Activation of human plasma prekallikrein by Pseudomonas aeruginosa elastase in vitro

1991 ◽  
Vol 1097 (1) ◽  
pp. 23-27 ◽  
Author(s):  
Yoko Shibuya ◽  
Hideaki Tanaka ◽  
Norikazu Nishino ◽  
Hiroaki Okabe ◽  
Takeshi Kambara ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Human Plasma ◽  
Pseudomonas Aeruginosa Elastase

Experimental studies of the pathogenesis of infections owing to Pseudomonas aeruginosa: elastase, an IgG protease

1984 ◽  
Vol 30 (9) ◽  
pp. 1118-1124 ◽  
Author(s):  
Ian Alan Holder ◽  
Robert Wheeler
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Protease Inhibitor ◽  
Protective Effect ◽  
Local Treatment ◽  
Experimental Studies ◽  
Normal Human ◽  
Pseudomonas Aeruginosa Elastase ◽  
Insight Into

Pseudomonas aeruginosa elastase, but not alkaline protease, degraded pooled, normal, human IgG in vitro and this degraded IgG lost its protective effect when used to treat burned, P. aeruginosa infected mice. Plasma IgG levels in burned, uninfected mice declined immediately postburning, but remained relatively constant thereafter; the levels in burned, P. aeruginosa infected mice continued to decline until death ensued. Infection of burned mice with an elastase+ strain caused the IgG decline, while infection with an elastase− strain did not, suggesting that elastase production caused the in vivo decline in plasma IgG. Local treatment with the protease inhibitor α2-macroglobulin, of burned mice infected with an elastase+ organism, reduced the IgG decline observed in control mice. These data support the hypothesis that P. aeruginosa elastase acts as an IgG protease both in vitro and in vivo and gives insight into how this enzyme may act as a virulence factor in P. aeruginosa.

scholarly journals In Vitro Inhibition of Pseudomonas aeruginosa Elastase by Metal-Chelating Peptide Derivatives

1982 ◽  
Vol 38 (2) ◽  
pp. 716-723 ◽  
Author(s):  
Efrat Kessler ◽  
Mary Israel ◽  
Nahum Landshman ◽  
Aaron Chechick ◽  
Shmaryahu Blumberg
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Metal Chelating ◽  
Peptide Derivatives ◽  
In Vitro Inhibition ◽  
Pseudomonas Aeruginosa Elastase

Potentially Thrombogenic Materials in Factor IX Concentrates

1975 ◽  
Vol 33 (03) ◽  
pp. 617-631 ◽  
Author(s):  
H. S Kingdon ◽  
R. L Lundblad ◽  
J. J Veltkamp ◽  
D. L Aronson
Keyword(s):  
Human Plasma ◽  
Antithrombin Iii ◽  
Factor Ix ◽  
In Vitro Assays ◽  
Substantial Agreement ◽  
Coefficient Of Correlation

SummaryFactor IX concentrates manufactured from human plasma and intended for therapeutic infusion in man have been suspected for some time of being potentially thrombogenic. In the current studies, assays were carried out in vitro and in vivo for potentially thrombogenic materials. It was possible to rank the various materials tested according to the amount of thrombogenic material detected. For concentrates not containing heparin, there was substantial agreement between the in vivo and in vitro assays, with a coefficient of correlation of 0.77. There was no correlation between the assays for thrombogenicity and the antithrombin III content. We conclude that many presently available concentrates of Factor IX contain substantial amounts of potentially thrombogenic enzymes, and that this fact must be considered in arriving at the decision whether or not to use them therapeutically.

Presence and Possible Origin of ɛ(γ-Glutamyl)Lysine Isodipeptide in Human Plasma

1992 ◽  
Vol 67 (01) ◽  
pp. 060-062 ◽  
Author(s):  
J Harsfalvi ◽  
E Tarcsa ◽  
M Udvardy ◽  
G Zajka ◽  
T Szarvas ◽  
...  
Keyword(s):  
Human Plasma ◽  
Fibrinolytic Therapy ◽  
Normal Human Plasma ◽  
Normal Human ◽  
Hplc Technique ◽  
Significant Change

Summaryɛ(γ-glutamyl)lysine isodipeptide has been detected in normal human plasma by a sensitive HPLC technique in a concentration of 1.9-3.6 μmol/1. Incubation of in vitro clotted plasma at 37° C for 12 h resulted in an increased amount of isodipeptide, and there was no further significant change when streptokinase was also present. Increased in vivo isodipeptide concentrations were also observed in hypercoagulable states and during fibrinolytic therapy.

Observations on the in vitro Effects of Chylomicra, Low-Density Lipoproteins and Phospholipids on Human Plasma Euglobulin Lysis

1963 ◽  
Vol 09 (01) ◽  
pp. 164-174 ◽  
Author(s):  
Albert R Pappenhagen ◽  
J. L Koppel ◽  
John H Olwin
Keyword(s):  
Human Plasma ◽  
Phosphatidyl Ethanolamine ◽  
Phosphatidyl Inositol ◽  
Plasma Lipoproteins ◽  
Low Density ◽  
Inhibitory Effects ◽  
Soybean Phospholipids ◽  
In Vitro Effects ◽  
Complete Precipitation

SummaryData have been presented on the in vitro effects of human chylomicra, low-density human plasma lipoproteins, and partially purified preparations of various phospholipids on human plasma euglobulin lysis. Euglobulin lysis was found to be accelerated by preparations of mixed soybean phospholipids (aso-lectin), cephalin, phosphatidyl inositol, phophatidyl serine and phosphatidyl ethanolamine. In contrast, it was found to be inhibited by preparations of human chylomicra, low-density human plasma liproproteins and lecithin. Inhibition of euglobulin lysis produced by any of these three agents could be diminished or completely overcome by the simultaneous presence of suitable levels of any one of the accelerating agents. In all cases studied, both inhibitory and accelerating effects were observed to be concentration-dependent. Evidence has been obtained to suggest that in the case of the accelerating agents the observed increased rate of euglobulin lysis is not a direct effect on lysis itself, but rather is due to more complete precipitation of plasminogen in the presence of these substances. On the other hand, it appears that the inhibitory effects observed are not related to the extent of plasminogen precipitation, but are actually true inhibitions of euglobulin lysis. The possible clinical significance of some of these observations has been briefly discussed.

Absence of Synergism Between Tissue-Type Plasminogen Activator (t-PA), Single-Chain UrokinaseType Plasminogen Activator (scu-PA) and Urokinase on Clot Lysis in a Plasma Milieu In Vitro

1986 ◽  
Vol 56 (01) ◽  
pp. 035-039 ◽  
Author(s):  
D Collen ◽  
F De Cock ◽  
E Demarsin ◽  
H R Lijnen ◽  
D C Stump
Keyword(s):  
Human Plasma ◽  
Plasminogen Activator ◽  
Dose Response ◽  
Fibrinolytic System ◽  
Tissue Type ◽  
Clot Lysis ◽  
Single Chain ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator

SummaryA potential synergic effect of tissue-type plasminogen activator (t-PA), single-chain urokinase-type plasminogen activator (scuPA) or urokinase on clot lysis was investigated in a whole human plasma system in vitro. The system consisted of a human plasma clot labeled with 125I-fibrinogen, immersed in titrated whole human plasma, to which the thrombolytic agents were added. Clot lysis was quantitated by measurement of released 125I, and activation of the fibrinolytic system in the surrounding plasma by measurements of fibrinogen and α2-antiplasmin.t-PA, scu-PA and urokinase induced a dose-dependent and time-dependent clot lysis; 50 percent lysis after 2 h was obtained with 5 nM t-PA, 20 nM scu-PA and 12 nM urokinase. At these concentrations no significant activation of the fibrinolytic system in the plasma was observed with t-PA and scu-PA, whereas urokinase caused significant α2-antiplasmin consumption and concomitant fibrinogen degradation. The shape of the dose-response curves was different; t-PA and urokinase showed a log linear dose-response whereas that of scu-PA was sigmoidal.

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