Thomas A. Horbett

University of Washington

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Buddy D. Ratner

University of Washington

Allan S. Hoffman

University of Washington

John L. Brash

McMaster University

Jack E. Lemons

University of Alabama at Birmingham

Paul Ducheyne

University of Pennsylvania

Jan Feijén

University of Twente

Robert Baier

University at Buffalo, State University of New York

James M. Anderson

Case Western Reserve University

Larry L. Hench

Florida Institute of Technology

Pratima Bajpai

Central Pulp & Paper Research Institute

Cooperative Institutions

Case Western Reserve University

469

Cornell University

335

University of Leeds

252

University Hospitals of Cleveland

136

John Wiley & Sons (United States)

116

University of Washington

100

Harvard University

Walker (United States)

Brigham and Women's Hospital

Cleveland Research (United States)

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Radiofrequency plasma deposition of oxygen‐containing films on polystyrene and poly(ethylene terephthalate) substrates improves endothelial cell growth

Journal of Biomedical Materials Research (1990)

Sylvie I. Ertel Buddy D. Ratner Thomas A. Horbett

Abstract Polystyrene and poly(ethylene terephthalate) substrates were modified by radiofrequency plasma deposition with organic vapors comprised of carbon, oxygen, and hydrogen (acetone, methanol, glutaraldehyde, formic acid, allyl alcohol, and ethylene oxide). The treatments resulted in the deposition of a film at least 100 Å thick containing up to 26% atomic oxygen at the surface. A high oxygen incorporation was observed for vapors with a large oxygen‐to‐carbon ratio. Bovine aortic endothelial cell growth measured on acetone, methanol, and glutaraldehyde films was linearly correlated with the oxygen content of the treated surfaces. Nitrogen was incorporated in the surface by blending nitrogen gas into the organic vapors used for plasma deposition. The resulting nitrogen‐containing substrates exhibited a high affinity for serum fibronectin but a moderate cell growth.

Polystyrene

Glutaraldehyde

10.1002/jbm.820241207

Cite

Citations (161)

Issue Information – TOC

Journal of Biomedical Materials Research Part A (2016)

James M. Anderson Ahmed El‐Ghannam Andr Es Garcia Kevin Eugene Healy

Part A is an international, interdisciplinary, Englishlanguage publication of original contributions concerning studies of the preparation, performance, and evaluation of biomaterials; the chemical, physical, toxicological, and mechanical behavior of materials in physiological environments; and the response of blood and tissues to biomaterials.The Journal publishes peer-reviewed articles on all relevant biomaterial topics including the science and technology of alloys, polymers, ceramics, and reprocessed animal and human tissues in surgery, dentistry, artificial organs, and other medical devices.The Journal also publishes articles in interdisciplinary areas such as tissue engineering and controlled release technology where biomaterials play a significant role in the performance of the medical device.

10.1002/jbm.a.35785

Cite

Citations (0)

Hydrophilic-hydrophobic copolymers as cell substrates: Effect on 3T3 cell growth rates

Journal of Colloid and Interface Science (1985)

Thomas A. Horbett Michael B. Schway Buddy D. Ratner

Protein Adsorption

10.1016/0021-9797(85)90006-2

Cite

Citations (142)

Plasma-deposited tetraglyme surfaces greatly reduce total blood protein adsorption, contact activation, platelet adhesion, platelet procoagulant activity, andin vitro thrombus deposition

Journal of Biomedical Materials Research Part A (2007)

Lan Cao Mark Chang Chi‐Ying Lee David G. Castner Sivaprasad Sukavaneshvar

Abstract The ability of tetraethylene glycol dimethyl ether (tetraglyme) plasma deposited coatings exhibiting ultralow fibrinogen adsorption to reduce blood activation was studied with six in vitro methods, namely fibrinogen and von Willebrand's factor adsorption, total protein adsorption, clotting time in recalcified plasma, platelet adhesion and procoagulant activity, and whole blood thrombosis in a disturbed flow catheter model. Surface plasmon resonance results showed that tetraglyme surfaces strongly resisted the adsorption of all proteins from human plasma. The clotting time in the presence of tetraglyme surfaces was lengthened compared with controls, indicating a lower activation of the intrinsic coagulation cascade. Platelet adhesion and thrombin generation by adherent platelets were greatly reduced on tetraglyme‐coated materials, compared with uncoated and Biospan®‐coated glass slides. In the in vitro disturbed blood flow model, tetraglyme plasma coated catheters had 50% less thrombus than did the uncoated catheters. Tetraglyme‐coated materials thus had greatly reduced blood interactions as measured with all six methods. The improved blood compatibility of plasma‐deposited tetraglyme is thus not only due to their reduced platelet adhesion and activation, but also to a generalized reduction in blood interactions. © 2007 Wiley Periodicals, Inc. J Biomed Mater Res 2007

Platelet adhesiveness

Protein Adsorption

Factor XII

10.1002/jbm.a.31091

Cite

Citations (84)

Masthead

Journal of Biomedical Materials Research (1993)

James M. Anderson Jonathan Black Robert M. Craig Robert M. Pilliar Buddy D. Ratner

10.1002/jbm.820270301

Cite

Citations (0)

In vitro study of the intrinsic toxicity of synthetic surfaces to cells

Journal of Biomedical Materials Research (1994)

Sylvie I. Ertel Buddy D. Ratner Amarjeev Kaul Michael B. Schway Thomas A. Horbett

Abstract A trypan blue inclusion assay was used to measure cell death on poly(dimethyl siloxane) (PDMS), polyethylene (PE), poly(methyl methacrylate) (PMMA), polyurethanes, glass, and glow‐discharge‐treated polystyrene or poly(ethylene terephthalate). Cell lines used were bovine aortic endothelial, 3T3, mouse peritoneal macrophage, and BHK cells. In the absence of proteins in the media, PDMS, PE, PMMA, and some polyurethanes were consistently found to induce cell death. This toxic effect disappeared if the cells were seeded in serum‐containing medium or if concentrated solutions of proteins (albumin, IgG, or fibronectin) were preadsorbed on the materials. The substrate toxicity appeared to be due to the physical properties of the substrate and not to the release of toxic leachables. © 1994 John Wiley & Sons, Inc.

Trypan blue

Bovine serum albumin

Polystyrene

10.1002/jbm.820280603

Cite

Citations (94)

Adsorption of proteins from plasma to a series of hydrophilic‐hydrophobic copolymers. I. Analysis with the in situ radioiodination technique

Journal of Biomedical Materials Research (1981)

Thomas A. Horbett P. K. Weathersby

Abstract The adsorption of proteins affects cellular interactions with foreign surfaces and thus plays an important role in determining the biocompatibility of implants. Previous studies have indicated differences in the affinity of various proteins for a given polymer, and differences in the affinity of fibrinogen for a series of polymers varying in hydrophilicity. These studies suggest that differences in the composition of the protein layer adsorbed to polymers from plasma might exist. To examine this hypothesis, the proteins adsorbed from plasma to a series of polymers varying in hydrophilicity were analyzed with the iodogram technique. Copolymers of hydroxyethyl methacrylate and ethyl methacrylate made by the radiation grafting technique were exposed to plasma for 0.5 or 150 min. The adsorbed proteins were iodinated, eluted with SDS, and separated with polyacrylamide gel electrophoresis. Fibrinogen, immunoglobulin G, hemoglobin, and a peak tentatively ascribed to prothrombin were the major proteins detected. Very little iodine was incorporated into adsorbed albumin, even though it was shown to be present by a separate experiment using dye binding. The fraction of total radioactivity associated with each of nine proteins was found to vary markedly and systematically among the surfaces. The distribution of radioactivity into the proteins was very different on 0.5 and 150‐min plasma exposed polymers. The results reflect both compositional differences in the adsorbed protein layer on the polymers and differences in the accessibility of proteins to the labeling reagent in the adsorbed state. Differences in the organization of the adsorbed protein layer may play a key role in determining whether cell surface receptors can come in contact with the specific plasma protein able to further stimulate the cell.

Protein Adsorption

Biocompatibility

10.1002/jbm.820150311

Cite

Citations (96)

Platelet and monoclonal antibody binding to fibrinogen adsorbed on glow‐discharge‐deposited polymers

Journal of Biomedical Materials Research (1995)

David Kiaei Allan S. Hoffman Thomas A. Horbett Ken R. Lew

Abstract The state of fibrinogen adsorbed on untreated and glow‐discharge‐treated surfaces was examined by measuring platelet adhesion, monoclonal antibody (mAb) binding, the amount of fibrinogen adsorbed, and the amount of adsorbed fibrinogen which could be eluted with sodium dodecyl sulfate (SDS). Tetrafluoroethylene (TFE) glow‐discharge‐treated polymers have a lower surface free energy (in air) and retain a larger fraction of adsorbed fibrinogen than untreated surfaces after SDS elution. Platelet adhesion was lowest on the TFE‐treated surfaces which retain the highest amounts of fibrinogen after SDS elution. Fibrinogen may undergo unfolding or spreading on the TFE‐treated surfaces to minimize interfacial free energy (in water) and maximize protein–;surface interactions. When it is adsorbed on the TFE‐treated surfaces, fibrinogen evidently assumes a state which somehow prevents its recognition and binding by platelet receptors. Monoclonal antibodies that bind to the three regions in fibrinogen thought to be involved in platelet adhesion were therefore used to detect changes in adsorbed fibrinogen. These regions and the antibodies which bind to them are: the COOH‐terminal of the γ‐chain, mAb M1; the RGD peptide sequence at Aα 95–98, mAb R1; the RDG sequence at Aα 572–575, mAb R2. For fibrinogen adsorbed on the untreated or TFE‐treated surfaces, M1 and R2 binding was relatively high compared to background, while R1 binding was low. However, the amount of binding of each mAb to fibrinogen adsorbed on the TFE‐treated surfaces was equal to or greater than fibrinogen adsorbed to the untreated surfaces. Therefore, antibody‐detectable changes in the platelet binding regions of adsorbed fibrinogen that might have been caused by conformational or orientational rearrangements were not observed for the TFE‐treated surfaces. The data suggest that the tight binding of fibrinogen on a surface may directly affect the ability of the fibrinogen to interact with the platelet receptors—i.e., that fibrinogen must be loosely held to facilitate maximal interaction with platelet receptors. © 1995 John Wiley & Sons, Inc.

Protein Adsorption

10.1002/jbm.820290609

Cite

Citations (63)

Masthead

Journal of Biomedical Materials Research (1995)

James M. Anderson John Brunski Nobuo Nakabayashi Robert M. Pilliar Buddy D. Ratner

10.1002/jbm.820290301

Cite

Citations (0)

Masthead

Journal of Biomedical Materials Research (1995)

James M. Anderson John Brunski Nobuo Nakabayashi Robert M. Pilliar Buddy D. Ratner

10.1002/jbm.820291101

Cite

Citations (0)