• Journal of Genetic Medicine
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• v.13 no.2
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• pp.89-94
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• 2016

Purpose: Molecular genetic analysis is the main approach used for prenatal diagnosis of hemophilia A and B. However, in certain cases, such analysis is uninformative. In such situations, direct measurement of fetal coagulation factor levels is still the best option, and it may be the only option in some cases. This study was conducted to determine the normal ranges of mid-trimester cord blood factor VIII (FVIII) and IX (FIX) in a Korean population. Materials and Methods: Twenty-six FVIII samples and 29 FIX samples were assayed in fetal cord blood acquired by ultrasound-guided cordocentesis. Sampling was conducted during gestational ages of 19-24 weeks. Results: The mean and standard deviations for FVIII and FIX activity were $45.5{\pm}30.5%$ and $19.9{\pm}12.2%$, respectively. Ranges for FVIII and FIX were 1.5-125.0% and 6.0-52.0%, respectively. Conclusion: Our study revealed the normal ranges and lowest level of factor VIII and factor IX in non-affected normal fetus by fetal cord blood sampling during the mid-trimester in a Korea population. The factor assay of the fetal cord blood is invasive but feasible and provides important basic data related to hemophilia.

• Journal of Korean Biological Nursing Science
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• v.26 no.1
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• pp.1-15
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• 2024

Purpose: This study aimed to evaluate the effectiveness of exercise in patients with hemophilia. Methods: We carried out a systematic review and meta-analysis in accordance with the Preferred Reporting Items for Systematic Review and Meta-analysis (PRISMA) guidelines. A literature search was conducted of published randomized controlled trials for exercise interventions from January 1, 2014 to March 15, 2023. To estimate the size of the effects of exercise, a meta-analysis was performed using the R package "meta." Results: Five databases were searched to obtain articles published in Korean or English. Of 1,150 articles reviewed, 13 were included in the systematic review and 9 in the meta-analysis. The risk of bias was assessed using RoB 2.0. The overall effect sizes of exercise interventions, calculated as the standardized mean difference, were -0.11 (95% confidence interval [CI] = -1.41 to -1.20) for pain, -2.13 (95% CI = -3.33 to -0.93) for joint health, 9.96 (95% CI = 7.51 to 12.28) for physical activity, and 0.59 (95% CI = -0.39 to -1.56) for quality of life. Conclusion: These findings suggest that exercise is useful for improving the joint health and physical activity of patients with hemophilia. Thus, it is necessary to develop and apply exercise interventions for patients with hemophilia to reduce their pain and improve their quality of life.

• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.338.2-338
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• 1995

No Abstract, See Full Text

• Bulletin of the Korean Chemical Society
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• v.30 no.1
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• pp.77-82
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• 2009

Thrombin activatable fibrinolysis inhibitor (TAFI) also known as plasma procarboxypeptidase B or U is a 60 kD glycoprotein, which is the major modulator of fibrinolysis in plasma. TAFI is a proenzyme, which is activated by proteolytic cleavage to an active carboxypeptidase B-like enzyme (TAFIa, 35.8 kD) by thrombin/thrombomodulin and plasmin. Modulation of fibrinolysis occurs when TAFIa enzymatically removes C-terminal lysine residues of partially degraded fibrin, thereby inhibiting the stimulation of tissue plasminogen activator (t-PA) modulated plasminogen activation. TAFIa undergoes a rapid conformational change at $37{^{\circ}C}$ to an inactive isoform called TAFIai. Potato tuber carboxypetidase inhibitor (PTCI) was shown to specifically bind to TAFIa as well as TAFIai. In this study, a novel immunoassay TAFIa/ai ELISA was used for quantitation of the two TAFI activation isoforms TAFIa and TAFIai. The ELISA utilizes PTCI as the capture agent and a double antibody sandwich technique for the detection. Low levels of TAFIa/ai antigen levels were detected in normal plasma and elevated levels were found in hemophilia A plasmas. TAFIa/ai antigen represents a novel marker to monitor fibrinolysis and TAFIa/ai ELISA may be a valuable assay for studying the role of TAFI in normal hemostasis and in pathological conditions.

• Archives of Plastic Surgery
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• v.34 no.4
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• pp.516-519
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• 2007

Purpose: Hemophilia is one of the most common bleeding disorder, and circulating levels of factor VIII or IX are closely related to the severity and frequency of the bleeding. The severity of hemophilia is classified to be severe, moderate, and mild when the factor level is less than 1%, between 1% and 5%, and between 5% and 25%, respectively. Hemophilic pseudotumor is a rare complication occurring in 1 - 2% of patients with factor VIII or IX deficiency. If the treatment is delayed, it would cause disabling and life threatening results. Methods: We experienced hemophilic pseudotumor developed at the fracture site of the proximal phalanx of the hand in a hemophilic B patient. Hemophilic pseudotumor was successfully treated with perioperative factor replacement and surgical intervention included excision and autologous bone graft. Results: Hemophilic pseudotumor was healed with complete regression, and no specific complication was developed. Conclusion: When we accounter hematoma like lesion after surgery unpredictably, we must consider hemophilic pseudotumor and make a accurate diagnosis with preoperative hematologic screening and various imaging study. Subsequently, adequate perioperative supplement of concentrate and surgical intervention brings to the satisfactory result without recurrence.

• Biomedical Science Letters
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• v.2 no.2
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• pp.231-240
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• 1996

Human blood clotting (coagulation) factor 9 cDNA which codes for 461 amino acid has been cloned by screening human fetal liver cDNA library using PCR. This 1.4 kb cDNA spanning from the ATG initiation codon to the TAA termination codon was cloned into bacterial .expression vector pGEX-2T, generating pGEX-F9 plasmid. The plasmid pGEX-F9 expresses about 73 kDa GST (Glutathione S-transferase)-Factor 9 fusion protein when introduced into E. coli. Western blot analysis using polyclonal antibody raised against human factor 9 confirmed this fusion protein contains factor 9 protein. The level of GST-factor 9 expression was about 20% of total protein and the purification of fusion protein was efficiently achieved by using GST agarose bead based on one step purification protocol.

• Molecules and Cells
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• v.24 no.1
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• pp.125-131
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• 2007

von Willebrand factor (vWF) is a multimeric glycoprotein which functions within the coagulation system. It colocalizes with factor VIII (FVIII) by non-covalent interaction and alters its intracellular trafficking. vWF is also instrumental in maintaining the stability of secreted FVIII. The principal objective of this study was to generate a lentivirus-based vWF expression vector for gene therapy of hemophilia A. We inserted a vWF of 8.8 Kb into a lentiviral vector thereby producing VSV-G-pseudotyped vEx52. However, its titer was quite low, presumably because the length of vWF gene exceeds the size limit of the lentiviral vector. In order to overcome the low-titer, we concentrated the vEx52 and thus increased the efficiency of transduction approximately 6-fold with $1/100^{th}$ of the volume. However, as concentration requires an additional laborious step, we attempted to enhance the transduction efficiency by deleting exons 24-46 and 29-46 in pRex52 to construct pRex23 and pRex28, and in pvEx52, yielding pvEx23 and pvEx28, respectively. The transfected pRex52 had a profound effect on the activity of secreted FVIII, and this activity declined as domains of vWF were deleted. However, when the domain-deleted vWF-lentiviruses were transduced into K562 cells, the vEx28 increased the activity of the secreted FVIII compared to what was observed with vEx52. This result is probably due to higher efficiencies of transduction and expression while retaining the essential domains required for proper interaction with FVIII.