COAGULATION TEST FEATURES DEPENDING ON THE AB0-BLOOD GROUPS SYSTEM ANTIGENIC COMPOSITION

The maintenance of normal blood flow through the vessels is the result of the coordinated work of the coagulation and anticoagulation systems of our body. The balance of this system depends on many factors, including endothelial, humoral, platelet ones, however, we still lack knowledge about the effect of antigenic determinants on the state of the hemostatic system. This study is devoted to assessing the effect of the presence and absence of antigens on the AB0 system, presented on erythrocyte and platelet membranes, on hemostatic parameters. The study was conducted in the Clinics of Samara State Medical University and consisted of127 clinically healthy individuals who underwent a general analysis and biochemical blood analysis, 52 people with the most stable indicators of cell composition and metabolic profile were selected for a coagulation test, including determination of the activity of coagulation factors and routine tests. A significant decrease in the activity of the VIII and VII coagulation factors was revealed, as well as an increase in the prothrombin time in patients with 0 (I) blood group compared to the “antigenic” blood groups. The presence of biological variation for indicators of external and internal coagulation paths was noted, depending on the group of blood belonging to the AB0 system. The findings suggest that there is an increased susceptibility to bleeding in patients with 0 (I) blood groups due to the absence of antigenic determinants on the cell membrane, while for “antigenic” blood groups, on the contrary, there is a susceptibility to thrombosis due to increased activity of the components of the coagulation system.

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Cold Promoted Activation of Factor VII

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649052 ◽

1972 ◽

Vol 28 (02) ◽

pp. 155-168 ◽

Cited By ~ 20

Author(s):

H Gjønnæs

Keyword(s):

Coagulation Factors ◽

Oral Contraception ◽

Factor Vii ◽

Coagulation System ◽

Plasma Coagulation ◽

Main Effect

SummaryThe cold promoted shortening of the thrombotest-times occuring in the plasmas of the majority of women on oral contraception or in the last trimester of pregnancy when incubated overnight at 0°–4° was investigated.The short thrombotest-times were caused by activation of factor VII in a time consuming reaction. Activation was also revealed in the intrinsic coagulation system, but the changes in the activities of coagulation factors other than factor VII were small.Comparison was made between clot promoting effects of cooling and contact, and it was concluded that while contact apparently exerted its main effect in the intrinsic system, cooling predominately activated the extrinsic plasma coagulation system.The cold promoted activation of factor VII seemed to be brought about by an activator.

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Interaction between Haptoglobin Subtypes and AB0 Blood Groups in a Bengalee Population

Anthropologischer Anzeiger ◽

10.1127/anthranz/63/2005/335 ◽

2005 ◽

Vol 63 (3) ◽

pp. 335-340

Author(s):

Arup Ratan Bandyopadhyay ◽

Jayita Ghoshal Roy

Keyword(s):

Blood Groups ◽

Ab0 Blood Groups ◽

Haptoglobin Subtypes

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Rajputs and their AB0 blood groups

Zeitschrift für Morphologie und Anthropologie ◽

10.1127/zma/65/1973/237 ◽

1973 ◽

Vol 65 (2) ◽

pp. 237-244

Author(s):

B. R. K. Shukla ◽

Deepak Tyagi

Keyword(s):

Blood Groups ◽

Ab0 Blood Groups

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Peptic ulcer, secretor status and AB0 blood groups in an Indian population

Zeitschrift für Morphologie und Anthropologie ◽

10.1127/zma/70/1979/191 ◽

1979 ◽

Vol 70 (2) ◽

pp. 191-194

Author(s):

Rama Chakravartti ◽

M. R. Chakravartti

Keyword(s):

Peptic Ulcer ◽

Indian Population ◽

Blood Groups ◽

Secretor Status ◽

Ab0 Blood Groups

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Retinoblastoma and AB0 blood groups

Human Genetics ◽

10.1007/bf00285408 ◽

1983 ◽

Vol 63 (1) ◽

pp. 87-87 ◽

Cited By ~ 2

Author(s):

E. Matsunaga ◽

K. Minoda

Keyword(s):

Blood Groups ◽

Ab0 Blood Groups

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Coagulation (Hemostasis and Thrombosis)

10.1093/med/9780199755691.003.0295 ◽

2012 ◽

Author(s):

Rajiv K. Pruthi

Keyword(s):

Risk Factors ◽

Platelet Activation ◽

Coagulation Factors ◽

Fibrin Clot ◽

Coagulation System ◽

Bleeding Disorders ◽

Hemostatic System ◽

Blood Clots ◽

Anticoagulant System ◽

Plug Formation

The coagulation system has 2 essential functions: to maintain hemostasis and to prevent and limit thrombosis. The procoagulant component of the hemostatic system prevents and controls hemorrhage. Vascular injury results in activation of hemostasis, which consists of vasospasm, platelet plug formation (platelet activation, adhesion, and aggregation), and fibrin clot formation (by activation of coagulation factors in the procoagulant system). The anticoagulant system prevents excessive formation of blood clots, and the fibrinolytic system breaks down and remodels blood clots. Quantitative abnormalities (deficiencies) and qualitative abnormalities of platelets and coagulation factors lead to bleeding disorders, whereas deficiencies of the anticoagulant system are risk factors for thrombosis. Common disorders of hemostasis and thrombosis are reviewed.

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Association of Tissue Factor Pathway Inhibitor With Human Umbilical Vein Endothelial Cells

Blood ◽

10.1182/blood.v90.9.3568 ◽

1997 ◽

Vol 90 (9) ◽

pp. 3568-3578 ◽

Cited By ~ 20

Author(s):

John-Bjarne Hansen ◽

Randi Olsen ◽

Paul Webster

Keyword(s):

Endothelial Cells ◽

Cell Surface ◽

Tissue Factor ◽

Tissue Factor Pathway Inhibitor ◽

Umbilical Vein ◽

Coagulation Factors ◽

Coagulation System ◽

Human Umbilical Vein ◽

Tissue Factor Pathway ◽

Umbilical Vein Endothelial Cells

AbstractTissue factor pathway inhibitor (TFPI) is a serine protease inhibitor of the extrinsic coagulation system, synthesized in endothelial cells, which has recently been shown to play an important role in the regulation of activated coagulation factors at the endothelial cell surface. In the present study we investigated the subcellular localization and metabolism of TFPI in human umbilical vein endothelial cells (HUVEC). Immunocytochemical labeling of HUVEC with anti-TFPI showed specific labeling associated with the cell surface and with many intracellular organelles including the Golgi complex. Further characterization of these organelles was performed by colocalizing the anti-TFPI with 3-(2,4-dinitroanilino)′-amino-N-methyldipropylamine (DAMP; to demonstrate low pH), mannose phosphate receptor (endosomes), and LAMP 1 (late endocytic compartments). TFPI also colocalized with antibodies to the human transferrin receptor, a marker for early endocytic, recycling compartment. Endogenous TFPI colocalized with biotin in intracellular vesicles during endocytosis after biotinylation of the cell surface, which indicated that TFPI was being co-internalized with the surface biotin. The binding of exogenously added 125I-TFPI increased linearly to HUVEC over the concentration range of 0 to 32 nmol/L without saturation, the binding was not affected by up to a thousand-fold molar excess of unlabeled TFPI, and heparin inhibited the binding dose dependently. An intact C-terminal domain was important for the interaction between TFPI and the cell surface of HUVEC, because less than 10% of a C-terminal truncated form of TFPI (TFPI1-161 ) was bound after addition of equimolar concentrations of full-length TFPI. Exogenously added 125I-TFPI was not degraded in HUVEC during 4 hours at 37°C. The presence of TFPI in endocytic and recycling compartments support the hypothesis that endogenous, membrane-anchored TFPI could be internalized for subsequent recycling back to the cell surface.

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