Literature DB >> 2035620

Antibody-detectable changes in fibrinogen adsorption affecting platelet activation on polymer surfaces.

E Shiba1, J N Lindon, L Kushner, G R Matsueda, J Hawiger, M Kloczewiak, B Kudryk, E W Salzman.   

Abstract

Reactivity of platelets with an artificial surface exposed to whole blood is correlated with the concentration of adsorbed fibrinogen detectable by antifibrinogen antibodies. To examine the effect on platelets of the organization (distribution, orientation, conformation) of fibrinogen adsorbed on a hydrophobic surface, we studied the binding of polyclonal and monoclonal antifibrinogen antibodies to polyalkyl methacrylate polymers previously exposed to purified fibrinogen solution or diluted plasma and compared the results with platelet retention in methacrylate bead columns. There was an increase in platelet retention following diluted plasma pretreatment, which was eliminated by a polyclonal antibody against fibrinogen or against a gamma-(395-411) peptide from fibrinogen and was reduced by monoclonal antibodies (4A5, 4-2) against other COOH-terminal gamma-chain epitopes. Monoclonal antibody 10E5 against the fibrinogen receptor GpIIb/IIIa totally inhibited platelet retention in the bead columns. Our data suggest that different methacrylate polymers induce different changes in adsorbed fibrinogen, which may interfere with its interaction with platelets, and that platelet retention in a methacrylate bead column involves interaction of the COOH-terminal end of the gamma-chain of adsorbed fibrinogen with platelet GpIIb/IIIa receptors.

Entities:  

Mesh:

Substances:

Year:  1991        PMID: 2035620     DOI: 10.1152/ajpcell.1991.260.5.C965

Source DB:  PubMed          Journal:  Am J Physiol        ISSN: 0002-9513


  7 in total

1.  Substitution of the human αC region with the analogous chicken domain generates a fibrinogen with severely impaired lateral aggregation: fibrin monomers assemble into protofibrils but protofibrils do not assemble into fibers.

Authors:  Lifang Ping; Lihong Huang; Barbara Cardinali; Aldo Profumo; Oleg V Gorkun; Susan T Lord
Journal:  Biochemistry       Date:  2011-09-27       Impact factor: 3.162

2.  Ligand density dramatically affects integrin alpha IIb beta 3-mediated platelet signaling and spreading.

Authors:  Markéta Jirousková; Jyoti K Jaiswal; Barry S Coller
Journal:  Blood       Date:  2007-03-01       Impact factor: 22.113

Review 3.  Surface chemistry influences implant biocompatibility.

Authors:  Paul Thevenot; Wenjing Hu; Liping Tang
Journal:  Curr Top Med Chem       Date:  2008       Impact factor: 3.295

4.  Efficiency of platelet adhesion to fibrinogen depends on both cell activation and flow.

Authors:  A Bonnefoy; Q Liu; C Legrand; M M Frojmovic
Journal:  Biophys J       Date:  2000-06       Impact factor: 4.033

5.  Exposure of the lysine in the gamma chain dodecapeptide of human fibrinogen is not enhanced by adsorption to poly(ethylene terephthalate) as measured by biotinylation and mass spectrometry.

Authors:  Vitaliy Ovod; Evan A Scott; Megan M Flake; Stanley R Parker; Randall J Bateman; Donald L Elbert
Journal:  J Biomed Mater Res A       Date:  2011-12-30       Impact factor: 4.396

6.  Mass spectrometric mapping of fibrinogen conformations at poly(ethylene terephthalate) interfaces.

Authors:  Evan A Scott; Donald L Elbert
Journal:  Biomaterials       Date:  2007-06-19       Impact factor: 12.479

7.  Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets.

Authors:  J V Frangioni; A Oda; M Smith; E W Salzman; B G Neel
Journal:  EMBO J       Date:  1993-12       Impact factor: 11.598

  7 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.