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20 patients scheduled for total hip replacement were given 1,000 ml of a new preparation of 10% hydroxyethylstarch (HES) (MW 270,000: 0.5) preoperatively. They were compared to a group of 20 patients who received 1,000 ml of 3.5% plasma protein solution (PPS). HES caused a more pronounced hemodilution than PPS. With HES, central venous pressure (CVP) rose significantly higher than with PPS. PTT was significantly prolonged in the HES but not in the PPS group. TT was significantly reduced by HES in comparison to PPS. PT (Quick-value %) and fibrinogen levels showed no difference in both groups. Blood loss and transfusion volume were comparable to HES and PPS until 24 h after the operation. One patient showed generalised flush after HES. This HES preparation is a colloid with volume-expanding properties and appears to be without clinically apparent effects on coagulation (up to a volume of 11).
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Blood coagulation plays a critical role not only in hemostasis but also in many physiological and pathological conditions. Epidemiological studies have shown that blood coagulation capacity in humans increases with age. Towards understanding the underlying mechanisms, the age regulation of factor IX, a key blood coagulation factor, was extensively studied. A series of human factor IX minigenes, consisting of various components of the human factor IX gene, were constructed and subjected to systematic analyses with HepG2 cells in culture and over the entire life span of transgenic mice. These studies identified critical gene structures that are essential for the unique age-dependent expression patterns of the human factor IX gene--one acting by stabilizing gene transcription and another increasing the amount of mRNA present, presumably by augmenting mRNA stability. These studies have set the stage for analyzing the overall age-based regulatory mechanisms of blood coagulation.
Blood coagulation studies showed there was a pronounced thrombocytopenia and hypofibrinogenemia in Holstein calves infected with Trypanosoma congolense TREU 112. There was also ineffective thrombopoiesis characterized by an increased megakaryocytic mass, reduced uptake of 35S-methionine into peripheral blood platelets and a normal platelet lifespan. There was an increased uptake of isotopic label into fibrinogen and a shortened half life indicating a consumptive error with increased peripheral use of fibrinogen. No consistent abnormalities were found in ethanol gelation, partial thromboplastin time, clot retraction and lysis or plasminogen assay. Fibrin split products were rarely detected. These findings suggest that in the chronic form of bovine trypanosomiasis there is a partially compensated consumption coagulopathy.
Blood coagulation activity in humans increases with age. We previously identified two genetic elements, age-related stability element (ASE; GAGGAAG) and age-related increase element (AIE; unique stretch of dinucleotide repeats), which were responsible for age-related stable and increasing expression patterns, respectively, and together recapitulated normal age regulation of the human factor IX (hFIX) gene. Here we report the age-regulatory mechanisms of human anticoagulant protein C (hPC), which shows an age-stable pattern of circulatory levels. The murine protein C gene showed an age-related stable expression pattern in general agreement with that of the hPC. Through longitudinal analyses of transgenic mice carrying hPC minigenes, the hPC gene was found to have a functional age-related stability element (hPC ASE; CAGGAAG) in the 5'-upstream proximal region but was found to lack any age-related increase element. Three other ASE-like sequences present in the hPC gene, GAGGAAA and (G/C)AGGATG, also bound nuclear proteins but were not active in the age regulation of the hPC gene. Functional hPC ASE and hFIX ASE were apparently generated through convergent evolution, and hFIX ASE can fully substitute for the hPC ASE in conferring age-related stable expression pattern of the hPC gene. In the presence of the hPC ASE, hFIX AIE can convert the age-stable expression pattern of the hPC gene to a hFIX-like age-related increase pattern. These results support the universality of ASE and AIE functions across different genes. Clearance of hPC protein from the circulation was not significantly affected by age. We now have established the basic mechanisms responsible for the age-related increase of blood coagulation activity.
Blood coagulation is a system in which a series of zymogens of serine proteases are sequentially activated. In this regard, there is little fundamental difference between coagulation and the activation of the homologous pancreatic zymogens. There are, however, several aspects unique to coagulation which are discussed in detail. These are (1) the requirement for a high-molecular-weight protein or lipoprotein cofactor for optimal reaction rates, (2) the requirement for membranes or a membrane-like surface which further distinguishes this system; (3) a metal ion requirement for most reactions (in contrast to the pancreatic serine proteases) relating to the content of the newly described amino acid gamma-carboxyglutamic acid in the four vitamin K-dependent proteins, regarding which recent data relating to the metal binding sites on prothrombin are discussed in detail; and (4) the uniqueness of the initiating reactions in comparison to those which activate the pancreatic zymogens, insofar as no enzyme corresponding to enterokinase has been identified. The implications of this phenomenon are analyzed with particular attention to the potential role of the endogenous activity of certain zymogens in initiating coagulation. The article deals finally with the specific problems attendant on analyzing a system in which many serine proteases lacking absolute specificity are generated and regulated.
Blood coagulation forms part of an integrated series of haemostatic reactions, involving plasma, platelet, and vascular components. Platelets adhere to damaged endothelium or to subendothelium under the influence of adhesive proteins, and when activated they aggregate and expose binding sites for coagulation factors. Platelets, therefore, act as vehicles to concentrate and potentiate coagulation reactions on the damaged vessels. Following interaction of the 'contact' factors XII and XI, the coagulation protease zymogens undergo sequential activation, resulting in the generation of thrombin, the conversion of fibrinogen to fibrin, and the formation of a platelet-fibrin haemostatic plug. The fibrinolytic system interacts to regulate fibrin deposition and removal during healing. Central to coagulation is the generation of thrombin. It is involved in promoting haemostatic reactions as well as a number of protective functions. The activities of thrombin and other serine proteases are modulated by the serine protease inhibitors (serpins), including antithrombin III and heparin cofactor II which are important in regulating the physiological anticoagulant action of glycosaminoglycans at the endothelium and the pharmacological action of heparin. Reduction of the formation or function of thrombin and other serine proteases is one of the primary aims of anticoagulant therapy.
Blood coagulation is a basic physiological defense mechanism that occurs in all vertebrates to prevent blood loss following vascular injury. In all species the basic mechanism of clot formation is similar; when endothelium is damaged a complex sequence of enzymatic reactions occurs that is localized to the site of trauma and involves both activated cells and plasma proteins. The reaction sequence is initiated by the expression of tissue factor on the surface of activated cells and results in the generation of thrombin, the most important enzyme in blood clot formation. Thrombin converts soluble fibrinogen, via soluble fibrin monomers, into the insoluble fibrin that forms the matrix of a blood clot as well as exerting positive-feedback regulation that effectively promotes additional thrombin generation that facilitates the rapid development of a thrombus. Both spontaneous and trauma-induced haemorrhagic episodes can develop in all mammals with inherited or acquired abnormalities in one or more of the coagulant proteins. Experimental studies with plasma from a wide range of species have led to the conclusion that there are extensive differences in the rates of thrombin generation and fibrin formation among species. However, current evidence suggests that at least some of these quantitative differences are likely due to the use of non-species specific laboratory reagents. Although the individual proteins involved in the procoagulant pathways exhibit similar functions in all animals, differences in amino acid sequence cause incomplete homology and varying degrees of immunological cross-reactivity for the same protein across species.
Blood coagulation can be initiated by two pathways: the extrinsic pathway, which is triggered by release of tissue factor from the site of injury, and the intrinsic system, which is stimulated by contact with a negatively charged surface. Following initial triggering, a series of serine proteases are sequentially activated, culminating in the formation of thrombin, the enzyme responsible for the conversion of soluble fibrinogen to the insoluble fibrin clot. Activation of coagulation is tightly regulated. Initiation by tissue factor is inhibited by tissue factor pathway inhibitor. Antithrombin can inactivate many of the serine proteases, including thrombin, by forming stable complexes which are rapidly cleared from the circulation. Protein C and protein S combine to inactivate coagulation factors V and VIII. The deposition of excess fibrin is prevented by the fibrinolytic system which can lyse fibrin into fibrin degradation products. Both genetic and environmental factors can influence the activation of coagulation and may predispose affected individuals to thrombosis.
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