Zuckerman, Sean T. | - |
dc.contributor.author | Kao, Weiyuan John | - |
dc.date.accessioned | 2015-08-25T10:22:15Z | - |
dc.date.available | 2015-08-25T10:22:15Z | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | Biomaterials, 2006, v. 27, n. 20, p. 3745-3757 | - |
dc.identifier.issn | 0142-9612 | - |
dc.identifier.uri | http://hdl.handle.net/10722/216183 | - |
dc.description.abstract | Macrophages 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.language | eng | - |
dc.relation.ispartof | Biomaterials | - |
dc.subject | Inflammation | - |
dc.subject | U937 | - |
dc.subject | Tyrosine phosphorylation | - |
dc.subject | Proteomics | - |
dc.subject | LC/MS | - |
dc.subject | Fibronectin | - |
dc.title | Effect of surface-adsorbed proteins and phosphorylation inhibitor AG18 on intracellular protein expression in adherent macrophages | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.biomaterials.2006.02.028 | - |
dc.identifier.pmid | 16530822 | - |
dc.identifier.scopus | eid_2-s2.0-33645960432 | - |
dc.identifier.volume | 27 | - |
dc.identifier.issue | 20 | - |
dc.identifier.spage | 3745 | - |
dc.identifier.epage | 3757 | - |
dc.identifier.isi | WOS:000237346000007 | - |
dc.identifier.issnl | 0142-9612 | - |