Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The control of coagulation and fibrinolytic events appears to be primarily due to four plasma proteinase inhibitors, antithrombin III, C-1-esterase inhibitor, alpha-2-antiplasmin, and alpha-2-macroglobulin. Results to date indicate that antithrombin III controls the activity of both thrombin and Factor Xa, C-1-esterase inhibitor controls kallikrein and probably activated Hageman Factor (Factor XIIa), and alpha-2-antiplasmin controls plasmin activity. The role of alpha-2-macroglobulin is not clear since it does not appear to be a primary inhibitor of any of the above enzymes. However, it is probable that it serves two functions, first as a "transfer" agent for the rapid removal of proteinases from the circulation which have been first bound by antithrombin III, C-1-esterase inhibitor, or alpha-2-antiplasmin. The second function is probably that of a back-up inhibitor when the levels of the three important controlling plasma proteins become low. The role of other plasma inhibitors such as alpha-1-proteinase inhibitor, alpha-1-antichymotrypsin, and the inter-alpha-trypsin inhibitor in coagulation and fibrinolysis would appear to be minor since these proteins either do not inactivate enzymes involved in these systems or do so at a rate too slow to be of biological significance.
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PMID:Control of coagulation and fibrinolysis by plasma proteinase inhibitors. 620 38

We have studied the main protease inhibitors of leukocytes, alpha-1-protease (alpha 1-PI), alpha-1-antichymotrypsin (alpha 1-Achy) and alpha-2-macroglobulin (alpha 2-M), as well as different parameters of coagulation and fibrinolysis in 21 cases of acute nonlymphoblastic leukemia (ANLL) before, during and after therapy. Nine of the patients presented signs of DIC, 8 of whom belonged to subtype M3 and to subtype 1 M1. The initial alpha 1-PI and alpha 1-Achy levels, which were elevated, increased during the treatment period. There was no significant difference between patients with and without DIC. However, those leukemic patients with DIC showed a significant decrease in plasminogen (p less than 0.005) and fast antiplasmin (p less than 0.01) only during the treatment compared with DIC free patients. All DIC cases demonstrated circulating plasmin-antiplasmin complex (P-AP) both before and during treatment. Independent of a possible proteolytic action of leukocyte enzymes on clotting factors in the clinical course of ANLL (mainly M3 subtype), our results suggest an activation of plasmin-mediated fibrinolysis related to the activation of plasminogen by leukocytes, reactive DIC or both.
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PMID:Changes in plasma levels of protease and fibrinolytic inhibitors induced by treatment in acute myeloid leukemia. 623 45

Second trimester amniotic fluid fibrinolytic system was examined in normal pregnancies and those complicated by anencephaly, spina bifida and fetal chromosome abnormalities. No significant difference was demonstrated between the fibrinolytic systems from normal pregnancies and those complicated by fetal chromosome abnormalities. In pregnancies complicated with anencephaly and spina bifida no significant difference was demonstrated for alpha-1-antitrypsin, alpha-1-antichymotrypsin and urokinase. Plasminogen was significantly lower (p less than 0.02) and plasmin significantly higher (p less than 0.001) than levels from normal amniotic fluid. Alpha-2-macroglobulin, fibrinogen, FDP-D and FDP-E were detected only in pregnancies complicated with anencephaly and spina bifida.
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PMID:Amniotic fluid fibrinolytic system in fetal neural tube defects. 635

The association rate constants for the interaction of alpha-1-proteinase inhibitor, oxidized alpha-1-proteinase inhibitor, and alpha-1-antichymotrypsin with several mammalian serine proteinases have been determined. The results indicate that leukocyte elastase reacts more rapidly with alpha-1-proteinase inhibitor than any other proteinase tested, while leukocyte cathepsin G shows the strongest association with alpha-1-antichymotrypsin. Oxidation of the critical methionine residue of alpha-1-proteinase inhibitor reduces the association with leukocyte elastase by a factor of more than 2000 and also lowers the association with all of the other enzymes tested with the exception of chymotrypsin. Significantly, oxidation completely abolishes any interaction of alpha-1-proteinase inhibitor with porcine elastase, human plasmin or human thrombin. These data support previous results (Johnson, D., and Travis, J. (1979) J. Biol. Chem. 254, 4022-4026) which indicated that oxidation of human alpha-1-proteinase inhibitor in vivo could reduce the effectiveness of this inhibitor in controlling proteolysis. In the lung, in particular, oxidizing agents of both chemical and biological sources could, indirectly, augment elastolysis in this tissue, resulting in the development of pulmonary emphysema.
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PMID:Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin. 698 30