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Plasma fibrinogen, increases

Mature human albumin consists of one polypeptide chain of 585 amino acids and contains 17 disulfide bonds. By the use of proteases, albumin can be subdivided into three domains, which have different functions. Albumin has an ellipsoidal shape, which means that it does not increase the viscosity of the plasma as much as an elongated molecule such as fibrinogen does. Because of its relatively low molecular mass (about 69 kDa) and high concentration, albumin is thought to be responsible for 75-80% of the osmotic pressure of human plasma. Electrophoretic smdies have shown that the plasma of certain humans lacks albumin. These subjects are said to exhibit analbuminemia. One cause of this condition is a mutation that affects spUcing. Subjects with analbuminemia show only moderate edema, despite the fact that albumin is the major determinant of plasma osmotic pressure. It is thought that the amounts of the other plasma proteins increase and compensate for the lack of albumin. [Pg.584]

Common risk factors for developing branch retinal vein thrombosis (BRVT) and central retinal vein thrombosis (CRVT) include increased plasma fibrinogen, diabetes, decreased exercise, hypertension, and hyperviscosity (205). Sickle cell anemia, polycythemia vera, and other proliferative disorders may also lead to this syndrome. [Pg.17]

Although cerebral blood flow is strongly related to hematocrit, any effect of increasing hematocrit on risk of stroke, or type of stroke, is weak and confounded by cigarette smoking, blood pressure and plasma fibrinogen (Welin et al. 1987). However, raised hematocrit does seem to be associated with an increased case-fatality in ischemic stroke (Allport et al. 2005). [Pg.22]

Table V shows that the amount of adsorption onto Silastic from plasma is significantly depressed below its saturation value measured in buflFer presumably because of competition from other components of the plasma. The diflFerence in adsorption from the two plasma pools may result from the increased fibrinogen concentration in one pool which would allow more eflFective competition for adsorption onto Silastic and result in enhanced adsorption. Since the adsorption of fibrinogen onto poly (HEMA)/Silastic from plasma is not so greatly depressed relative to adsorption from buflFer (see Table V), an increase in plasma fibrinogen concentration might not have so large an eflFect on adsorption onto poly-(HEMA)/Silastic as it apparently does on adsorption onto Silastic itself. Table V shows that the amount of adsorption onto Silastic from plasma is significantly depressed below its saturation value measured in buflFer presumably because of competition from other components of the plasma. The diflFerence in adsorption from the two plasma pools may result from the increased fibrinogen concentration in one pool which would allow more eflFective competition for adsorption onto Silastic and result in enhanced adsorption. Since the adsorption of fibrinogen onto poly (HEMA)/Silastic from plasma is not so greatly depressed relative to adsorption from buflFer (see Table V), an increase in plasma fibrinogen concentration might not have so large an eflFect on adsorption onto poly-(HEMA)/Silastic as it apparently does on adsorption onto Silastic itself.
Streptokinase, anistreplase and urokinase are not well absorbed by fibrin thrombi and are called nonfibrin-selective. They convert plasminogen to plasmin in the circulation, which depletes plasma fibrinogen and induces a general hypocoagulant state. This does not reduce their local thrombolytic potential but increases the risk of bleeding. [Pg.578]

Immediately after an injury, there is loss of fluid to extravascular tissue with a resulting decrease in plasma volume. If the decrease is enough to impair circulation, glomerular filtration is diminished. Diminished renal function leads to the accumulation of urea and other end products of protein metabolism in the circulation. In burned patients, serum total protein concentration falls by as much as 0.8g/dL became of both loss to extravascular spaces and catabolism of protein. Serum aj-, tt2-, and y-globulin concentrations increase, but not enough to compensate for the reduced albumin concentration. The plasma fibrinogen concentration responds dramatically to trauma and may double in 2 to 8 days after surgery. The concentration of C-reactive protein rises at the same time. [Pg.466]

Fibrinogen, Another abnormality of blood with the onset of scurvy is the marked increase of plasma fibrinogen concentration reported both in the guinea pig (M14) and the monkey (S2). [Pg.184]

Bertini, R., Bianchi, M., Villa, P., and Ghezzi, P. (1988). Depression of liver drug metabolism and increase in plasma fibrinogen by interleukin 1 and tumor necrosis factor A comparison with lymphotoxin and interferon. Int. J. Immunopharmacol. 10, 525-530. [Pg.287]

The development of anti-fibrinolytic compounds to control hemorrhage due to excessive fibrinolytic activity has assumed more importance because of the increasing use of fibrinolytic therapy. A side effect of theraypy with the protein activators SK and UK is destruction of plasma fibrinogen which causes hemorrhage. The subject of fibrinolysis inhibition has been reviewed by Baumgeurten and Maxwell ... [Pg.239]

A plasma protein, synthesized by the liver. It is converted to fibrin during the coagulation process to form the matrix of the blood clot. Thrombin is required for this conversion. Increased plasma fibrinogen levels are found after trauma and in many inflammatory diseases. The increases in the plasma fibrinogen level account, at least in part, for the increased erythrocyte sedimentation rate in such cases. Decreased plasma levels are found in liver diseases and in the genetic defect congenital hypo-fibrinogenaemia. [Pg.136]

Several mechanisms have been suggested whereby an increase in plasma fibrinogen concentration may be linked to CHD. These include the involvement of fibrinogen and fibrin in the evolution of the atheromatous plaque through fibrin deposition and in... [Pg.165]


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See also in sourсe #XX -- [ Pg.184 ]




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