Fibrinogen In Liver Cirrhosis. Lack Of Correlation Between Soluble Fibrin Monomer Complexes And Fibrinopeptide A Levels

1981 ◽  
Author(s):  
S Coccheri ◽  
P M Mannucci ◽  
G Palareti ◽  
M Cattaneo ◽  
M Poggi ◽  
...  
Keyword(s):  
Liver Cirrhosis ◽  
Liver Biopsy ◽  
Half Life ◽  
Collaborative Study ◽  
Gel Filtration ◽  
Fibrinopeptide A ◽  
Confidence Limits ◽  
Parametric Test ◽  
Soluble Fibrin ◽  
The Difference

In this collaborative study we have investigated the coexistence of two different markers of fibrinogen to fibrin conversion in 19 patients with liver cirrhosis, confirmed with liver biopsy, and classified according to standardized criteria into 11 moderate and 8 severe cases. Sepharose gel filtration of plasma allowed separation of fibrinogen-like material (FLM) into high m.w. (HMWF), peak, and low m.w. (LMWF) fractions, quantitated as percent (w/w) of the total FLM eluted. FPA was assayed radioimmunologically.HMWF was markedly increased in the whole group of cirrhotics (av ± SD 10.4% ± 2.77) , and in both moderate and severe patients, vs controls (6.9% ± 1.39; n=16; p < 0.01 for each comparison). LMWF was moderately increased in patients (6.8% ± l.84) vs controls (5.3% ± 1.35; p < 0.05).FPA levels (controls: median (m) ng/ml 2.2; m confidence limits (mcl) 1.4-2.5; range (r) < 0.6 to 4.1) showed an increase in cirrhotics (m 2.8; mcl 2.64-3.35, r<0.6 to 94) but the difference was not statistically significant using a non-parametric test. However, in 6 out of 19 patients FPA values exceeded av ± 2 SD of controls (av ± SD 2.05 ± 1.15). No significant correlations were found between FPA and HMWF or LMWF levels.The lack of correlation between FPA and HMWF although possibly related to half-life differences, suggests that, besides thrombin effect, other mechanisms for excess formation and/or accumulation of HMWF, as dysproteinaemia, dys- fibrinogenaemia, or impaired clearance, should be considered.

Heparin Elimination in Patients with Liver Cirrhosis

1977 ◽  
Vol 38 (03) ◽  
pp. 0701-0706 ◽  
Author(s):  
Arne N. Teien
Keyword(s):  
Renal Function ◽  
Body Weight ◽  
Liver Cirrhosis ◽  
Normal Renal Function ◽  
Half Life ◽  
Antithrombin Iii ◽  
Normal Liver ◽  
Normal Group ◽  
Heparin Concentration ◽  
The Difference

SummaryHeparin (100 U/kg body-weight) was injected intravenously, and heparin concentration in plasma determined by polybrene titration. Mean heparin half-life was 117.8 min in a group of patients with liver cirrhosis and normal renal function (n = 6) as compared to 74.0 min in the normal group (n = 6). The difference between the two groups is statistically significant (p ≈ 0. 02). Heparin half-life was correlated to galactose half-life in the patients (r = 0.83, p = 0. 05). The findings suggest that heparin is metabolized in the liver. There was a significant fall in antithrombin III activities in the normals, but not in the patients. A possible explanation may be that the normal liver removes heparin bound to antithrombin III, and that this function is impaired in liver cirrhosis.

Relationship Between Fibrinopeptide A and Fibrinogen/Fibrin Fragment E in Thromboembolism, DIC and Various Non-Thromboembolic Diseases

1987 ◽  
Vol 58 (02) ◽  
pp. 758-763 ◽  
Author(s):  
G Mombelli ◽  
R Monotti ◽  
A Haeberli ◽  
P W Straub
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Liver Cirrhosis ◽  
Healthy Subjects ◽  
Vascular Diseases ◽  
Fibrinopeptide A ◽  
Normal Range ◽  
Collagen Vascular Diseases ◽  
Intravascular Coagulation ◽  
Fibrin Formation

SummaryIncreased fibrinopeptide A (FPA) levels have been reported in various non-thrombotic disorders, including cancer, acute myocardial infarction, liver cirrhosis and collagen vascular diseases. To investigate the significance of these findings, the present study combined the radioimmunoassay of FPA with that of fibrinogen/fibrin degradation fragment E (FgE) in the aforementioned disorders and compared the results with those observed in healthy subjects as well as in patients with thromboembolism and overt disseminated intravascular coagulation (DIC). Mean FPA and FgE in malignancy were 6.3 and 305 ng/ml, in myocardial infarction 5.6 and 98 ng/ml, in liver cirrhosis 2.7 and 132 ng/ml and in collagen vascular diseases 5.6 and 142 ng/ml. All these values were significantly higher than in healthy controls (mean FPA 1.6 ng/ml, mean FgE 49 ng/ml) but significantly lower than in thromboembolism (mean FPA 10.7 ng/ml, mean FgE 639 ng/ ml) and DIC (mean FPA 22.0 ng/ml, mean FgE 1041 ng/ml). The overall correlation between FPA and FgE was highly significant. Elowever, different disorders showed peculiar patterns in FPA, FgE and fibrinogen levels. In malignancy, a definite increase of FPA, FgE and plasma fibrinogen levels was observed. This finding probably indicates a compensated state of (intra- or extravascular) fibrin formation and lysis. Acute myocardial infarction was characterized by a high FPA to FgE ratio, which is interpreted to reflect acute thrombin generation and fibrin formation. FPA in cirrhosis was only marginally elevated with most single values within the normal range, indicating that intravascular coagulation was infrequent and unimportant in quantitative terms.

Apolipoprotein(a), Fibrinopeptide A and Carotid Atherosclerosis in Middle-Aged Men

1994 ◽  
Vol 72 (04) ◽  
pp. 563-566 ◽  
Author(s):  
Tuomo Rankinen ◽  
Sari Väisänen ◽  
Michele Mercuri ◽  
Rainer Rauramaa
Keyword(s):  
Risk Factors ◽  
Cardiovascular Diseases ◽  
Carotid Atherosclerosis ◽  
Intima Media Thickness ◽  
Carotid Bifurcation ◽  
Carotid Intima Media Thickness ◽  
Fibrinopeptide A ◽  
Carotid Imt ◽  
Apolipoprotein A ◽  
The Difference

SummaryThe association between apolipoprotein(a) [apo(a)], fibrinogen, fibrinopeptide A (FPA) and carotid intima-media thickness (IMT) was analyzed in Eastern Finnish men aged 50 to 60 years. Apo(a) correlated directly with carotid bifurcation (r = 0.26, p = 0.001), but not with common carotid IMT. Men in the lowest quartile of apo(a) had thinner (p = 0.013) IMT in bifurcation [1.59 mm (95% Cl 1.49; 1.68)] compared to the men in the highest [1.91 mm (95% Cl 1.73; 2.09)] apo(a) quartile. The difference remained (p=0.038) after adjusting for confounders. Plasma fibrinogen was not related to carotid IMT, whereas FPA correlated with common carotid (r = 0.21, p = 0.016) and carotid bifurcation (r = 0.21, p = 0.018) IMT. These associations abolished after adjusting for the confounders. The data suggest that apo(a) associate with carotid atherosclerosis independent of other risk factors for ischemic cardiovascular diseases.

Half-Life of Platelet Factor 4 (PF-4) in Plasma and Platelets from Macaca Mulatta

1977 ◽  
Vol 37 (01) ◽  
pp. 073-080 ◽  
Author(s):  
Knut Gjesdal ◽  
Duncan S. Pepper
Keyword(s):  
Macaca Mulatta ◽  
Half Life ◽  
Human Platelet ◽  
Gel Filtration ◽  
Platelet Factor 4 ◽  
Active Protein ◽  
Platelet Factor ◽  
Membrane Bound

SummaryHuman platelet factor 4 (PF-4) showed a reaction of complete identity with PF-4 from Macaca mulatta when tested against rabbit anti-human-PF-4. Such immunoglobulin was used for quantitative precipitation of in vivo labelled PF-4 in monkey serum. The results suggest that the active protein had an intra-platelet half-life of about 21 hours. In vitro 125I-labelled human PF-4 was injected intravenously into two monkeys and isolated by immuno-precipita-tion from platelet-poor plasma and from platelets disrupted after gel-filtration. Plasma PF-4 was found to have a half-life of 7 to 11 hours. Some of the labelled PF-4 was associated with platelets and this fraction had a rapid initial disappearance rate and a subsequent half-life close to that of plasma PF-4. The results are compatible with the hypothesis that granular PF-4 belongs to a separate compartment, whereas membrane-bound PF-4 and plasma PF-4 may interchange.

Soluble Fibrin Complexes and Fibrinogen Heterogeneity in Diabetes mellitus

1980 ◽  
Vol 44 (03) ◽  
pp. 130-134 ◽  
Author(s):  
E B Tsianos ◽  
N E Stathakis
Keyword(s):  
Diabetes Mellitus ◽  
Molecular Weight ◽  
Plasma Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Lower Molecular Weight ◽  
Polyacrylamide Gels ◽  
Soluble Fibrin ◽  
Α2 Macroglobulin ◽  
Patients With Diabetes

SummaryThe presence of soluble fibrin complexes (SFC) measured by gel filtration of plasma on 4% agarose columns, fibrinogen heterogeneity on 3.5% SDS-polyacrylamide gels and the concentrations of several plasma proteins were evaluated in 39 patients with diabetes mellitus (DM) and 19 matched control subjects. A small but significant increase of SFC was found in DM (p<0.01). On individual basis 51.2% of the patients had increased SFC (>M + 2 SD of the controls). Polyacrylamide gel electrophoresis of the SFC showed no evidence of cross-linking or proteolysis. Plasma clots formed in the presence of EDTA and trasylol were analysed in SDS-polyacrylamide gels in a normal and two lower molecular weight fibrin bands (band I, II, III). The percentage of band I fibrinogen was in diabetics (65.3 ± 4.7%) lower than that of the controls (71.8 ± 4.5%) (p < 0.01). Fibrinogen levels, antithrombin III, α1-antitrypsin, α2-macroglobulin and plasminogen were significantly increased in DM. We suggest that in DM there is an enhancement of intravascular fibrin formation and accelerated fibrinogen degradation to lower molecular weight forms.

Turnover of Human Extrinsic (Tissue-Type) Plasminogen Activator in Rabbits

1981 ◽  
Vol 46 (03) ◽  
pp. 658-661 ◽  
Author(s):  
C Korninger ◽  
J M Stassen ◽  
D Collen
Keyword(s):  
Plasminogen Activator ◽  
Intravenous Injection ◽  
Active Site ◽  
Half Life ◽  
Degradation Products ◽  
Gel Filtration ◽  
Tissue Type ◽  
Organ Distribution ◽  
Small Rise

SummaryThe turnover of highly purified human extrinsic plasminogen activator (EPA) (one- and two-chain form) was studied in rabbits. Following intravenous injection, EPA-activity declined rapidly. The disappearance rate of EPA from the plasma could adequately be described by a single exponential term with a t ½ of approximately 2 min for both the one-chain and two-chain forms of EPA.The clearance and organ distribution of EPA was studied by using 125I-labeled preparations. Following intravenous injection of 125I-1abeled EPA the radioactivity disappeared rapidly from the plasma also with a t ½ of approximately 2 min down to a level of 15 to 20 percent, followed by a small rise of blood radioactivity. Gel filtration of serial samples revealed that the secondary increase of the radioactivity was due to the reappearance of radioactive breakdown products in the blood. Measurement of the organ distribution of 125I at different time intervals revealed that EPA was rapidly accumulated in the liver, followed by a release of degradation products in the blood.Experimental hepatectomy markedly prolonged the half-life of EPA in the blood. Blocking the active site histidine of EPA had no effect on the half-life of EPA in blood nor on the gel filtration patterns of 125I in serial plasma samples.It is concluded that human EPA is rapidly removed from the blood of rabbits by clearance and degradation in the liver. Recognition by the liver does not require a functional active site in the enzyme. Neutralization in plasma by protease inhibitors does not represent a significant pathway of EPA inactivation in vivo.

scholarly journals Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the corresponding cDNA

1997 ◽  
Vol 325 (3) ◽  
pp. 761-769 ◽  
Author(s):  
Isabelle GARCIA ◽  
Matthew RODGERS ◽  
Catherine LENNE ◽  
Anne ROLLAND ◽  
Alain SAILLAND ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Gel Filtration ◽  
Peptide Sequence ◽  
Amino Acid Residues ◽  
Carrot Cells ◽  
Expression Studies ◽  
Sds Page ◽  
Molecular Masses ◽  
The Difference ◽  
Dioxygenase Activity

p-Hydroxyphenylpyruvate dioxygenase catalyses the transformation of p-hydroxyphenylpyruvate into homogentisate. In plants this enzyme has a crucial role because homogentisate is the aromatic precursor of all prenylquinones. Furthermore this enzyme was recently identified as the molecular target for new families of potent herbicides. In this study we examine precisely the localization of p-hydroxyphenylpyruvate dioxygenase activity within carrot cells. Our results provide evidence that, in cultured carrot cells, p-hydroxyphenylpyruvate dioxygenase is associated with the cytosol. Purification and SDS/PAGE analysis of this enzyme revealed that its activity is associated with a polypeptide of 45–46 kDa. This protein specifically cross-reacts with an antiserum raised against the p-hydroxyphenylpyruvate dioxygenase of Pseudomonas fluorescens. Gel-filtration chromatography indicates that the enzyme behaves as a homodimer. We also report the isolation and nucleotide sequence of a cDNA encoding a carrot p-hydroxyphenylpyruvate dioxygenase. The nucleotide sequence (1684 bp) encodes a protein of 442 amino acid residues with a molecular mass of 48094 Da and shows specific C-terminal regions of similarity with other p-hydroxyphenylpyruvate dioxygenases. This cDNA encodes a functional p-hydroxyphenylpyruvate dioxygenase, as evidenced by expression studies with transformed Escherichia coli cells. Comparison of the N-terminal sequence of the 45–46 kDa polypeptide purified from carrot cells with the deduced peptide sequence of the cDNA confirms that this polypeptide supports p-hydroxyphenylpyruvate dioxygenase activity. Immunodetection studies of the native enzyme in carrot cellular extracts reveal that N-terminal proteolysis occurs during the process of purification. This proteolysis explains the difference in molecular masses between the purified protein and the deduced polypeptide.

Early manifestations and first-contact incidence of schizophrenia in different cultures: A preliminary report on the initial evaluation phase of the WHO Collaborative Study on Determinants of Outcome of Severe Mental Disorders

1986 ◽  
Vol 16 (4) ◽  
pp. 909-928 ◽  
Author(s):  
N. Sartorius ◽  
A. Jablensky ◽  
A. Korten ◽  
G. Ernberg ◽  
M. Anker ◽  
...  
Keyword(s):  
Collaborative Study ◽  
Strong Support ◽  
Developed Countries ◽  
Incidence Rates ◽  
Symptom Profiles ◽  
Evaluation Phase ◽  
Different Populations ◽  
The Difference ◽  
Different Cultures ◽  
First Contact

SynopsisIn a context of a WHO collaborative study, 12 research centres in 10 countries monitored geographically defined populations over 2 years to identify individuals making a first-in-lifetime contact with any type of ‘helping agency’ because of symptoms of psychotic illness. A total of 1379 persons who met specified inclusion criteria for schizophrenia and other related non-affective disorders were examined extensively, using standardized instruments, on entry into the study and on two consecutive follow-ups at annual intervals. Patients in different cultures, meeting the ICD and CATEGO criteria for schizophrenia, were remarkably similar in their symptom profiles and 49% of them presented the central schizophrenic conditions as defined by CATEGO class S+. However, the 2-year pattern of course was considerably more favourable in patients in developing countries compared with patients in developed countries, and the difference could not be fully explained by the higher frequency of acute onsets among the former. Age- and sex-specific incidence rates and estimates of disease expectancy were determined for a ‘broad’ diagnostic group of schizophrenic illness and for CATEGO S+ cases. While the former showed significant differences among the centres, the differences in the rates for S+ cases were non-significant or marginal. The results provide strong support for the notion that schizophrenic illnesses occur with comparable frequency in different populations and support earlier findings that the prognosis is better in less industrialized societies.

Rate of loss of radioiron from mouse and man

1960 ◽  
Vol 198 (4) ◽  
pp. 784-786 ◽  
Author(s):  
John D. Bonnet ◽  
Alan L. Orvis ◽  
Albert B. Hagedorn ◽  
Charles A. Owen
Keyword(s):  
Life Span ◽  
Half Life ◽  
Whole Body ◽  
Entire Body ◽  
Rapid Loss ◽  
Male And Female ◽  
Female Mice ◽  
Steady Rate ◽  
Normal Man ◽  
The Difference

Forty-two male and female mice, 8 weeks old, were given radioiron (Fe59) in doses of 0.006–0.1 µc, containing 0.013–0.17 µg of iron, by intraperitoneal or intravenous routes. Assays of the radioactivity of the whole body revealed an initial rapid loss of Fe59 (15–20%) lasting about 6 days. Thereafter the Fe59 left the mice at a steady rate of 0.39%/day (half-life 180 days). One 34-year-old normal man was given 10.6 µc of Fe59, containing 8.2 µg of iron, intravenously. Based on counts from the entire body, the biologic rate of loss of the Fe59 was about 0.14%/day (half-life 500 days), and there was little or no initial loss such as occurred in the mouse. The Fe59 in the circulating erythrocytes was essentially unchanged for the first 3 months. It then fell to a new level of about 90% of the previous one; the mid-point of the fall was about 120 days after the administration of the radioiron. The difference in the rates of loss of radioiron from mice and man seems to be related primarily to the life span of the circulating red cells.

High Pressure Liquid Chromatographic Determination of Fensulfothion: Collaborative Study

1983 ◽  
Vol 66 (3) ◽  
pp. 801-803
Author(s):  
Margie E Owen ◽  
◽  
O O Bennett ◽  
L T Chenery ◽  
C J Cohen ◽  
...  
Keyword(s):  
Coefficient Of Variation ◽  
Collaborative Study ◽  
Internal Standard ◽  
Chromatographic Determination ◽  
Peak Height ◽  
Matched Pair ◽  
Standard Material ◽  
Liquid Chromatographic Determination ◽  
The Difference ◽  
Liquid Chromatographic

Abstract A method for analyzing fensulfothion was tested by 10 collaborators. Formulations were dissolved, or extracted from inerts, in methanol. Benzophenone was used as an internal standard. The solution was diromatographed on a Partisil-10 ODS-2, or equivalent, reverse phase column, and detected at 230 nm. A mobile phase of methanol-water-phosphoric acid was used. The ratio of fensulfothion peak height to benzophenone peak height was calculated from the UV response and compared to the standard material for quantitation. A 15% granular formulation was analyzed as a matched pair. The results of one collaborator were outliers by the Dixon test. The coefficient of variation for the granular formulation was 1.6%. A matched pair of 63% spray concentrate samples was analyzed by 10 collaborators. The difference in results was an outlier for one collaborator; the coefficient of variation for the other collaborators was 1.5%. The method has been adopted official first action.

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