Patterns of Adsorption of Proteins From Human Plasma Onto Foreign Surfaces

1982 ◽  
Vol 47 (03) ◽  
pp. 285-290 ◽  
Author(s):  
S Uniyal ◽  
J L Brash
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Thromboembolic Events ◽  
Hydrophilic Surfaces ◽  
Adsorbed Proteins ◽  
Foreign Surface ◽  
Determining Factor ◽  
Hydrophilic Materials ◽  
Fibrinogen Adsorption

SummaryThe deposition of proteins on blood-contacting surfaces is known to be a determining factor in subsequent thromboembolic events. The composition of the protein layers and how they change with time are unknown. To generate information relevant to these questions, the quantities of albumin, fibrinogen and IgG adsorbed on seven surfaces from human plasma as a function of time were measured using a tracelabeling method. Materials studied include several segmented polyether-urethanes, glass, siliconized glass (SG), polystyrene (PS) and polyethylene (PE).Fibrinogen, surprisingly, was not adsorbed from plasma to any of the hydrophilic surfaces. On PE and SG adsorption passed through an early maximum (before 2 min) then declined to near zero. Only on PS was adsorption substantial and constant with time. Albumin was also not detected on the hydrophilic materials, but was adsorbed substantially on the hydrophobic surfaces. IgG was detected on all surfaces, although in relatively low surface concentrations.These results suggest: 1. that the plasma itself interacts with initially adsorbed proteins, 2. that the role of fibrinogen adsorption in foreign-surface initiated thrombosis may need to be reevaluated and 3. that since the major plasma proteins are only minimally adsorbed, trace proteins may be important in blood-material interactions.

Kinetics Of Adsorption Of Proteins From Human Plasma Onto Foreign Surfaces

1981 ◽  
Author(s):  
J L Brash ◽  
S Uniyal
Keyword(s):  
Human Plasma ◽  
Surface Concentration ◽  
Kinetics Of Adsorption ◽  
Hydrophilic Surfaces ◽  
Adsorption Data ◽  
First Occurrence ◽  
Foreign Surface ◽  
Kinetics Of ◽  
Hydrophilic Materials ◽  
Zero Time

It is believed that adsorption of proteins is the first occurrence after blood/foreign surface contact. The composition of the protein layer, how it depends on surface properties, and how it changes with time are essentially unknown. The objective of this work was to develop data relevant to these questions. To this end, the quantities of �albumin, fibrinogen and IgG adsorbed on seven surfaces from human plasma as a function of time were measured. Human plasma (ACD anticoagulant) was diluted 1:4 with tris buffer. Purified proteins were labelled with iodine isotopes using the IC1 method and added to the plasma as tracers. Materials studied include several segmented polyether-urethanes, both hydrophilic and hydrophobic, glass, siliconized glass (SG), polystyrene (PS) and polyethylene (PE).The results may be summarized as follows: Fibrinogen: Within the 2 min to 3 h range of contact times, fibrinogen was not detected on any of the hydrophilic surfaces. On PE and SG the quantity adsorbed passed through a maximum between zero time and 2 min, then declined to near zero. Only on PS was adsorption substantial (0.4 μg cm-2) and constant with time, similar to that from a solution of fibrinogen. Albumin: Albumin was also not detected on the hydrophilic materials. In general its surface concentration when it was adsorbed (hydrophobic surfaces) was similar to that observed for solutions of albumin. IgG: IgG was detected on all surfaces. The surface concentrations were low (about 0.1 μg cm-2) compared to solution values but were generally constant with time.The following conclusions are drawn: (1) The plasma itself modifies adsorption. Therefore solution adsorption data cannot be used to predict plasma adsorption. (2) Contrary to popular belief, fibrinogen is absent or transient on most surfaces. (3) IgG appears to be ubiquitous as a component of protein layers adsorbed from Plasma.

Simple radioimmunoassay of cortisol in diluted samples of human plasma.

1978 ◽  
Vol 24 (9) ◽  
pp. 1468-1472 ◽  
Author(s):  
T M Connolly ◽  
P Vecsei
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Extraction Method ◽  
Plasma Cortisol ◽  
Room Temperature ◽  
Binding Proteins ◽  
Abnormal Protein ◽  
Protein Carriers ◽  
Direct Competition

Abstract We describe a simple radioimmunoassay of plasma cortisol, which can be performed in 3 h and which requires no purification, heating, or refrigeration steps. The plasma proteins are inhibited through direct competition between them and the antiserum at room temperature, at which the antiserum's affinity exceeds that of the binding proteins. Plasma, diluted with water, is incubated for 3 h at room temperature with [3H]cortisol and the antiserum. We compared results with those by the usual extraction method. The correlation between methods on evaluating normal samples with one antiserum. We compared results with those by the usual extraction method. The correlation between methods on evaluating normal samples with one antiserum was r = 0.954 (P less than 0.001), and the slope was 0.661. With three other antisera it was r = 0.922 (P less than 0.001) and slope 0.644. Plasmas with abnormal protein concentrations (i.e., from preganant women, and after corticotropin administration), tested to examine the validity of the method for routine use, and to define the role of the protein carriers, showed r = 0.859 (P less than 0.001) and slope 0.726 for the four antisera used. Additional samples, assayed with diluted standards plus stripped plasma, showed a correlation with the usual extraction method of r = 0.945 (P less than 0.001) and slope 1.026.

The Role of Fibrinogen in Platelet Interaction with Methacrylate Polymers

1987 ◽  
Vol 110 ◽  
Author(s):  
Jack N. Lindon ◽  
Eiichi Shiba ◽  
Leslie Kushner ◽  
Edwin W. Salzman
Keyword(s):  
Protein Conformation ◽  
Blood Cells ◽  
Plasma Proteins ◽  
Platelet Reactivity ◽  
Surface Protein ◽  
Surface Interactions ◽  
Methacrylate Polymers ◽  
Foreign Surface ◽  
Protein Surface Interactions

AbstractWhen blood comes in contact with a foreign surface, protein adsorption occurs within seconds and precedes the arrival of blood cells. Since a layer of plasma proteins is laid down on any surface in contact with blood before the platelets arrive, differences in platelet reactivity with different surfaces must result from variations in the nature of the protein-surface interactions. These interactions may vary in terms of which proteins bind to the surfaces, the amounts bound, and the various changes in protein conformation induced by surface contact.

Plasma Components which Interfere with Ristocetin-induced Platelet Aggregation

1975 ◽  
Vol 33 (03) ◽  
pp. 540-546 ◽  
Author(s):  
Robert F Baugh ◽  
James E Brown ◽  
Cecil Hougie
Keyword(s):  
Platelet Aggregation ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Binding Protein ◽  
Plasma Heating ◽  
Protein S ◽  
Fold Increase ◽  
Normal Human Plasma ◽  
Preliminary Examination ◽  
Normal Human

SummaryNormal human plasma contains a component or components which interfere with ristocetin-induced platelet aggregation. Preliminary examination suggests a protein (or proteins) which binds ristocetin and competes more effectively for ristocetin than do the proteins involved in ristocetin-induced platelet aggregation. The presence of this protein in normal human plasma also prevents ristocetin-induced precipitation of plasma proteins at levels of ristocetin necessary to produce platelet aggregation (0.5–2.0 mg/ml). Serum contains an apparent two-fold increase of this component when compared with plasma. Heating serum at 56° for one hour results in an additional 2 to 4 fold increase. The presence of a ristocetin-binding protein in normal human plasma requires that this protein be saturated with ristocetin before ristocetin-induced platelet aggregation will occur. Variations in the ristocetin-binding protein(s) will cause apparent discrepancies in ristocetin-induced platelet aggregation in normal human plasmas.

Baboon Fibrinogen Adsorption and Platelet Adhesion to Polymeric Materials

1991 ◽  
Vol 65 (05) ◽  
pp. 608-617 ◽  
Author(s):  
Joseph A Chinn ◽  
Thomas A Horbett ◽  
Buddy D Ratner
Keyword(s):  
Platelet Adhesion ◽  
Coagulation Factor ◽  
Polymeric Materials ◽  
Platelet Suspension ◽  
Perfusion Chamber ◽  
Static Conditions ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Fibrinogen Adsorption

SummaryThe role of fibrinogen in mediating platelet adhesion to polymers exposed to blood plasma was studied by comparison of the effect of plasma dilution on fibrinogen adsorption and platelet adhesion, and by the use of coagulation factor deficient plasmas. Polyetherurethane substrates were first preadsorbed with dilute plasma, then contacted with washed platelets suspended in a modified, apyrase containing Tyrode’s buffer. Platelet adhesion was studied under static conditions in Multiwell dishes, and also under shearing conditions using a parallel plate perfusion chamber. Fibrinogen adsorption and platelet adhesion were measured using 125I radiolabeled baboon fibrinogen and min radiolabeled baboon platelets, respectively. Surfaces were characterized by electron spectroscopy for chemical analysis (ESCA).When fibrinogen adsorption to Biomer was measured after 2 h contact with a series of dilute plasma solutions under static conditions, a peak in adsorption was observed from 0.26% plasma, i.e., adsorption was greater from 0.26% plasma than from either more or less dilute plasma. A peak in subsequent platelet adhesion to the plasma preadsorbed surfaces, measured after 2 h static incubation with washed platelets, was also observed but occurred on Biomer preadsorbed with 1.0% plasma.When fibrinogen adsorption was measured after 5 min contact under shearing conditions, the fibrinogen adsorption peak occurred on surfaces that had been exposed to 1.0% plasma. A peak in platelet adhesion to these preadsorbed surfaces, measured after 5 min contact with the platelet suspensions under shearing conditions, was observed on Biomer preadsorbed with 0.1% plasma. Shifts between the positions of the peaks in protein adsorption and platelet adhesion occurred on other polymers tested as well.Platelet adhesion was almost completely inhibited when baboon and human plasmas lacking fibrinogen (i. e., serum, heat defibrinogenated plasma, and congenitally afibrinogénémie plasma) were used. Platelet adhesion was restored to near normal when exogenous fibrinogen was added to fibrinogen deficient plasmas. Adhesion was also inhibited completely when a monoclonal antibody directed against the glycoprotein IIb/IIIa complex was added to the platelet suspension. Platelet adhesion to surfaces preadsorbed to von Willebrand factor deficient plasma was the same as to surfaces preadsorbed with normal plasma.While it appears that surface bound fibrinogen does mediate the initial attachment of platelets to Biomer, the observation that the fibrinogen adsorption and platelet adhesion maxima do not coincide exactly also suggests that the degree of subsequent platelet adhesion is dictated not only by the amount of surface bound fibrinogen but also by its conformation.

High Antibody Levels to Prothrombin Imply a Risk of Deep Venous Thrombosis and Pulmonary Embolism in Middle-aged Men

1997 ◽  
Vol 78 (04) ◽  
pp. 1178-1182 ◽  
Author(s):  
Timo Palosuo ◽  
Jarmo Virtamo ◽  
Jari Haukka ◽  
Philip R Taylor ◽  
Kimmo Aho ◽  
...  
Keyword(s):  
Pulmonary Embolism ◽  
Venous Thrombosis ◽  
Deep Venous Thrombosis ◽  
Plasma Proteins ◽  
Alpha Tocopherol ◽  
Index Number ◽  
Thromboembolic Events ◽  
Middle Aged ◽  
Phospholipid Binding ◽  
Antiprothrombin Antibodies

SummaryAntibodies against phospholipid-binding plasma proteins, such as β2-glycoprotein I (β2-GPI) and prothrombin, are associated with thromboembolic events in patients with systemic lupus erythematosus and also in subjects with no evident underlying diseases. We wanted to examine whether increased levels of antibodies to negatively-charged phospholipids (cardiolipin), to phospholipid-binding plasma proteins β2-GPI and prothrombin and to oxidised low-density lipoprotein (LDL) were associated with risk of deep venous thrombosis or pulmonary embolism in subjects with no previous thrombosis. The antibodies were measured in stored serum samples from 265 cases of deep venous thrombosis of the lower extremity or pulmonary embolism occurring during a median follow-up of about 7 years and from 265 individually matched controls. The study subjects were middle-aged men participating in a cancer prevention trial of alpha-tocopherol and beta-carotene and the cases of thromboembolic events were identified from nationwide Hospital Discharge Register.The risk for thrombotic events was significantly increased only in relation to antiprothrombin antibodies. As adjusted for body mass index, number of daily cigarettes and history of chronic bronchitis, myocardial infarction and heart failure at baseline, the odds ratio per one unit of antibody was 6.56 (95% confidence interval 1.73-25.0). The seven highest individual optical density-unit values of antiprothrombin antibodies were all confined to subjects with thromboembolic episodes.In conclusion, the present nested case-control study showed that high autoantibody levels against prothrombin implied a risk of deep venous thrombosis and pulmonary embolism and could be involved in the development of the thrombotic processes.

scholarly journals Endothelial Dysfunction in Diabetes Is Aggravated by Glycated Lipoproteins; Novel Molecular Therapies

Biomedicines ◽  
2020 ◽  
Vol 9 (1) ◽  
pp. 18
Author(s):  
Laura Toma ◽  
Camelia Sorina Stancu ◽  
Anca Volumnia Sima
Keyword(s):  
Plasma Proteins ◽  
Diabetes Complications ◽  
Vascular Complications ◽  
High Density Lipoproteins ◽  
Diabetic Patients ◽  
Inflammatory Stress ◽  
Glycation End Products ◽  
Molecular Therapies ◽  
Specific Receptors

Diabetes and its vascular complications affect an increasing number of people. This disease of epidemic proportion nowadays involves abnormalities of large and small blood vessels, all commencing with alterations of the endothelial cell (EC) functions. Cardiovascular diseases are a major cause of death and disability among diabetic patients. In diabetes, EC dysfunction (ECD) is induced by the pathological increase of glucose and by the appearance of advanced glycation end products (AGE) attached to the plasma proteins, including lipoproteins. AGE proteins interact with their specific receptors on EC plasma membrane promoting activation of signaling pathways, resulting in decreased nitric oxide bioavailability, increased intracellular oxidative and inflammatory stress, causing dysfunction and finally apoptosis of EC. Irreversibly glycated lipoproteins (AGE-Lp) were proven to have an important role in accelerating atherosclerosis in diabetes. The aim of the present review is to present up-to-date information connecting hyperglycemia, ECD and two classes of glycated Lp, glycated low-density lipoproteins and glycated high-density lipoproteins, which contribute to the aggravation of diabetes complications. We will highlight the role of dyslipidemia, oxidative and inflammatory stress and epigenetic risk factors, along with the specific mechanisms connecting them, as well as the new promising therapies to alleviate ECD in diabetes.

scholarly journals Role of combining anticoagulant and antiplatelet agents in COVID-19 treatment: a rapid review

Open Heart ◽  
2021 ◽  
Vol 8 (1) ◽  
pp. e001628
Author(s):  
Kamal Matli ◽  
Raymond Farah ◽  
Mario Maalouf ◽  
Nibal Chamoun ◽  
Christy Costanian ◽  
...  
Keyword(s):  
Treatment Guidelines ◽  
Anticoagulation Therapy ◽  
Antiplatelet Agents ◽  
Organ Damage ◽  
Multiple Organ ◽  
Rapid Review ◽  
Thromboembolic Events ◽  
Antithrombotic Agent ◽  
Heparin Resistance

Although primarily affecting the respiratory system, COVID-19 causes multiple organ damage. One of its grave consequences is a prothrombotic state that manifests as thrombotic, microthrombotic and thromboembolic events. Therefore, understanding the effect of antiplatelet and anticoagulation therapy in the context of COVID-19 treatment is important. The aim of this rapid review was to highlight the role of thrombosis in COVID-19 and to provide new insights on the use of antithrombotic therapy in its management. A rapid systematic review was performed using preferred reporting items for systematic reviews. Papers published in English on antithrombotic agent use and COVID-19 complications were eligible. Results showed that the use of anticoagulants increased survival and reduced thromboembolic events in patients. However, despite the use of anticoagulants, patients still suffered thrombotic events likely due to heparin resistance. Data on antiplatelet use in combination with anticoagulants in the setting of COVID-19 are quite scarce. Current side effects of anticoagulation therapy emphasise the need to update treatment guidelines. In this rapid review, we address a possible modulatory role of antiplatelet and anticoagulant combination against COVID-19 pathogenesis. This combination may be an effective form of adjuvant therapy against COVID-19 infection. However, further studies are needed to elucidate potential risks and benefits associated with this combination.

scholarly journals Anti-phospholipid syndrome and COVID-19 thrombosis: connecting the dots

2021 ◽  
Vol 5 (1) ◽  
Author(s):  
Moon Ley Tung ◽  
Bryce Tan ◽  
Robin Cherian ◽  
Bharatendu Chandra
Keyword(s):  
Endothelial Dysfunction ◽  
Severe Acute Respiratory Syndrome ◽  
Potential Role ◽  
Molecular Mimicry ◽  
Thromboembolic Events ◽  
The Past ◽  
High Prevalence ◽  
Connecting The Dots ◽  
Anti Phospholipid Syndrome

Abstract As the coronavirus disease 2019 (COVID-19) pandemic, which is caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), is spreading rapidly worldwide, it has emerged as a leading cause of mortality, resulting in >1 million deaths over the past 10 months. The pathophysiology of COVID-19 remains unclear, posing a great challenge to the medical management of patients. Recent studies have reported an unusually high prevalence of thromboembolic events in COVID-19 patients, although the mechanism remains elusive. Several studies have reported the presence of aPLs in COVID-19 patients. We have noticed similarities between COVID-19 and APS, which is an autoimmune prothrombotic disease that is often associated with an infective aetiology. Molecular mimicry and endothelial dysfunction could plausibly explain the mechanism of thrombogenesis in acquired APS. In this review, we discuss the clinicopathological similarities between COVID-19 and APS, and the potential role of therapeutic targets based on the anti-phospholipid model for COVID-19 disease.

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