Effects of Certain Phospholipids on Plasminogen Activation and Plasmin Activity

SummaryCrude and partially purified phospholipid preparations have been studied for their effects on a) the activation of purified human plasminogen by streptokinase and b) the activity of plasmin resulting from such activation. Plasmin activity has been measured as BAMe esterase, caseinolytic, and fibrinolytic activities.Plasmin BAMe esterase activity was significantly enhanced by phosphatidyl inositol and phosphatidyl serine but only slightly by phosphatidyl ethanolamine. Preparations of asolectin and cephalin, although not having any effect on plasmin BAMe esterase activity per se, did appear to increase plasminogen activation by streptokinase. None of the above-mentioned effects was observed when plasmin caseinolytic activity was measured. The phospholipid preparation having the greatest effect on plasmin BAMe esterase activity, phosphatidyl inositol, also exhibited an effect on plasmin fibrinolytic activity. With both BAMe esterase and fibrinolytic activities the effects produced by the phospholipid materials were concentration dependent and, in the case of fibrinolytic activity, increased concentrations beyond the optimum level resulted in a gradual diminution in activity and eventual inhibition.

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Platelet Phospholipid Changes in Atherosclerosis

10.1055/s-0039-1680410 ◽

1977 ◽

Author(s):

A. Z. Aktulga ◽

O. N. Ulutin

Keyword(s):

Fibrinolytic Activity ◽

Phosphatidyl Ethanolamine ◽

Total Phospholipid ◽

Phosphatidyl Inositol ◽

Phosphatidyl Serine ◽

Platelet Phospholipid ◽

Lipid Contents ◽

Coagulation Mechanism ◽

The Individual ◽

Platelet Functions

The platelet phospholipids content and their per cent distribution in atherosclerotic cases and in thromboembolic cases related to atherosclerosis was investigated with respect to normals. In normals the total phospholipid phosphorus value was found to be 10.88±0.24μg/109 platelets whereas this value changed to 14.29±0.39μg/109 platelets in atherosclerosis. The individual phospholipids follow the decreasing order of phosphatidyl choline, phosphatidyl ethanolamine, sphingomyeline, phosphatidyl serine, phosphatidyl inositol. In atherosclerotic cases although no difference was observed in this order, there was an increase in the quantity of certain phospholipids. In these cases the coagulation mechanism, the fibrinolytic activity, the platelet functions, and the serum lipid contents were also investigated in comparison to the above findings.

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Screening Tests of Reproductive Immunology in Systemic Lupus Erythematosus

Autoimmune Diseases ◽

10.1155/2012/812138 ◽

2012 ◽

Vol 2012 ◽

pp. 1-6 ◽

Cited By ~ 2

Author(s):

Zdenka Ulcova-Gallova ◽

Alice Mockova ◽

Miroslava Cedikova

Keyword(s):

Systemic Lupus Erythematosus ◽

Lupus Erythematosus ◽

Phosphatidyl Ethanolamine ◽

Phosphatidyl Inositol ◽

Phosphatidyl Serine ◽

Sperm Cells ◽

Systemic Lupus ◽

Ethanolamine Phosphatidyl ◽

Glycoprotein I ◽

Beta 2

Female patients in reproductive age with systemic lupus erythematosus and fertility complications together are observed by rheumatologists, gynecologists, and reproductive immunologists. The paper notes the presence of autoantibodies to zona pellucida, to phospholipids (phosphatidyl serine, phosphatidyl ethanolamine, phosphatidyl inositol, phosphatidyl glycerol, phosphatidic acid, annexin V, beta-2 glycoprotein I, and cardiolipin) and of isoantibodies to sperm cells. Isoantibodies to sperm cells are not significantly predominant, but autoimmunity is well expressed in IgG positivity against phosphatidyl inositol, phosphatidyl ethanolamine, phosphatidyl serine, cardiolipin, and beta-2 glycoprotein I, as well as antizona pellucida antibodies in IgG isotype. According to the levels of autoantibodies we have to choose preventive treatment to protect mother and her foetus.

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METABOLISM OF EHRLICH ASCITES TUMOR IN VITRO: SUBCELLULAR DISTRIBUTION OF PHOSPHOLIPIDS NEWLY FORMED FROM14C-LABELED PRECURSORS

Canadian Journal of Biochemistry ◽

10.1139/o66-166 ◽

1966 ◽

Vol 44 (11) ◽

pp. 1461-1468 ◽

Cited By ~ 3

Author(s):

V. Donisch ◽

R. J. Rossiter

Keyword(s):

Microsomal Fraction ◽

Phosphatidyl Ethanolamine ◽

Lipid Fraction ◽

Specific Radioactivity ◽

Phosphatidyl Inositol ◽

Phosphatidyl Serine ◽

Ethanolamine Phosphatidyl ◽

Ehrlich Ascites ◽

Ethanolamine Plasmalogen

When Ehrlich ascites cells were incubated in a suitable medium containing choline-1,2-14C, ethanolamine-1,2-14C, L-serine-14C, or glycerol-1-14C, radioactivity was recovered from the lipid fraction. With choline-1,2-14C, radioactivity was incorporated into the three choline-containing phospholipids, lecithin, choline plasmalogen, and sphingomyelin. Radioactivity from ethanolamine-1,2-14C was incorporated into phosphatidyl ethanolamine, ethanolamine plasmalogen, choline plasmalogen, and lecithin. Radioactivity from L-serine-14C was incorporated into phosphatidyl serine, serine plasmalogen, and phosphatide acid, with lesser amounts into phosphatidyl ethanolamine, lecithin, ethanolamine plasmalogen, choline plasmalogen, and sphingomyelin. Radioactivity from glycerol-1-14C was incorporated into the glycerophosphatides, phosphatidic acid, lecithin, phosphatidyl ethanolamine, phosphatidyl serine, phosphatidyl inositol, and choline plasmalogen. Radioactivity from this precursor was also incorporated into sphingomyelin.In all instances, radioactivity was recovered from the phosphatides in the nuclear, mitochondrial, and microsomal fractions of the tumor. Usually, the specific radioactivity of the phosphatides in the microsomal fraction exceeded that in the other two subcellular fractions.

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Regulation of fibrinolysis by non-esterified fatty acids

Biochemical Journal ◽

10.1042/bj3000251 ◽

1994 ◽

Vol 300 (1) ◽

pp. 251-255 ◽

Cited By ~ 18

Author(s):

A A Higazi ◽

R Aziza ◽

A A Samara ◽

M Mayer

Keyword(s):

Oleic Acid ◽

Palmitic Acid ◽

Fibrinolytic Activity ◽

Fibrin Clot ◽

Plasminogen Activation ◽

Plasmin Activity ◽

Esterified Fatty Acids ◽

Marked Inhibition ◽

Sds Page ◽

Dependent Inhibition

The ability of oleic acid to modulate fibrinolysis was measured by following the urokinase-mediated and plasminogen-dependent cleavage of 125I-labelled fibrin clots. Oleic acid levels within the physiological range exerted a concentration-dependent inhibition of urokinase-mediated fibrinolytic activity. SDS/PAGE revealed that oleic acid enhances urokinase activity but simultaneously increases the autolytic cleavage of the newly formed low-molecular-mass subunit of plasmin. Oleic acid-induced cleavage of this subunit containing the catalytic site of plasmin was suppressed by the plasmin substrate H-D-valyl-L-leucyl-L-lysine-p-nitroanilide (S-2251) and was prevented by alpha 2-antiplasmin. A concentration-dependent inhibition of the activity of purified plasmin on 125I-labelled fibrin clot was also observed; 93% and 50% inhibition was noted with 150 microM and 32 microM oleic acid respectively. Oleic acid at 200 microM also effectively displaced plasmin prebound to a polylysine-Sepharose column. Examination of the fatty acid specificity showed that a minimal chain length of 16 carbon atoms and the presence of at least one double bond, preferably in a cis configuration, were required for inhibition of the fibrinolytic activity of plasmin. Oleic acid at a concentration that produced only a minimal inhibition of plasmin activity induced a marked inhibition by palmitic acid, while palmitic acid alone is ineffective. The findings suggest that oleic acid stimulates plasminogen activation and modulates the fibrinolytic and autolytic activities of plasmin.

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Clotting Activity of Platelet Phospholipids in Rat and Man

Thrombosis and Haemostasis ◽

10.1055/s-0038-1647707 ◽

1974 ◽

Vol 32 (02/03) ◽

pp. 382-390 ◽

Cited By ~ 4

Author(s):

P Gautheron ◽

E Dumont ◽

S Renaud

Keyword(s):

Phosphatidyl Choline ◽

Phosphatidyl Ethanolamine ◽

Phosphatidyl Inositol ◽

Phosphatidyl Serine ◽

The Other ◽

Active Fraction ◽

Platelet Phospholipid ◽

Experimental Conditions ◽

Ethanolamine Phosphatidyl ◽

Recalcification Time

SummaryThe clotting activity of man and rat platelet phospholipid fractions separated by bi-dimensional TLC, resuspended in Tyrode by sonication, was studied in the recalcification (manual) and in the Stypven (recalcification plus Russell’s viper venom) clotting time (determined in a coagulometer). Phosphatidyl serine was the most active fraction to shorten the two clotting tests utilized, in both rat and man, but it was much more effective in the Stypven time. The phosphatidyl ethanolamine was the second most active fraction, in the Stypven time; this fraction was almost as active as phosphatidyl serine in both animal species. The other fractions studied (phosphatidyl inositol, phosphatidyl choline and sphingomyelin) were sligthly active or not active, depending on the experimental conditions.The clotting activity of platelet phosphatidyl serine from rat, at concentrations corresponding to platelet counts from 1 to 10 ( X105), was much smaller than this of the disrupted (sonicated) platelets from which it originated. However, the clotting activity of sonicated platelets could be completely reproduced, either at each concentration studied (Stypven time) or at a concentration corresponding to lOxlO5 platelets (recalcification time), by adding to phosphatidyl serine the other four phospholipid fractions (phosphatidyl inositol, phosphatidyl ethanolamine, phosphatidyl choline, sphingomyelin) dispersed in a homogeneous way by sonication.The feeding of a butter-rich diet to rats considerably increased the activity of each of the platelet phospholipid fractions in the two clotting tests carried out.

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Different Assessment of Plasmin with Different Substrates

Thrombosis and Haemostasis ◽

10.1055/s-0038-1650029 ◽

1980 ◽

Vol 43 (02) ◽

pp. 112-117 ◽

Cited By ~ 3

Author(s):

B Lämmle ◽

F Duckert ◽

Ch Bondeli ◽

L Hänni ◽

Keyword(s):

Fibrinolytic Activity ◽

The Other ◽

Amidolytic Activity ◽

Chromogenic Substrates ◽

Plasmin Activity ◽

Fibrin Plate ◽

Caseinolytic Activity

SummaryThe alteration of human and porcine plasmin and the influence of EACA and AMCHA on their activity were investigated. Solutions of both plasmins undergo storage induced alteration, which is best recorded by Chromozym PL, whereas the other chromogenic substrates, S-2251 and S-2302, and casein are less sensitive, and the fibrin plate inadequate. Plasmin amidolytic and fibrinolytic activity is maximally enhanced at 7.6 × 10–3 M EACA and 6.4 × 10–4 M AMCHA, and decay through storage is reversed. The caseinolytic activity seems slightly inhibited at the same EACA and AMCHA concentrations.Our results show:1. The quotient: plasmin activity towards Chromozym PL/Activity towards S-2251 is a useful indicator of "plasmin quality". The quotient decreases markedly upon storage of plasmin solutions.2. Plasmin stability is improved in the presence of AMCHA.3. It is valueless to add EACA or AMCHA to inhibit plasmin in amidolytic assays since the chosen concentration enhances the amidolytic activity of already formed plasmin.

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Lipidomic profiling of the developing kernel clarifies the lipid metabolism of Paeonia ostii

Scientific Reports ◽

10.1038/s41598-021-91984-9 ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

Shui-Yan Yu ◽

Ying Zhang ◽

Yu-Ping Lyu ◽

Zu-Jie Yao ◽

Yong-Hong Hu

Keyword(s):

Phosphatidyl Ethanolamine ◽

Phosphatidyl Inositol ◽

Phosphatidyl Serine ◽

Sphingolipid Metabolism ◽

Phosphatidyl Glycerol ◽

Alpha Linolenic Acid ◽

Oil Accumulation ◽

Oil Crops ◽

Sphingosine 1 Phosphate ◽

Fatty Acyls

AbstractLipid components in the developing kernel of Paeonia ostii were determined, and the fatty acid (FA) distributions in triacylglycerol and phospholipids were characterized. The lipids in the kernel were mainly phospholipids (43%), neutral glycerides (24%), fatty acyls (26%), and sphingolipids (4.5%). The dominant neutral glycerides were TAG and diacylglycerol. The PL components included phosphatidic acid, phosphatidyl glycerol, phosphatidyl choline, phosphatidyl serine, phosphatidyl inositol, and phosphatidyl ethanolamine. As the kernel developed, the profiles of the molecular species comprising TAG and PL changed, especially during the earlier phases of oil accumulation. During rapid oil accumulation, the abundances of sphingosine-1-phosphate, pyruvic acid, stearic acid, and alpha-linolenic acid changed significantly; the sphingolipid metabolism and unsaturated FAs biosynthesis pathways were significantly enriched in these differentially abundant metabolites. Our results improve our understanding of lipid accumulation in tree peony seeds, and provide a framework for the analysis of lipid metabolisms in other oil crops.

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STUDIES ON PLASMINOGEN: II. A COMPARISON OF THE ESTEROLYTIC, CASEINOLYTIC, AND FIBRINOLYTIC ACTIVITIES OF BOVINE AND HUMAN PLASMINOGEN

Canadian Journal of Biochemistry and Physiology ◽

10.1139/o61-211 ◽

1961 ◽

Vol 39 (12) ◽

pp. 1911-1919

Author(s):

Edmond R. Cole ◽

Edwin T. Mertz

Keyword(s):

Chemical Treatment ◽

Phosphate Buffer ◽

Fibrinolytic Activity ◽

Similar Relationship ◽

Single Straight Line ◽

Straight Line ◽

Caseinolytic Activity ◽

Esterolytic Activity ◽

Human Plasminogen ◽

Line Relationship

Preparations of bovine and human plasminogen which varied in purity and mode of preparation were activated and assayed for esterolytic, caseinolytic, and fibrinolytic activities. Variations in the ratio of attack of bovine plasmin on TAMe and casein were observed among the plasminogen preparations which represent different stages of purification. Two plasminogen products with different TAMe/casein ratios were separated from both bovine and human products with intermediate TAMe/casein ratios, by the use of phosphate buffer as a precipitant. Bovine plasminogen preparations extracted with acid, then subjected to alkali denaturation, were purified with respect to their caseinolytic activity, but the esterolytic activity remained the same or decreased, resulting in a decrease in the TAMe/casein ratio. Human plasminogen prepared from fraction III by this method showed as much as a fourfold decrease in the TAMe/casein ratio. The observed differences in activity of various plasminogen preparations towards the two substrates, TAMe and casein, may arise from the chemical treatment and manipulation that the proenzyme receives during purification. When the fibrinolytic activity was compared with the caseinolytic activity, a single straight-line relationship was obtained for both bovine and human plasminogen preparations. However, a similar relationship was not found between the fibrinolytic and esterolytic activities.

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FORMATION OF PHOSPHATIDES FROM C14-LABELLED PRECURSORS IN RAT BRAIN SLICES. EFFECT OF CHLORPROMAZINE

Canadian Journal of Biochemistry and Physiology ◽

10.1139/y63-043 ◽

1963 ◽

Vol 41 (1) ◽

pp. 341-345 ◽

Cited By ~ 3

Author(s):

E. T. Pritchard ◽

R. J. Rossiter

Keyword(s):

Guinea Pig ◽

Phosphatidic Acid ◽

Rat Brain ◽

Phosphatidyl Ethanolamine ◽

Brain Slices ◽

Phosphatidyl Inositol ◽

Phosphatidyl Serine ◽

Inorganic P ◽

The Individual ◽

Guinea Pig Brain

The addition of chlorpromazine (0.1 mM) to slices of rat brain respiring in a suitable medium caused an increase in the incorporation of radioactivity from glycerol-1-C14, glycine-2-C14, and serine-3-C14 into the phospholipids of the slices. There was no increase in the incorporation of radioactivity from choline-1,2-C14 or ethanolamine-1,2-C14. Examination of the individual phosphatides showed an increase in the incorporation of radioactivity from glycerol-1-C14 into phosphatidc acid and phosphatidyl serine, with no change for lecithin and phosphatidyl ethanolamine. Higher concentrations of chlorpromazine (1.0 mM) either inhibited (glycerol-1-C14, choline-1,2-C14), did not significantly alter (glycine-2-C14, ethanolamine-1,2-C14), or stimulated (serine-3-C14) the incorporation of radioactivity into phospholipids. These results are discussed in relation to previous experiments, in which it was found that the addition of chlorpromazine (0.1 mM) to slices of guinea pig brain caused an increase in the incorporation of inorganic P32 into phosphatidic acid, phosphatidyl inositol, phosphatidyl serine, but not into lecithin or phosphatidyl ethanolamine.

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