Correction of the Delayed Fibrin Aggregation of Fetal Fibrinogen by Partial Removal of Sialic Acid

1979 ◽  
Author(s):  
D.K. Galanakis ◽  
M.W. Mosesson
Keyword(s):  
Sialic Acid ◽  
Acid Content ◽  
Acid Value ◽  
Full Term ◽  
Thrombin Time ◽  
Sialic Acid Content ◽  
Vibrio Cholera ◽  
The Mean ◽  
Fraction I ◽  
Free Sialic Acid

Human umbilical oord fibrinogen characteristically displays delayed fibrin aggregation under conditions of relatively high ionic strength. This delay is greater in fibrinogen obtained from premature (p) (24–35 weeks gestation) infants, as compared with that from full term (FT) infants. We compared the sialic acid content of (fraction I-2) fetal (P and FT) with adult (A) fibrinogen, obtained from pooled plasma. The mean sialic acid μg/100mg protein) values were: P, 818 (±135 SD, range 621–1030); FT, 720 (±212, range 505–1280); A, 626 (±110, range 487-806). One P fibrinogen preparation (thrombin time 22.6 seconds) was partially desialated (resulting sialic acid value 490) by incubation with Vibrio cholera neuraminidase, dialyzed , and precipitated with ethanol to remove free sialic acid. The thrombin time of the resulting preparation was 15.4 (range 15.2–15.8), compared to 16.1 (range 15.5–16.4) for untreated A fibrinogen. The results suggest that the delayed fibrin aggregation of fetal fibrinogen is attributable to its relatively high sialic acid content. Moreover, the intermediate sialic acid (and thrombin time) values of FT (as compared to those of p) fibrinogen intimate the presence of a mixture of adult and fetal fibrinogen in full term cord blood.

scholarly journals Role of Sialic Acid in the Dysfibrinogenemia Associated with Liver Disease

1977 ◽  
Author(s):  
J. Martinez ◽  
J. Palascak ◽  
D. Kwasniak ◽  
S.S. Shapiro
Keyword(s):  
Liver Disease ◽  
Sialic Acid ◽  
Acid Content ◽  
Polyacrylamide Gel Electrophoresis ◽  
Precipitation Method ◽  
Thrombin Time ◽  
Functional Abnormality ◽  
Sialic Acid Content ◽  
Fibrin Monomer

We have described an abnormal fibrinogen in 6 patients with liver disease who had prolonged plasma thrombin times due to impaired fibrin monomer aggregation. To investigate the role of sialic acid in this functional abnormality, fibrinogen was purified from normal and patient plasmas by the glycine precipitation method. Sialic acid content of the fibrinogens was measured by the thriobarbituric acid assay after acid hydrolysis. Normal fibrinogen had 6.1 ± 0.5 residues per molecule of fibrinogen, whereas patient fibrinogen sialic acid content ranged between 7.5 and 10 residues per molecule. The reduced fibrinogen demonstrated normal mobility of Aα, B3 and γ chains on SDS Polyacrylamide gel electrophoresis when stained for protein and, similar to normal fibrinogen, only the Bβ and γ chains stained with PAS. The degree of prolongation of the thrombin times of the purified patient fibrinogens appeared to correlate with the increase in the fibrinogen sialic acid. The effect on fibrin monomer aggregation of decreasing patient fibrinogen sialic acid content was studied. Partially desialated patient fibrinogen was prepared by treating the protein with Vibrio cholerae neuraminidase for varying periods of time. Partial removal of sialic acid from patient fibrinogen resulted in normalization of the thrombin time and improvement in fibrin monomer aggregation. Thrombin times ranged from 31.5 to 49.5 seconds prior to removal of excess sialic acid compared to 20.5 to 25.5 seconds post removal. These findings indicate that the dysfibrinogenemia associated with liver disease is biochemically characterized by increased sialic acid content and removal of this sialic acid results in a functional normalization of the protein.

Influence of the Carbohydrate Moiety in the Dysfibrinogenemia of Liver Disease

1979 ◽  
Author(s):  
J. Martinez ◽  
J.E. Palascak
Keyword(s):  
Liver Disease ◽  
Sialic Acid ◽  
Acid Content ◽  
Similar Distribution ◽  
Thrombin Time ◽  
Sialic Acid Content ◽  
Human Fibrinogen ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Functional Defect

Human fibrinogen is a glycoprotein which contains 6 sialic acid residues per molecule. Enzymatic removal of sialic acid modifies its functional properties as indicated by shortening of the thrombin time due to enhanced asialofibrin monomer polymerization. The abnormal fibrinogen of liver disease contains an Increased amount of sialic acid and is functionally characterized by impaired fibrin monomer polymerization. The prolongation of its thrombin time correlates with its increased sialic acid content. Enzymatic cleavage of the excess sialic acid results in normalization of the thrombin time and the fibrin monomer polymerization. Quantitative labelling of sialic acid with (3H) demonstrates increased labelling of the abnormal fibrinogen compared to normal fibrinogen reflecting the sialic acid content of the abnormal molecule. The radioactivity of the labelled normal and abnormal fibrinogens after reduction and SDS-PAGE was limited to the Bβ and γ chains with 60% of the radioactivity in the Bβ chain and 40% in the γ chain. A similar distribution of radioactivity was found after removal of the excess sialic acid from the respective chains. β-galactose was also increased in the abnormal fibrinogen and paralleled the increase in sialic acid. These studies indicate that sialic acid is distributed normally on the chains of the abnormal fibrinogen of liver disease, but its increased content is responsible for the functional defect of the protein.

Fibrinogen In Liver Cirrhosis. Sialic Acid Content Of Fibrinogen In Moderate And Severe Cirrhosis And Relation To Thrombin Time

1981 ◽  
Author(s):  
G Palareti ◽  
M Poggi ◽  
S Coccheri
Keyword(s):  
Liver Cirrhosis ◽  
Sialic Acid ◽  
Liver Damage ◽  
Acid Content ◽  
Fibrinogen Level ◽  
Carbohydrate Moiety ◽  
Thrombin Time ◽  
Severe Liver ◽  
Sialic Acid Content ◽  
Severe Cirrhosis

An increased content in sialic acid in the carbohydrate moiety of fibrinogen (fibrinogen sialic acid, FSA) as described in a number of different liver patients has been accounted for the polymerization defect often found in conditions of liver damage.In 22 cases of liver cirrhosis divided into “moderate” (n = 11) and “severe” (n = 11) according to standardized criteria, FSA was measured with the method of Warren after purification of fibrinogen with β-alanine and glycine, and expressed in mg per 100 mg of fibrinogen.In the whole group of cirrhotics FSA was 0.79 mg ± 0.17 (controls n = 10, FSA 0.70 mg ± 0.13, p > 0.05). However, FSA was markedly increased in “severe” cases (0.90 mg ± 0.16) both vs controls (p < 0.001) and vs “moderate” cases (0.69 mg ± 0.10, p < 0.005). Thrombin time (TT) although prolonged in cirrhotics (p < 0.001) was not significantly different between the subgroups. FSA correlated inversely with fibrinogen level (p < 0.01) but did not correlate with TT.These results show that the increase in FSA is a feature of severe liver cirrhosis especially in presence of a low fibrinogen level. Although probably involved in the polymerization defect, this increase alone cannot properly explain the prolongation of TT which is known to occur also in absence of serum FDP.

Removal of O-acetylated sialic acids from rat colonic epithelial glycoproteins by cell-free extracts of rat faeces

1983 ◽  
Vol 61 (8) ◽  
pp. 868-874 ◽  
Author(s):  
H. Poon ◽  
P. E. Reid ◽  
C. W. Ramey ◽  
W. L. Dunn ◽  
M. G. Clay
Keyword(s):  
Sialic Acid ◽  
Acid Content ◽  
Minimal Medium ◽  
Wistar Rat ◽  
Sialic Acids ◽  
Side Chain ◽  
Sialic Acid Content ◽  
Vibrio Cholera ◽  
Sterile Cell

Sterile, cell-free, extracts of freshly defaecated Wistar rat faeces in a pH 7.0 "minimal medium" contain neuraminidase(s), capable of removing sialic acids both with and without side-chain substituents from bovine submandibular mucin and rat colonic epithelial glycoproteins, and an esterase which removes O-acetyl substituents from the side chain of sialic acid residues. Studies of the removal of sialic acids from bovine submandibular mucin and rat colonic epithelial glycoproteins indicated that (i) the faecal enzymes removed a greater proportion of the sialic acid of both the de-O-acetylated and native glycoproteins than was removed with Vibrio cholera neuraminidase, (ii) sialic acids were removed more rapidly from de-O-acetylated glycoproteins, and (iii) the resistance to removal of sialic acids was apparently dependent at least in part upon the O-acetyl sialic acid content of the substrate.

129: Sialic Acid Content of Urinary TAMM-Horsfall Protein is Reduced in Interstitial Cystitis Patients

2007 ◽  
Vol 177 (4S) ◽  
pp. 44-45
Author(s):  
C. Lowell Parsons ◽  
Mahadevan Rajasekaran ◽  
Marianne Chenoweth ◽  
Paul Stein
Keyword(s):  
Sialic Acid ◽  
Interstitial Cystitis ◽  
Acid Content ◽  
Sialic Acid Content

scholarly journals Differences in Sialic Acid Content of Human Interferons

1978 ◽  
Vol 41 (1) ◽  
pp. 175-178 ◽  
Author(s):  
J. Morser ◽  
J. P. Kabayo ◽  
D. W. Hutchinson
Keyword(s):  
Sialic Acid ◽  
Acid Content ◽  
Sialic Acid Content

scholarly journals Infection with Listeria monocytogenes impairs sialic acid addition to host cell glycoproteins.

1994 ◽  
Vol 180 (6) ◽  
pp. 2137-2145 ◽  
Author(s):  
M S Villanueva ◽  
C J Beckers ◽  
E G Pamer
Keyword(s):  
Listeria Monocytogenes ◽  
Sialic Acid ◽  
Host Cell ◽  
Mhc Class I ◽  
Acid Content ◽  
Class I ◽  
Sialic Acid Content ◽  
Infected Cells ◽  
The Impact ◽  
Glycosylation Defect

Listeria monocytogenes is a facultative intracellular bacterium that causes severe disease in neonates and immunocompromised adults. Although entry, multiplication, and locomotion of Listeria in the cytosol of infected cells are well described, the impact of such infection on the host cell is unknown. In this report, we investigate the effect of L. monocytogenes infection on MHC class I synthesis, processing, and intracellular trafficking. We show that L. monocytogenes infection interferes with normal processing of N-linked oligosaccharides on the major histocompatibility complex (MHC) class I heavy chain molecule, H-2Kd, resulting in a reduced sialic acid content. The glycosylation defect is more pronounced as the infection progresses and results from interference with the addition of sialic acid rather than its removal by a neuraminidase. The effect is found in two different cell lines and is not limited to MHC class I molecules since CD45, a surface glycoprotein, and LGP120, a lysosomal glycoprotein, are similarly affected by L. monocytogenes infection. The glycosylation defect is specific for infection by L. monocytogenes since neither Trypanosoma cruzi nor Yersinia enterocolitica, two other intracellular pathogens, reproduces the effect. The resultant hyposialylation of H-2Kd does not impair its surface expression in infected cells. Diminished sialic acid content of surface glycoproteins may enhance host-defense by increasing susceptibility to lysis and promoting clearance of Listeria-infected cells.

scholarly journals Erythrocyte Sialic Acid Content during Aging in Humans: Correlation with Markers of Oxidative Stress

2012 ◽  
Vol 32 (3) ◽  
pp. 179-186 ◽  
Author(s):  
Mohammad Murtaza Mehdi ◽  
Prabhakar Singh ◽  
Syed Ibrahim Rizvi
Keyword(s):  
Oxidative Stress ◽  
Sialic Acid ◽  
Erythrocyte Membrane ◽  
Acid Content ◽  
Lipid Hydroperoxide ◽  
Plasma Lipid ◽  
Sialic Acids ◽  
Sialic Acid Content ◽  
Total Antioxidant ◽  
The Relationship

Sialic acids are substituted neuraminic acid derivatives which are typically found at the outermost end of glycan chains on the membrane in all cell types. The role of erythrocyte membrane sialic acids during aging has been established however the relationship between sialic acid and oxidative stress is not fully understood. The present work was undertaken to analyze the relationship between erythrocyte membrane sialic acid with its plasma level, membrane and plasma lipid hydroperoxide levels and plasma total antioxidant capacity. Results show that sialic acid content decreases significantly (P< 0.001) in RBC membrane (r= −0.901) and increases in plasma (r= 0.860) as a function of age in humans. Lipid peroxidation measured in the form of hydroperoxides increases significantly (P< 0.001) in plasma (r= 0.830) and RBC membranes (r= 0.875) with age in humans. The Trolox Equivalent Total Antioxidant Capacity (TETAC) of plasma was found to be significantly decreased (P< 0.001,r= −0.844). We observe significant correlations between decrease of erythrocyte membrane sialic acid and plasma lipid hydroperoxide and TETAC. Based on the observed correlations, we hypothesize that increase in oxidative stress during aging may influence the sialic acid decomposition from membrane thereby altering the membrane configuration affecting many enzymatic and transporter activities. Considering the importance of plasma sialic acid as a diagnostic parameter, it is important to establish age-dependent reference.

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