• Journal of Microbiology and Biotechnology
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• v.18 no.3
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• pp.503-511
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• 2008

An edible marine red alga, Grateloupia filicina, collected from Jeju Island of Korea was hydrolyzed by cheap food-grade carbohydrases (Viscozyme, Celuclast, AMC, Termamyl, and Ultraflo) to investigate its anticoagulant activity. Among the tested enzymatic extracts of G. filicina, a Termamyl extract showed the highest anticoagulant activity. Anion-exchange chromatography on DEAE-cellulose and gel-permeation chromatography on Sepharose-4B were used to purify the active polysaccharide from the crude polysaccharide fraction of G. filicina. The purified sulfated polysaccharide (0.42 sulfate/total sugar) showed ${\sim}1,357kDa$ molecular mass and was comprised mainly of galactose(98%) and 1-2% of glucose. The sample showed potential anticoagulant activity on activated partial thromboplastin time (APTT) thrombin time (TT) assays. The purified G. filicina anticoagulant (GFA) inhibited the coagulation factor X (92%), factor II (82%), and factor VII (68%) of the coagulation cascade, and the molecular interaction (protein-polysaccharide) was highly enhanced in the presence of ATIII (antithrombin III). The dissociation constant of polysaccharide towards serine proteins decreased in the order of FXa (58.9 nM) >FIIa (74.6 nM) >FVII (109.3 nM). The low/less cytotoxicity of the polysaccharide benefits its use in the pharmaceutical industry; however, further studies that would help us to elucidate the mechanism of its activity are needed.

• Korean Journal of Food Science and Technology
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• v.29 no.1
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• pp.161-166
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• 1997

Tissue thromboplastin (tissue factor), a membrane bound glycoprotein is an important initiating factor in blood coagulation cascade, which leads to the formation of thrombin by activating both factor X and IX. Activation of blood coagulation by TF is essential for blood injury, and stimulates the blood coagulation in myocardial infarction, cancer and blood coagulatory diseases. High density lipoprotein, apolipoprotein A-II were known to be biological TF inhibitors. Recently, studies on search for TF inhibitors from natural products have been active in Korea. Among the edible mushrooms screened for inhibitory activities on the TF, Lentinus edodes showed the most strong activity, followd by Agaricus bisporus and Ganoderma lucidium. And the fractionation of the above mushrooms with the chloroform ($CHCl_3$) and ethylacetate (EtOAc) was done and evaluated for the inhibitory activities on TF. In Ganoderma lucidium, $CHCl_3$ fraction and $H_2O$ layer were not active, but EtOAc fraction exhibited a strong inhibitory activity on TF and the $IC_{50}$ value was $1.07{\times}10^{-4}\;g$. In the case of Agaricus bisporus, there were no inhibitory activities on the TF in all of the fractions. $CHCl_3$ fraction and $H_2O$ layer of Lentinus edodes did not show inhibition on the TF but EtOAc fraction showed strong inhibition on the TF, and the $IC_{50}$ value was $7.70{\times}10^{-4}\;g$.

• Journal of the Korean Society of Food Science and Nutrition
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• v.31 no.5
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• pp.917-923
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• 2002

Inhibitory mechanism of the anticoagulant polysaccharide purified from Codium fragile was investigated. The anticoagulant compounds (Cf-30-IV-4-ii, CF-30-IV) prolonged the clotting time at both activated partial thrombo-plastin time (aPTT) and thrombin time (TT). The Inhibition factor assay of instrinsic coagulation pathway in the blood showed that the anticoagulant polysaccharide (CF-30-IV-4-ii) inhibited other factors such as Ⅷ, Ⅸ, Ⅵ and Ⅷ of the coagulation cascade, which did not affect the lupus anticoagulant AB activity. In the thrombin inhibition pattern the CF-30-IV-4-ii did not directly influence the fibrine formation mediated by thrombin but af-fected the anticoagulant activity through the activation of antithrombin III. Base on these result, the anticoaglant polysaccharide (CF-30-IV-4-ii) was considered to inhibit serine pretense involved in the blood coagulation cascade through the enhancing antithrombin III activity. The residual effects of anticoagulant activity and antithrombosis were tested with ICR mice. The anticoagulant polysaccharide (CF-30-W) kept its anticoagulant activitv for 6 hrs with 100% survival at a dose of 150 mg/kg in the antithromboisis test. The anticoagulant effect of CF-30-RF in ex vivo was proportional to the concentration of intravenously injected dose up to 100 mg/kg.

• Biomedical Science Letters
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• v.18 no.3
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• pp.237-243
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• 2012

This study was undertaken to know the effect of fat diet (for eight weeks) on changes of inflammatory markers [tumor necrosis factor (TNF-${\alpha}$) and prostaglandin $E_2$ ($PGE_2$)] and blood coagulation system [platelet aggregation function (PAF), prothrombin time (PT), activated partial thromboplastin time (aPTT)] in rats. Serum TNF-${\alpha}$, $PGE_2$, biochemical markers, PAF, PT, aPTT, and body weight were measured and compared between the control (normal diet-rats) and the fat group (fat diet-rats). The weights in the fat group were higher than those of the control group. TNF-${\alpha}$, $PGE_2$, glucose, aspartate aminotransferase (AST), alanine aminotransferase (ALT), and creatinine levels were greater in the fat group compared with the control group. The degree of platelet aggregation was lower, whereas PT and aPTT levels were longer in the fat group than in the control group. These findings have shown that fat diet may cause inflammatory response, diabetes, liver and renal dysfunction, and disturbances of fibrinolysis and coagulation system.

• Korean Journal of Clinical Laboratory Science
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• v.45 no.3
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• pp.87-90
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• 2013

The activated partial thromboplastin time (APTT) is used primarily to evaluate coagulation abnormalities in the intrinsic pathway. The proper specimen is very important factor for precise results of blood coagulation analysis. The objective of this study was to get to the conclusion of whether to analyze again and to collect blood sample over again when APTT result shows below the reference value. We evaluated 126 samples showing a value below 20.0 sec at ATPT result, which consist of 48 males and 78 females candidates during night duty from March 2012 to December 2012. Average comparisons of APTT result between first and retested analysis among study subjects were significantly different in male samples. APTT results comparison of recollected subjects among clotted samples were also significantly different with both sexes (p<0.000). We suggest that we should carefully check the samples to get accurate results and collect samples again in case of only obtaining improper samples; even though the APTT result show below reference value.

• Asian Pacific Journal of Cancer Prevention
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• v.15 no.11
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• pp.4545-4548
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• 2014

Objective: To investigate the changes of serum vascular endothelial growth factor (VEGF), soluble interleukin-2 receptor (SIL-2R) and hepatocyte growth factor (HGF) contents in patients with primary hepatocellular carcinoma (HCC) before and after percutaneous microwave coagulation therapy (PMCT) and determine their clinical significance. Materials and Methods: Fasting venous blood (3 mL) from 81 patients with primary HCC diagnosed by pathology was collected in the mornings 1 day before PMCT, and 1 day, 7 days and 1 month after PMCT, and then the serum was separated and stored in $-70^{\circ}C$. The contents of VEGF, SIL-2R and HGF were detected by enzyme linked immunosorbent assay (ELISA). Results: The serum VEGF, SIL-2R and HGF contents in 81 patients with primary HCC had obviously dynamic changes before and after PMCT. By comparison to 1 day after PMCT with pre-operation, there was no statistical significance regarding VEGF and SIL-2R contents (P>0.05), but HGF content showed significant difference (P<0.01). Compared with pre-operation, VEGF, SIL-2R and HGF contents 7 days and 1 month after PMCT all manifested significant differences (P<0.01). By comparison to 7 days with 1 month after PMCT, there was no statistical significance regarding the VEGF content (P>0.05), whereas SIL-2R and HGF contents showed significant change (P<0.01). Conclusions: The contents of serum VEGF, SIL-2R and HGF have obviously dynamic changes in primary HCC before and after PMCT, and their joint detection is expected to be an effective hematologic evaluation index of PMCT for primary HCC.

• Journal of Veterinary Science
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• v.21 no.3
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• pp.45.1-45.15
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• 2020

Background: Feline mammary carcinoma is the third most common cancer that affects female cats. Objectives: The purpose of this study was to screen differential serum proteins in feline and clarify the relationship between them and the occurrence of feline mammary carcinoma. Methods: Chinese pastoral cats were used as experimental animals. Six serum samples from cats with mammary carcinoma (group T) and six serum samples from healthy cats (group C) were selected. Differential protein analysis was performed using a Label-free technique, while parallel reaction monitoring (PRM) was performed to verify the screened differential proteins. Results: A total of 82 differential proteins were detected between group T and group C, of which 55 proteins were down regulated and 27 proteins were up regulated. Apolipoprotein A-I, Apolipoprotein A-II (ApoA-II), Apolipoprotein B (ApoB), Apolipoprotein C-III (ApoC-III), coagulation factor V, coagulation factor X, C1q, albumen (ALB) were all associated with the occurrence of feline mammary carcinoma. Differential proteins were involved in a total of 40 signaling pathways, among which the metabolic pathways associated with feline mammary carcinoma were the complement and coagulation cascade and cholesterol metabolism. According to the Label-free results, ApoB, ApoC-III, ApoA-II, FN1, an uncharacterized protein, and ALB were selected for PRM target verification. The results were consistent with the trend of the label-free. Conclusions: This experimen is the first to confirm ApoA-II and ApoB maybe new feline mammary carcinoma biomarkers and to analyze their mechanisms in the development of such carcinoma in feline.

• Journal of Periodontal and Implant Science
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• v.13 no.1
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• pp.60-60
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• 1983

• Journal of Life Science
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• v.13 no.4
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• pp.463-472
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• 2003

Interactions between factor Va (HFVa) and membrane phosphatidylserine (PS) regulate the activity of the prothrombinase complex. I have previously shown that two solvent exposed hydrophobic residues located in the C2-domain, Trp2063 and Trp2064, are required for binding to immobilized PS and for expression of procoagulant activity on membranes containing 5% PS. In order to fully define the functional importance of these two residues I have expressed and isolated recombinant factor Va (rHFVa) W2063A/W2064A double mutant. In contrast to the native protein the two glycoforms resulting from alternative glycosylation of Asn2181 eluted as a single peak with rHFVa1 W2063A/W2064A eluting on the leading edge and rHFVa2 W2063A/W2064A eluting on the trailing edge. The double mutant rHFVa2 W2063A/W2064A expressed little or no procoagulant activity on membranes containing 1-10% mol % PS. In contrast, the procoagulant activity of this mutant was slightly greater than the native protein on membranes containing>18 mol % PS. The binding of rHFVa2 W2063A/W2064A to immobilized phospholipid vesicles was markedly reduced compared to the native protein in a surface plasmon resonance binding assay. I conclude that Trp2063 and Trp2064 are required for high affinity binding of factor Va to PS membranes and that this interaction is necessary for assembly of the prothrombinase complex on membranes containing physiological concentrations of PS.

• Proceedings of the PSK Conference
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• 2003.04a
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• pp.238.1-238.1
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• 2003

Tissue Factor (TF), a principal initiator of the veterbrate coagulation cascade is known to to induced in endothelial cells, monocytes and macrophages by inflammetry stimuli and in many pathological conditions. Through our synthetic efforts to develop new TF inhibitors, seventeen N-C-18 alkenyl group (9-octadecenyl or 9,12-octadecadienyl) substituted aminoalcohols (2-aminoethanol, 1-amino-2-propanol and 3-amino-1-propanol) were prepared and their in vitro TF inhibitory activities were examined. (omitted)