Effect of hepatectomy on the posttraumatic fibrinolysis inhibition and the primary fibrinolysis inhibitor in the rat

Högstorp, Herman; Jacobsson, H.; Saldeen, Tom

doi:10.1016/0049-3848(80)90331-x

Cited by 15 publications

(3 citation statements)

References 18 publications

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“…5A and 5B). Levels above normal were seen for both ␣ 2 -antiplasmin and factor X at 48 h, whereafter these high levels dropped to be about normal at 72 h. This is probably due to an acute phase production of these proteins during the inflammatory trauma caused by the pancreatitis, and ␣ 2 -antiplasmin has earlier been shown to be an acute phase protein in the rat [36]. Our findings indicate that also factor X behaves as an acute phase protein in the rat.…”

Section: Discussionmentioning

confidence: 37%

Proteases and Protease Inhibitors in Cerulein-Induced Acute Pancreatitis in Rats

Kruse

Lasson

Häge

1999

Journal of Surgical Research

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Section: Discussionmentioning

confidence: 37%

Proteases and Protease Inhibitors in Cerulein-Induced Acute Pancreatitis in Rats

Kruse

Lasson

Häge

1999

Journal of Surgical Research

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“…Thus, the decreased level of AP may be an important factor in the increased fibrinolytic activity observed in liver cirrhosis. Moreover, it is likely that the liver is the organ of synthesis or storage of AP (30).…”

Section: Acquired Alpha 2 -Antiplasmin Deficiencymentioning

confidence: 99%

Gene targeting in hemostasis. alpha2-antiplasmin

Lijnen¹

2001

Front Biosci

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Apha2-antiplasmin (AP), the main physiological plasmin inhibitor in mammalian plasma, is a 70 kDa single chain serpin (serine proteinase inhibitor) with reactive site peptide bond Arg-Met. It inhibits plasmin very rapidly (second-order inhibition rate constant of = 2 x 107 M-1.s-1) following formation of an inactive 1:1 stoichiometric complex. The high reaction rate requires the presence of a free active site and free lysine-binding site(s) in plasmin. The pathophysiologic relevance of AP is suggested by the finding that homozygous deficient patients show a bleeding tendency; heterozygotes, in contrast, frequently have no or only mild bleeding complications. Inactivation of the AP gene in mice was achieved by replacing, via homologous recombination in embryonic stem cells, a 7 kb genomic sequence encoding the entire murine protein with the neomycin resistance expression cassette. Homozygous AP deficient mice display normal fertility, viability and development. They have an enhanced endogenous fibrinolytic capacity without overt bleeding; this is reflected by a higher spontaneous lysis rate of experimental pulmonary emboli, by a reduced fibrin deposition in the kidneys following challenge with endotoxin, by more limited photochemically induced arterial thrombosis, and by reduced infarct size following induction of focal cerebral ischemia by ligation of the left middle cerebral artery. In a vascular injury restenosis model, AP deficiency has no significant effect on smooth muscle cell migration and neointima formation. These data suggest that, at least in the murine system, the main role of alpha2-antiplasmin is in regulating plasmin activity in the circulating blood and in controlling intravascular fibrinolysis.

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“…In a previous investigation it was found that the fibrinolysis inhibition activity in serum, which involves not only plasmin inactivation but also inhibition of plasminogen activation and changes in plasmin(ogen) , fibrin interactions, was increased by 20 % 24 h after turpentine trauma even though no changes were observed in the plasmin inhibition activity in plasma or in the immunologically determined W2-antiplasmin concentration ( 9 ) . These results may be explained by the present finding of a 22 % increase in PB-AP but no change in the total APprovided that both a concomitant decrease in the non-plasminogen-binding form.…”

Section: -A P Was Increased In Rat Serum 24 H After Turpentine Trauma...mentioning

confidence: 96%

Two Forms of α₂-antiplasmin: Post-traumatic Changes in the Rat

Högstorp

Carlin

1987

Upsala Journal of Medical Sciences

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The plasminogen-binding (PB-AP) and non-plasminogen-binding (NPB-AP) forms of alpha 2-antiplasmin (AP), were assayed in rat plasma by a modified rocket immunoelectrophoretic technique before and up to 48 h after turpentine-induced trauma, using an intermediary gel containing kringles 1-3 from plasminogen. The concentration of PB-AP was significantly elevated by 22% 24 h post-traumatically, while NPB-AP was decreased at that point in time, leaving the total AP level unchanged. Total AP increased by 57% during the period 24-48 h after trauma, mainly on account of increases in the NPB-AP form. It is concluded that the plasma level of AP can remain unchanged in spite of increased fibrinolysis inhibition, owing to a relative increase in the functionally more active PB-AP.

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Effect of hepatectomy on the posttraumatic fibrinolysis inhibition and the primary fibrinolysis inhibitor in the rat

Cited by 15 publications

References 18 publications

Proteases and Protease Inhibitors in Cerulein-Induced Acute Pancreatitis in Rats

Proteases and Protease Inhibitors in Cerulein-Induced Acute Pancreatitis in Rats

Gene targeting in hemostasis. alpha2-antiplasmin

Two Forms of α₂-antiplasmin: Post-traumatic Changes in the Rat

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Effect of hepatectomy on the posttraumatic fibrinolysis inhibition and the primary fibrinolysis inhibitor in the rat

Cited by 15 publications

References 18 publications

Proteases and Protease Inhibitors in Cerulein-Induced Acute Pancreatitis in Rats

Proteases and Protease Inhibitors in Cerulein-Induced Acute Pancreatitis in Rats

Gene targeting in hemostasis. alpha2-antiplasmin

Two Forms of α2-antiplasmin: Post-traumatic Changes in the Rat

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Product

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Two Forms of α₂-antiplasmin: Post-traumatic Changes in the Rat