No abstract available.
Factor X*

PURPOSE: Clotting factor X deficiency is one of the least common coagulation disorders. The authors describe a case of cleft palate in a patient with a congenital clotting factor X deficiency. METHODS: In pediatric patients with a cleft palate, the coagulation problem is more worrisome, because they are more sensitive to blood than adults, and because postoperative bleeding can cause blood ingestion with subsequent vomiting, aspiration, and airway obstruction. To prevent hemorrhagic complications in the described case, fresh frozen plasma (FFP) was administered every 24 hours from the day before surgery to the second postoperative day. RESULTS: Good hemostasis, normal healing, and no complications was shown postoperatively. CONCLUSION: The replacement of fresh frozen plasma was useful in the case of congenital clotting factor deficiency for bleeding prophylaxis in cleft palate operation.
Adult ; Airway Obstruction ; Cleft Palate ; Eating ; Factor X ; Factor X Deficiency ; Hemorrhage ; Hemostasis ; Humans ; Plasma ; Vomiting

OBJECTIVETo deepen the understanding of acquired coagulation factor X (F X) deficiency.

METHODSThe clinical data of 3 patients were analyzed and related literature were reviewed.

RESULTSCase 1, a 57-year-old male, secondary to multiple myeloma and amyloidosis, was presented with spontaneous mucous hemorrhage with the level of FX:C 1.8%, which kept unchanged after chemotherapy with melphalan, glucocorticoid, and thalidomide, and died of primary disease progression. Case 2, a 41-year-old male with psoriasis, was presented with cerebral and retinal hemorrhage with the level of FX:C 26.8%. The signs of hemorrhage were alleviated after the supplement of folic acid, vitamin B12, and vitamin K, and transfusion with red blood cells, platelets, and fresh frozen plasma. Case 3, a 63-year-old female, associated with high level of lupus anticoagulant, was presented with repeated ecchymosis and haemarthrosis with the level of FX:C 6.1%, which was refractory to prothrombin complex concentrate, methyprednisolone, azathioprine, and rituximab.

CONCLUSIONAcquired FX deficiency is a rare disorder with variable symptoms. The diagnosis relies on history of disease and laboratory test. Currently, there is no standardized treatment. The prognosis of acquired FX deficiency is mainly related to the underlying disease.

Adult ; Factor X Deficiency ; Female ; Humans ; Male ; Middle Aged

We report a case of nephrotic syndrome and factor X deficiency secondary to primary amyloidosis. A 58-year-old man was referred to our hospital for evaluation of nephrotic syndrome and bleeding tendency. He was confirmed to have primary amyloidosis by renal biopsy, immunofixation electrophoresis and bone marrow findings. His bleeding tendency was due to prothrombin time prolongation caused by isolated factor X deficiency. If any patient with nephrotic syndrome has bleeding tendency due to coagulation abnormalities, that patient should be considered to have factor X deficiency secondary to primary amyloidosis.
Amyloidosis ; Biopsy ; Bone Marrow ; Electrophoresis ; Factor X ; Factor X Deficiency ; Hemorrhage ; Humans ; Middle Aged ; Nephrotic Syndrome ; Prothrombin Time

OBJECTIVETo identify potential mutation underlying coagulation factor X (FX) deficiency in a consanguineous Chinese pedigree.

METHODSProthrombin time (PT), activated partial thromboplastin time (APTT), fibrinogen, FX activity (FX:C) and other coagulant parameters were determined with a one-stage clotting assay. The FX antigen (FX:Ag) was determined with an ELISA assay. All coding exons and exon-intron boundaries of the F10 gene were amplified with PCR and subjected to direct sequencing. Suspected mutation was confirmed by reverse sequencing and analyzed with CLC Genomics Workbench 7.5 software.

RESULTSThe PT and APTT in the proband were prolonged to 67.2 s and 102.9 s, respectively. Further study showed that her FX:C and FX:Ag were reduced by 1% and 8%, respectively. The PT of her father, mother, and little brother were slightly prolonged to 14.5 s, 14.4 s and 14.4 s, respectively. The FX:C and FX:Ag in her father, mother and little brother were all slightly reduced. Genetic analysis of the proband has revealed a homozygous G>A change at nucleotide 27881 in exon 8 of the F10 gene, which predicted a p.Val298Met substitution. The proband's father, mother, and little brother were all heterozygous for the p.Val298Met mutation. The proband has inherited the homozygous mutation from her parents by consanguineous marriage. Other family members were all normal. Bioinformatics analysis has indicated that this mutation may result in changes in the secondary structure of the FX protein.

CONCLUSIONA homozygous mutation g.27881G>A(p.Val298Met) of the F10 gene has been identified, which probably accounts for the low FX concentrations in this pedigree.

Adult ; Amino Acid Sequence ; Consanguinity ; Factor X ; genetics ; Factor X Deficiency ; genetics ; Female ; Homozygote ; Humans ; Male ; Middle Aged ; Molecular Sequence Data ; Mutation, Missense ; Pedigree ; Prothrombin Time

OBJECTIVETo explore the molecular mechanisms involved in a pedigree with inherited coagulation factor X (FX) deficiency.

METHODSThe activated partial thromboplastin time (APTT), prothrombin time (PT), FX activity (FX:C) and FX antigen (FX:Ag) test were adopted for phenotype diagnosis. All the 8 exons, intron/exon boundaries and the 5'untranslated regions (UTR) of the FX gene were amplified by polymerase chain reaction (PCR) from the genomic DNA extracted from the peripheral blood of the propositus. The PCR products were screened by direct sequencing. The mutation was confirmed by allele specific PCR (ASPCR).

RESULTSThe phenotype of the propositus was identified as FX deficiency (type II). Two novel FX gene mutations were detected in the propositus: one was a donor site splice mutation in intron 1 (IVS1 + 1G-->A), another was a missense mutation 1185G-->A in exon 8 (Arg347His).

CONCLUSIONThe FX deficiency of the propositus is caused by double heterozygous mutations IVS1 + 1G-->A and Arg347His.

Antigens ; genetics ; Base Sequence ; DNA Mutational Analysis ; Factor X ; genetics ; Factor X Deficiency ; genetics ; Female ; Heterozygote ; Humans ; Male ; Mutation ; Pedigree ; Young Adult

OBJECTIVE: The objective of this study was to determine the correlations between changes in thrombogenesis or thrombolysis related factors, and the acute increase of a spontaneous intracerebral hemorrhage (sICH). MATERIALS AND METHODS: From January 2009 to October 2011, 225 patients with sICH were admitted to our hospital within 24 hours of onset. Among them, 111 patients with hypertensive sICH were enrolled in this study. Thrombogenic or thrombolytic factors were checked at admission. The authors checked computed tomography (CT) scans at admission and followed up the next day (between 12-24 hours) or at any time when neurologic signs were aggravated. Cases in which the hematoma was enlarged more than 33% were defined as Group A and the others were defined as Group B. RESULTS: Group A included 30 patients (27%) and group B included 81 patients (73%). Factors including activated partial thromboplastin time, prothrombin time, fibrinogen, and D-dimer showed a greater increase in group A than in group B. Factors including antithrombin III, factor V, and factor X showed a greater increase in group A than in group B. CONCLUSION: Based on the results of this study, it seems that the risk of increase in hematoma size can be predicted by serum thrombogenic or thrombolytic factors at admission.
Antithrombin III ; Cerebral Hemorrhage* ; Factor V ; Factor X ; Fibrinogen ; Hematoma ; Humans ; Neurologic Manifestations ; Partial Thromboplastin Time ; Prothrombin Time

OBJECTIVETo identify potential mutations and explore the molecular mechanism underlying combined inherited coagulation factors VII(FVII) and X(FX) deficiency for a family featuring consanguineous marriage between maternal cousins.

METHODSProthrombin time (PT), activated partial thromboplastin time (APTT), fibrinogen, FVII activity (FVII:C), FX activity (FX:C), FVII antigen (FVII:Ag), FX antigen (FX:Ag) and other coagulant parameters of the proband and 5 family members were measured. Potential mutations in exons, exon-intron boundaries and 5', 3' untranslated sequences of F7 and F10 genes were screened by polymerase chain reaction and direct sequencing. Suspected mutations were confirmed by sequencing the opposite strand.

RESULTSPT and APTT of the proband were obviously prolonged to become 76.4 s and 60.2 s, respectively. FVII:C, FVII:Ag,FX:C and FX:Ag of the proband were obviously reduced to become 4%, 6%, 6% and 33%, respectively. Both PT and APTT of her grandmother, father, mother and daughter were slightly prolonged, which have measured 16.4 s, 15.8 s,16.9 s, 16.5 s, and 44.0 s, 42.1 s, 41.1 s, 43.5 s, respectively. And their FVII:C (34%, 39%, 31%, 40%, respectively), FX:C (50%, 58%, 47%, 42%, respectively) and FX:Ag (51%, 54%, 58%, 47%, respectively) were slightly reduced, while FVII:Ag was in the normal range. The coagulant parameters of her younger brother were within normal range. Two homozygous mutations, g.11267C to T in exon 8 of F7 gene, which resulted in an Arg277Cys substitution, and g.28139G to T in exon 8 of F10 gene which led to a Val384Phe substitution, were identified in the proband. The proband's grandmother, parents and daughter were heterozygous for both Arg277Cys and Val384Phe mutationss. Wild-type alleles of both F7 and F10 genes were also found in the younger brother.

CONCLUSIONA homozygous Arg277Cys mutation and a Val384Phe mutation have been respectively identified in the F7 and F10 genes, which can explain the low levels of FVII and FX in this family. The former has been inherited from the consanguineous parents.

Adult ; Aged ; Consanguinity ; Factor VII Deficiency ; genetics ; Factor X Deficiency ; genetics ; Female ; Genotype ; Humans ; Male ; Middle Aged ; Mutation ; Pedigree ; Phenotype

PURPOSE: This preliminary rabbit study was conducted to evaluate the effect of recombinant human transforming growth factor-beta2 (rhTGF-beta2)/poly lactic-co-glycolic acid (PLGA) coating on osseointegration of the titanium (Ti) implant. MATERIALS AND METHODS: Eight Ti implants were anodized with 300 voltages for three minutes. Four of those were coated with rhTGF-beta2/PLGA by an electrospray method as the experimental group. The implants were placed into tibiae of four New Zealand rabbits, two implants per a tibia, one implant per each group. After 3 and 6 weeks, every two rabbits were sacrificed and micro-computed tomography (microCT) was taken for histomorphometric analysis. RESULTS: In scanning electron microscope (SEM) image, the surface of rhTGF-beta2/PLGA coated Ti implant showed well distributed particles. Although statistically insignificant, microCT analysis showed that experimental group has higher bone volume / total volume (BV/TV) and trabecular thickness (Tb.Th) values relatively. Cross sectional view also showed more newly formed bone in the experimental group. CONCLUSION: In the limitation of this study, rhTGF-beta2/PLGA particles coating on the Ti implant show the possibility of more favorable quantity of newly formed bone after implant installation.
Humans ; Osseointegration* ; Rabbits ; Tibia ; Titanium* ; Transforming Growth Factor beta2 ; X-Ray Microtomography*

Adult ; Amyloidosis ; complications ; Factor X Deficiency ; complications ; Humans ; Liver Diseases ; complications ; Male