Blood Compatibility of Stainless-Steel and Titanium Immobilized with Alginic Acid Layers

2002 ◽  
Vol 734 ◽  
Author(s):  
Tomohiko Yoshioka ◽  
Kanji Tsuru ◽  
Satoshi Hayakawa ◽  
Akiyoshi Osaka
Keyword(s):  
Stainless Steel ◽  
Photoelectron Spectroscopy ◽  
Blood Clotting ◽  
Alginic Acid ◽  
Blood Compatibility ◽  
Adhesion Assay ◽  
Clotting Factors ◽  
Titanium Substrates ◽  
Blood Clotting Factors

ABSTRACTγ-Aminopropyltriethoxysilane (γ-APS) was grafted on stainless-steel and titanium substrates, and subsequently alginic acid layer was immobilized on them. Their surfaces were characterized with X-ray photoelectron spectroscopy (XPS) and contact angle measurement. Blood compatibility of thus obtained substrates was evaluated in terms of both the number of the adhered platelets and blood clotting factors for plasma contacted with the substrates such as active partial thromboplastin time (PTT), prothrombin time (PT), and amount of fibrinogen (Fib). The steel and titanium substrates with alginic acid layer did not affect blood clotting factors. In vitro platelet adhesion assay indicated that those substrates adhered less number of platelets than non-treated substrates. Hence the alginic acid immobilization leads to blood compatible surfaces.

Reversible Inhibition of the In Vitro Coagulation of Human Plasma by Lectins

1982 ◽  
Vol 48 (02) ◽  
pp. 120-124 ◽  
Author(s):  
J-M Freyssinet ◽  
D Thevenon ◽  
A Souque ◽  
M Suscillon
Keyword(s):  
Blood Clotting ◽  
Inhibitory Effect ◽  
Phospholipid Vesicles ◽  
Carbohydrate Binding ◽  
Clotting Factors ◽  
Con A ◽  
Acetylneuraminic Acid ◽  
Human Control ◽  
Blood Clotting Factors

SummaryWheat germ agglutinin (WGA) and concanavalin A (Con-A) (also red kidney bean agglutinin, PHA) have been found to be inhibitors of plasma clotting in vitro. At 40 µg/ml and 250 µg/ml (4.4 µM and 10 µM in carbohydrate binding sites, final concentrations) respectively, WGA and Con-A are able to double the activated partial thromboplastin time of normal human control plasma. Their inhibitory effect is due to their capacity to interact with the carbohydrate portion of blood clotting factors. It is totally abolished in the presence of specific saccharides for WGA or Con-A and is attenuated in the presence of 4% (v/v, final concentration) of human erythrocytes. The action of WGA is mediated by its ability to interact with N-acetylneuraminic acid. When purified phospholipid vesicles plus kaolin are used as an activator instead of cephalidin, this effect persists to the same extent. These two lectins also prolong the plasma clotting time using Russell's viper venom plus purified phospholipid vesicles as an activator. Quick's time was also prolonged by WGA and Con-A but to a lesser extent in this case. WGA can interact directly with some purified blood clotting factors (IX, X and II) in a classical lectin-glycoprotein precipitin reaction. When assessed at individual factors level in whole plasma using clotting assays, direct inhibitions by WGA are only apparent.

Biological Activity of Low-Molecular Weight Dextran 40. The Effect on Serum Proteins, Plasma Blood Clotting Factors and Erythrocyte Sedimentation Rate

1973 ◽  
Vol 1 (3) ◽  
pp. 194-203
Author(s):  
Witold Rudowski ◽  
Ewa Kostrzewska ◽  
Anita Gregor ◽  
Angela Naleçzyńska
Keyword(s):  
Molecular Weight ◽  
Blood Clotting ◽  
Serum Proteins ◽  
Mean Value ◽  
Low Molecular Weight ◽  
Clotting Factors ◽  
Dextran 40 ◽  
Erythrocyte Sedimentation ◽  
Blood Clotting Factors

Dextran 40 infused in doses from 1.2 to 1.5 g/kg body weight decreases the concentration of proteins in the plasma and reduces the total amount of circulating protein. Dextran 40 in vitro precipitates high-molecular weight proteins participating in blood clotting, such as factor VIII and fibrinogen and, if infused, decreases their plasma levels. Addition in vitro of Dextran 40 to blood with a high ESR reduces the value proportionally to the concentration of dextran in the blood sample: after infusion of Dextran 40 the ESR decreases by a mean value of 19.9% after infusion of 500 ml and by 36.2% after 1000 ml. No bleeding was noted with these infusions.

Blood Coagulation Studies and Extracorporeal Circulation in Man

1967 ◽  
Vol 18 (03/04) ◽  
pp. 634-646 ◽  
Author(s):  
N Thurnherr
Keyword(s):  
Blood Coagulation ◽  
Extracorporeal Circulation ◽  
Blood Clotting ◽  
Heart Surgery ◽  
Open Heart Surgery ◽  
Fibrinolytic System ◽  
Open Heart ◽  
Clotting Factors ◽  
Blood Clotting Factors

SummaryBlood clotting investigations have been executed in 25 patients who have undergone open heart surgery with extracorporeal circulation. A description of alterations in the activity of blood clotting factors, the fibrinolytic system, prothrombin consumption and platelets during several phases of the operation is given.

Topology of the binding site of blood-clotting factors in model membranes. A fluorescence study

1986 ◽  
Vol 155 (1) ◽  
pp. 133-140 ◽  
Author(s):  
Jeanne PRIGENT-DACHARY ◽  
Jean-Francois FAUCON ◽  
Michel-Rene BOISSEAU ◽  
Jean DUFOURCQ
Keyword(s):  
Binding Site ◽  
Blood Clotting ◽  
Model Membranes ◽  
Clotting Factors ◽  
Fluorescence Study ◽  
Blood Clotting Factors

Surface Characterization and In Vitro Blood Compatibility of Poly(Ethylene Terephthalate) Immobilized with Hirudin

2005 ◽  
Vol 288-289 ◽  
pp. 421-424
Author(s):  
F. Li ◽  
Jin Wang ◽  
H. Sun ◽  
Nan Huang
Keyword(s):  
Free Energy ◽  
Photoelectron Spectroscopy ◽  
Surface Characterization ◽  
Ethylene Terephthalate ◽  
Blood Compatibility ◽  
Argon Plasma ◽  
Angle Measurement ◽  
Poly Ethylene Terephthalate ◽  
Poly Ethylene

Poly(ethylene terephthalate) films were exposed under argon plasma glow discharge and induced polymerization of acrylic acid (AA) in order to introduce carboxylic acid group onto PET (PET-AA) assisting by ultroviolet radiation. Hirudin-immobilized PETs were prepared by the grafting of PET-AA, followed by chemical reaction with hirudin. The surface structure of the treated PET is determined by X-ray photoelectron spectroscopy (XPS). The wettability and surface free energy, interface free energy of the films is investigated by contact angle measurement. Platelet adhesion evaluatiion is conducted to examine the blood compatibility in vitro. Scanning electron microscopy (SEM) and optical microscopy reveal that the amounts of adhered, aggregated and morphologically changed platelets are reduced on hirudin-immobilized PET films.

scholarly journals Surface Characteristics and Cell Adhesion Behaviors of the Anodized Biomedical Stainless Steel

2020 ◽  
Vol 10 (18) ◽  
pp. 6275
Author(s):  
Heng-Jui Hsu ◽  
Chia-Yu Wu ◽  
Bai-Hung Huang ◽  
Chi-Hsun Tsai ◽  
Takashi Saito ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Cell Culture ◽  
Stainless Steel ◽  
Cell Adhesion ◽  
Oxide Layer ◽  
Photoelectron Spectroscopy ◽  
X Ray ◽  
In Vitro Cell Culture ◽  
Cell Culture Assay

In this study, an electrochemical anodizing method was applied as surface modification of the 316L biomedical stainless steel (BSS). The surface properties, microstructural characteristics, and biocompatibility responses of the anodized 316L BSS specimens were elucidated through scanning electron microscopy, X-ray photoelectron spectroscopy, X-ray diffractometry, transmission electron microscopy, and in vitro cell culture assay. Analytical results revealed that the oxide layer of dichromium trioxide (Cr2O3) was formed on the modified 316L BSS specimens after the different anodization modifications. Moreover, a dual porous (micro/nanoporous) topography can also be discovered on the surface of the modified 316L BSS specimens. The microstructure of the anodized oxide layer was composed of amorphous austenite phase and nano-Cr2O3. Furthermore, in vitro cell culture assay also demonstrated that the osteoblast-like cells (MG-63) on the anodized 316L BSS specimens were completely adhered and covered as compared with the unmodified 316L BSS specimen. As a result, the anodized 316L BSS with a dual porous (micro/nanoporous) oxide layer has great potential to induce cell adhesion and promote bone formation.

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