Endocrine Influence on the Plasmin - Plasmin Inhibitor System in the Blood of Rats

1952 ◽  
Author(s):  
Elizabeth Gray ◽  
Evelyn T. Volkringer ◽  
David L. Chamovitz ◽  
Walter F. Kocholaty ◽  
H. Jensen
Keyword(s):  
Inhibitor System ◽  
Endocrine Influence ◽  
Plasmin Inhibitor

ENDOCRINE INFLUENCE ON THE PLASMIN-PLASMIN INHIBITOR SYSTEM IN THE BLOOD OF RATS1

Endocrinology ◽  
1953 ◽  
Vol 52 (2) ◽  
pp. 228-232 ◽  
Author(s):  
ELIZABETH J. GRAY ◽  
EVELYN T. VOLKRINGER ◽  
DAVID L. CHAMOVITZ ◽  
WALTER F. KOCHOLATY ◽  
H. JENSEN
Keyword(s):  
Inhibitor System ◽  
Endocrine Influence ◽  
Plasmin Inhibitor

On the Natural Blood Coagulation Inhibitor System Investigations of Inhibitor Factors Based on Antithrombin Deficient Blood

1965 ◽  
Vol 14 (03/04) ◽  
pp. 473-489 ◽  
Author(s):  
O Egeberg
Keyword(s):  
Normal Level ◽  
Antithrombin Iii ◽  
Strong Support ◽  
Blood Protein ◽  
Coagulation Inhibitor ◽  
Inhibitor System ◽  
Normal Human ◽  
Partial Deficiency ◽  
Antithrombin Iii Activity ◽  
Prothrombinase Activity

SummaryNatural coagulation inhibitor factors were studied in sera, or in fractions of sera, from patients with congenital partial deficiency of antithrombin and from normal persons. In the patients’ sera the progressive antithrombin (antithrombin III) and heparin cofactor (antithrombin II) had both been measured around 50 per cent of normal level.No decreased activity could be demonstrated in the patients’ sera as to antiprothrombinase, the inhibitor against blood intrinsic prothrombinase activity.For anticonvertin, the inhibitor against the tissue convertin complex, the activity was found decreased to about the same level as that demonstrated for antithrombin III and II. The results lend strong support to the hypothesis that the activities measured as anticonvertin, antithrombin III and antithrombin II represent functions of the same blood protein, which on the other side appears to be distinct from antiprothrombinase. In accordance with this explanation, an antithrombin III concentrate had also antithrombin II and anticonvertin activity, and further, adsorption of a normal human serum with convertin appeared to specifically reduce its antithrombin III activity.The inhibitor against activated antihemophilic C factor (AHC’ = activated f. XI) was studied in sera adsorbed with BaS04 and celite. The inhibitor activity was found at normal level in the patients’ sera, consistent with the view that anti-AHC’ is distinct from antithrombin III, II and from anticonvertin. No acceleration of the anti-AHC’ activity could be demonstrated after addition to the inhibition mixture of weak solutions of heparin.The results are discussed.

A New Fluorogenic Substrate Method for Assay of Bacterial Endotoxins Using Limulus Hemocyte Lysate

1979 ◽  
Author(s):  
T Harada ◽  
M Ohki ◽  
M Niwa ◽  
S Iwanaga
Keyword(s):  
Antithrombin Iii ◽  
Assay Method ◽  
Sensitive Assay ◽  
Fluorogenic Substrate ◽  
Toxin Concentration ◽  
Amidase Activity ◽  
E Coli ◽  
Bacterial Endotoxins ◽  
Plasmin Inhibitor ◽  
Limulus Test

Limulus hemocyte lysate contains a proclotting enzyme, which is transformed to the active clotting enzyme in the presence of gram-negative bacterial endotoxins. The clotting enzyme coagulates a clottable protein, named coagulogen, contained also in the lysate. This gelation reaction of the lysate, named Limulus test, has been widely employed as a simple and very sensitive assay method for endotoxins. We developed a new fluorogenic substrate, Boc-Leu-Gly-Arg-4-methylcoumarin amide, for Limulus clotting enzyme and established an enzymatic assay method for endotoxins, using the substrate. Because the endotoxin mediates the activation of proclotting enzyme in the lysate, the measurement of amidase activity could be applicable for quantitation of the endotoxins. In fact, the amidase activity determined fluorometrically increased by increasing concentration of E. coli 0111: B4 endotoxin added to the lysate, and a linear relationship between the toxin concentration and the activity was observed in the range of 5X10-6to 5xl0-2 µg endotoxin. The method was a fifty times more sensitive than that of the Limulus test and was very reproducible. However, the method was not directly applicable for the assay of endotoxins in circulating blood, as the amidase activity was strongly inhibited by antithrombin III and α2-plasmin inhibitor. Thus, some pretreatment with heat or chloroform on plasma samples before the assay was required.

Inhibition of the Activities of α2-Plasmin inhibitor (PI) and CI inhibitor (CI-Inh) by the Synthetic Fibrinolytic Agent, 3-Hydroxypropyl Flufenamide (Flu-HPA)

1979 ◽  
Author(s):  
L Miles ◽  
J Burnier ◽  
M Verlander ◽  
M Goodman ◽  
A Kleiss ◽  
...  
Keyword(s):  
Plasminogen Activators ◽  
Inhibitory Effect ◽  
Mechanisms Of Action ◽  
Flufenamic Acid ◽  
Clot Lysis ◽  
Factor Xiia ◽  
Dependent Inhibition ◽  
Normal Human ◽  
Plasmin Inhibitor

Flu-HPA is one of a series of flufenamic acid derivations that enhances plasminogen-dependent clot lysis in vitro. Studies of possible mechanisms of action of Flu-HPA were undertaken. The influence of Flu-HPA on the inhibition of purified plasmin by purified PI was studied. PI activity was assessed by its inhibition of the clevage of the tripeptide S-2251 (H-D-Val-Leu-Lys-pNA) by plasmin. Flu-HPA was dissolved in DMF or in methonol and preincubated with PI before addition of plasmin. At Flu-HPA concentrations greater than 1mM and up to 60mM, the inhibitory activity of PI was totally lost. The inhibitory effect of normal human plasma on plasmin was also completely abolished at concentrations of Flu-HPA between 2.5 and 40mM. The effect of Flu-HPA on the inhibition of purified plasma kallikrein by purified CI-Inh was also studied. CI-Inh activity was measured by its inhibition of cleavage of the tripeptide Bz-Pro-Phe-Arg-pNA by kallikrein. When Flu-HPA, dissolved in DMF or in methonol, was preincubated with CI-Inh, a concentration dependent inhibition of CI-Inh activity was observed. CI-Inh activity was abolished by concentrations of Flu-HPA greater than 1mM. Flu-HPA also inhibited the activity of CI-Inh on purified Factor XIIa. These observations suggest that this flufenamic acid derivative may enhance fibrinolysis not only by inhibiting PI activity but also by decreasing the inactivation of plasminogen activators by CI-Inh.

Effects of an Autoregulatory Senescence-inhibitor Gene Construct on Nicotiana alata Link and Otto.

HortScience ◽  
1998 ◽  
Vol 33 (3) ◽  
pp. 519d-519 ◽  
Author(s):  
Kenneth R. Schroeder ◽  
Dennis P. Stimart
Keyword(s):  
Agrobacterium Tumefaciens ◽  
Plant Height ◽  
Dry Weight ◽  
Nicotiana Alata ◽  
Wild Type ◽  
Gene Encoding ◽  
Delayed Senescence ◽  
Gene Construct ◽  
Shoot Dry Weight ◽  
Inhibitor System

Nicotiana alata Link and Otto. was transformed via Agrobacterium tumefaciens encoding a senescence-specific promoter SAG12 cloned from Arabidopsis thaliana fused to a Agrobacterium tumefaciens gene encoding isopentenyl transferase (IPT) that catalyzes cytokinin synthesis. This was considered an autoregulatory senescence-inhibitor system. In 1996, we reported delayed senescence of intact flowers by 2 to 6 d and delayed leaf senescence of transgenic vs. wild-type N. alata. Further evaluations in 1997 revealed several other interesting effects of the SAG12-IPT gene construct. Measurement of chlorophyll content of mature leaves showed higher levels of both chlorophyll a and b in transgenic material under normal fertilization and truncated fertilization regimes. At 4 to 5 months of age transgenic plants expressed differences in plant height, branching, and dry weight. Plant height was reduced by 3 to 13 cm; branch counts increased 2 to 3 fold; and shoot dry weight increased up to 11 g over wild-type N. alata. These observations indicate the system is not tightly autoregulated and may prove useful to the floriculture industry for producing compact and more floriferous plants.

scholarly journals Incorporation of α2-Plasmin Inhibitor into Fibrin Clots and Its Association with the Clinical Outcome of Acute Ischemic Stroke Patients

Biomolecules ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 347
Author(s):  
Zsuzsa Bagoly ◽  
Barbara Baráth ◽  
Rita Orbán-Kálmándi ◽  
István Szegedi ◽  
Réka Bogáti ◽  
...  
Keyword(s):  
Ischemic Stroke ◽  
Acute Ischemic Stroke ◽  
Intracranial Hemorrhage ◽  
Intravenous Thrombolysis ◽  
Fibrin Clot ◽  
Clot Lysis ◽  
Stroke Patients ◽  
Plasmin Inhibitor ◽  
Fibrin Clots

Cross-linking of α2-plasmin inhibitor (α2-PI) to fibrin by activated factor XIII (FXIIIa) is essential for the inhibition of fibrinolysis. Little is known about the factors modifying α2-PI incorporation into the fibrin clot and whether the extent of incorporation has clinical consequences. Herein we calculated the extent of α2-PI incorporation by measuring α2-PI antigen levels from plasma and serum obtained after clotting the plasma by thrombin and Ca2+. The modifying effect of FXIII was studied by spiking of FXIII-A-deficient plasma with purified plasma FXIII. Fibrinogen, FXIII, α2-PI incorporation, in vitro clot-lysis, soluble fibroblast activation protein and α2-PI p.Arg6Trp polymorphism were measured from samples of 57 acute ischemic stroke patients obtained before thrombolysis and of 26 healthy controls. Increasing FXIII levels even at levels above the upper limit of normal increased α2-PI incorporation into the fibrin clot. α2-PI incorporation of controls and patients with good outcomes did not differ significantly (49.4 ± 4.6% vs. 47.4 ± 6.7%, p = 1.000), however it was significantly lower in patients suffering post-lysis intracranial hemorrhage (37.3 ± 14.0%, p = 0.004). In conclusion, increased FXIII levels resulted in elevated incorporation of α2-PI into fibrin clots. In stroke patients undergoing intravenous thrombolysis treatment, α2-PI incorporation shows an association with the outcome of therapy, particularly with thrombolysis-associated intracranial hemorrhage.

Hopf bifurcation in an activator–inhibitor system with network

2019 ◽  
Vol 98 ◽  
pp. 22-28
Author(s):  
Yanling Shi ◽  
Zuhan Liu ◽  
Canrong Tian
Keyword(s):  
Hopf Bifurcation ◽  
Inhibitor System ◽  
Activator Inhibitor

scholarly journals Different N-terminal forms of α2-plasmin inhibitor in human plasma

1993 ◽  
Vol 291 (2) ◽  
pp. 623-625 ◽  
Author(s):  
K Bangert ◽  
A H Johnsen ◽  
U Christensen ◽  
S Thorsen
Keyword(s):  
Human Plasma ◽  
Cdna Sequence ◽  
Recognition Site ◽  
Signal Peptidase ◽  
Stable Complex ◽  
N Terminus ◽  
Functional Implications ◽  
Plasmin Inhibitor

Mature alpha 2-plasmin inhibitor in human plasma has 12 more N-terminal residues than hitherto anticipated. The first residue is the methionine at position 28, downstream from the N-terminus of the pre-protein. The cDNA sequence predicts that the site cleaved upon formation of the mature inhibitor is a typical signal-peptidase recognition site. The mature inhibitor (464 residues) and the previously reported, and presumably degraded, form with N-terminal asparagine (452 residues), are present in plasma in about equal amounts. They both form a stable complex with plasmin. Recent studies on a recombinant alpha 2-plasmin inhibitor suggest that the 12 additional residues have functional implications [Sumi, Ichikawa, Nakamura, Miura and Aoki (1989) J. Biochem. 106, 703-707].

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