Complement Activation Dramatically Accelerates Blood Plasma Fouling On Antifouling Poly(2‐Hydroxyethyl Methacrylate) Brush Surfaces

2021 ◽  
pp. 2100460
Author(s):  
Tomáš Riedel ◽  
Andres de los Santos Pereira ◽  
Johanka Táborská ◽  
Zuzana Riedelová ◽  
Ognen Pop‐Georgievski ◽  
...  
Keyword(s):  
Blood Plasma ◽  
Complement Activation ◽  
Hydroxyethyl Methacrylate

Complement activation in EDTA blood/plasma samples may be caused by coagulation proteases

1997 ◽  
pp. 363-369
Author(s):  
Philippe H. Pfeifer ◽  
Tony E. Hugli ◽  
Earl W. Davie ◽  
Kazuo Fujikawa
Keyword(s):  
Blood Plasma ◽  
Complement Activation ◽  
Plasma Samples ◽  
Edta Blood

The effect of substrate molecular mobility on surface induced immune complement activation and blood plasma coagulation

Biomaterials ◽  
2004 ◽  
Vol 25 (19) ◽  
pp. 4581-4590 ◽  
Author(s):  
Mattias Berglin ◽  
Marcus Andersson ◽  
Anders Sellborn ◽  
Hans Elwing
Keyword(s):  
Blood Plasma ◽  
Complement Activation ◽  
Molecular Mobility ◽  
Plasma Coagulation

An iron-binding component in human blood plasma

2001 ◽  
Vol 14 (2) ◽  
pp. 111-113
Author(s):  
Arthur L. Schade ◽  
Liona Caroline
Keyword(s):  
Blood Plasma ◽  
Human Blood ◽  
Human Blood Plasma ◽  
Iron Binding ◽  
Binding Component

The lectin-like domain of thrombomodulin interferes with complement activation and protects against diabetic nephropathy

2010 ◽  
Vol 5 (S 01) ◽  
Author(s):  
H Wang ◽  
V Ilya ◽  
Q Zhou ◽  
T He ◽  
M Thati ◽  
...  
Keyword(s):  
Diabetic Nephropathy ◽  
Complement Activation

The Mechanism of Platelet Aggregation Induced by HLA-Related Antibodies

1996 ◽  
Vol 76 (05) ◽  
pp. 774-779 ◽  
Author(s):  
John T Brandt ◽  
Carmen J Julius ◽  
Jeanne M Osborne ◽  
Clark L Anderson
Keyword(s):  
Platelet Aggregation ◽  
Platelet Activation ◽  
Complement Activation ◽  
Thromboembolic Disease ◽  
Clinical Samples ◽  
Hla Antigen ◽  
Aggregation Response ◽  
Immune Mediated ◽  
Dependent Pathway

SummaryImmune-mediated platelet activation is emerging as an important pathogenic mechanism of thrombosis. In vitro studies have suggested two distinct pathways for immune-mediated platelet activation; one involving clustering of platelet FcyRIIa, the other involving platelet-associated complement activation. HLA-related antibodies have been shown to cause platelet aggregation, but the mechanism has not been clarified. We evaluated the mechanism of platelet aggregation induced by HLA-related antibodies from nine patients. Antibody to platelet FcyRIIa failed to block platelet aggregation with 8/9 samples, indicating that engagement of platelet FcyRIIa is not necessary for the platelet aggregation induced by HLA-related antibodies. In contrast, platelet aggregation was blocked by antibodies to human C8 (5/7) or C9 (7/7). F(ab’)2 fragments of patient IgG failed to induce platelet activation although they bound to HLA antigen on platelets. Intact patient IgG failed to aggregate washed platelets unless aged serum was added. The activating IgG could be adsorbed by incubation with lymphocytes and eluted from the lymphocytes. These results indicate that complement activation is involved in the aggregation response to HLA-related antibodies. This is the first demonstration of complement-mediated platelet aggregation by clinical samples. Five of the patients developed thrombocytopenia in relationship to blood transfusion and two patients developed acute thromboembolic disease, suggesting that these antibodies and the complement-dependent pathway of platelet aggregation may be of clinical significance.

Protection from Hg-Inactivation of Factor XIII by Mercaptalbumin

1970 ◽  
Vol 24 (03/04) ◽  
pp. 352-355 ◽  
Author(s):  
P Fantl
Keyword(s):  
Blood Plasma ◽  
Factor Xiii ◽  
Active Component ◽  
Plasma Albumin ◽  
Plasma Factor ◽  
Mercuric Ions

SummaryThe blood plasma factor XIII (fibrin stabilizing factor) is inactivated by mercuric ions and can be reactivated by serum - or plasma albumin of which the active component is mercaptalbumin. A relation between mercaptalbumin concentration and factor XIII activity is pointed out.

Validation of Simvastatin Analysis Methods in Human Blood Plasma (In Vitro) Using HPLC-UV Detector

2018 ◽  
Vol 8 (2) ◽  
Author(s):  
Iyan Sopyan ◽  
Cynthia Jaya ◽  
Driyanti Rahayu
Keyword(s):  
Blood Plasma ◽  
Human Plasma ◽  
Disease Risk ◽  
Protein Precipitation ◽  
Precipitation Method ◽  
Human Blood Plasma ◽  
Analysis Method ◽  
Uv Detector ◽  
Number Of Patients ◽  
System Suitability

The use of simvastatin (SV) increases along with the increasing number of patients with hyperlipidemia and cardiovascular disease risk factors. Consequently, this condition leads to the increasing need of analytical determination of SV in blood plasma. Analysis of SV in human plasma using protein precipitation method and HPLC with UV detector has not been reported. This research was purpose to find out the rapid, accurate, and valid of SV analysis method in human plasma. In this research plasma samples were treated with protein precipitation method. The analyte was then analyzed using HPLC with C18 column 250x4 mm and 5 µm of particle size, the mobile phase contained of phosphate buffer 0.01 M (pH 4.0) and acetonitrile 30:70 v/v with flow rate 1 mL/minute, and detected at 239 nm. The analysis method was validated based on some parameters, such as selectivity, accuracy, precision, repeatability, linearity, LOD, LOQ, and system suitability. The result showed selectivity represented by Rs was 2.870, repeatability by its CV less than 2%, and linearity by its coefficient correlation (r) 0.9992 for concentration range 0.08-0.32 ppm. Based on chromatogram peak area, LOD and LOQ were 0.0132 and 0.0440 ppm respectively, accuracy and precision were 86.25-89.36% and 0.66-1.81% were obtained. The result of system suitability test from retention time and chromatogram peak area showed by its CV less than 2%. The analysis method was proved to be valid for SV analysis in human plasma

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