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Eco Efficiency (Factor X) for Electrical and Electronic Products and a Case Study on Home Appliances in a Household

Eco Efficiency (Factor X) for Electrical and Electronic Products and a Case Study on Home Appliances in a Household

Many institutes and companies are currently researching into eco-efficiency and Factor X as evaluation methods for environmentally conscious design. However, no standard method has been established. Moreover while the eco-efficiency of each home appliance is being improved, the increasing number and size of such home appliances may increase the overall environmental impact. This paper begins with describing a practical eco-efficiency (Factor X) indicator developed to evaluate environmentally conscious products or services. This indicator gives a rationalized relationship between their functional performance and environmental impacts. Next, the paper presents a brief case study of Factor X done in Japan that compared home appliances from 2003 with those from 1990 using such indicators. The number of home appliances used in a household increased 1.2 times from 65 to 79. However, GHG (greenhouse gas) emissions per year was 0.64 times the former amount, dropping from 8456 to 5383 kg–CO 2 eq/year, and the new resources and discarded resources per year became 0.99 times the previous amount,
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Increased local expression of coagulation factor X contributes to the fibrotic response in human and murine lung injury

Increased local expression of coagulation factor X contributes to the fibrotic response in human and murine lung injury

Increased local expression of coagulation factor X contributes to the fibrotic response in human and murine lung injury Chris J.. Uncontrolled activation of the coagulation cascade contr[r]

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Blood coagulation factor X exerts differential effects on adenovirus entry into human lymphocytes

Blood coagulation factor X exerts differential effects on adenovirus entry into human lymphocytes

Abstract: It has been proposed that blood coagulation factors, principally factor X (FX), enhance the uptake of human adenovirus type 5 (Ad5) into cultured epithelial cells by bridging the viral hexon capsid protein and cell-surface heparan sulphate proteoglycans (HSPGs). We studied the effects of FX on Ad transduction of lymphoid cell lines (NK92MI, a natural killer cell line; Daudi, a B-cell line and Jurkat, a T-cell line) as well as primary peripheral blood lymphocytes (PBL) and HeLa epithelial cells using either replication-deficient Ad5, or a derivative in which the Ad5 fiber was replaced with that of another Ad type, Ad35, termed Ad5F35. PBL and NK92MI were resistant to Ad5 transduction. Transduction of Jurkat and Daudi cells by Ad5 was reduced by FX but without discernible effects on cell-surface Ad5 binding. FX reduced virus binding and transduction of all lymphoid cell lines by Ad5F35, as well as transduction of the T- and Natural Killer (NK)-cell populations of PBL. Flow cytometry analysis showed that all lymphoid cell lines were negative for HSPG components, in contrast to HeLa cells. FX reduced transduction of an HSPG-negative mutant Chinese hamster ovary cell line (CHOpgsA745) by Ad5 and Ad5F35, with Ad5F35 binding also being reduced by FX. These results point to fiber-dependent differences (Ad5 versus Ad35 fiber) in Ad binding to and transduction of human lymphoid and epithelial cells in the presence of FX.
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Effect of Neutralizing Sera on Factor X-Mediated Adenovirus Serotype 5 Gene Transfer

Effect of Neutralizing Sera on Factor X-Mediated Adenovirus Serotype 5 Gene Transfer

The deployment of adenovirus serotype 5 (Ad5)-based vectors is hampered by preexisting immunity. When such vectors are delivered intravenously, hepatocyte transduction is mediated by the hexon-coagulation factor X (FX) interaction. Here, we demonstrate that human sera efficiently block FX-mediated cellular binding and transduction of Ad5-based vectors in vitro. Neutralizing activity correlated well with the ability to inhibit Ad5-mediated liver transduction, suggesting that prescreening patient sera in this manner accurately predicts the efficacy of Ad5-based gene therapies. Neutralization in vitro can be partially bypassed by pseudotyping with Ad45 fiber protein, indicating that a proportion of neutralizing antibodies are directed against the Ad5 fiber.
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Humoral factor that specifically regulates factor X levels in rabbits (coagulopoietin X)

Humoral factor that specifically regulates factor X levels in rabbits (coagulopoietin X)

A heat-stable humoral substance (coagulopoietin-X) is present in rabbits partially depleted of Factor X, which is capable of raising Factor X levels when injected into recipient rabbits. Rabbits were partially depleted of Factor X by slow infusion of a globulin fraction of goat anti-rabbit Factor X antibody. This resulted in the reduction of Factor X to 40--50% of normal at 1 h and 60--70% of normal at 6 h. No effect was noted on levels of Factors II, V, or VII. Plasma from these animals, when injected into 10 recipients, specifically raised Factor X levels when measured by four different assay: one-stage assay with bovine VII- and X- deficient plasma and Russell's viper venom; one-stage assay with human X-deficient plasma and thromboplastin; chromogenic substrate assay with Russell's viper venom; and an immunologic assay (Laurell technique). No rise was noted in two control experiments in which normal plasma was injected into recipient rabbits from 2 rabbits injected with a globulin fraction of normal goat serum, nor in 12 rabbits injected with plasma from normal rabbits, nor in 5 rabbits injected with boiled plasma from normal rabbits. The rise in biologic activity of 120--150% of base line was significantly greater than the rise in immunologic activity of 114--117% of base line (P less than 0.05) on 3 different days, suggesting the production of […]
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Combined Functional and Immunochemical Analysis of Normal and Abnormal Human Factor X

Combined Functional and Immunochemical Analysis of Normal and Abnormal Human Factor X

difference in measurement appears to result from the presence of a subpopulation of Factor X molecules devoid of coagulant activity. The radioimmunoassay was used to qualitatively and quantitatively compare purified Factor X to plasmic Factor X obtained from normal, warfarintreated, acquired Factor X-deficient, and congenitaldeficient patients. In all but one case, the Factor X present in these plasmas was immunochemically identical to the purified Factor X and permitted precise quantitation of these abnormal Factor X molecules. Factor X procoagulant activity was analyzed relative to Factor X antigen and the specific activities were used to characterize normal and abnormal Factor X molecules. Reduced Factor X activity in plasmas from warfarin-treated and acquired Factor X-deficient patients […]
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A factor X activating cysteine protease from malignant tissue

A factor X activating cysteine protease from malignant tissue

A proteolytic procoagulant has been identified in extracts of human and animal tumors and in cultured malignant cells. It directly activated Factor X but its similarity to other Factor S- activating serine proteases was not clear. This study describes work done to determine whether this enzyme, cancer procoagulant, is a serine or cysteine protease. Purified cancer procoagulant from rabbit V2 carcinoma was bound to a p-chloromercurialbenzoate-agarose affinity column and was eluted with dithiothreitol. The initiation of recalcified, citrated plasma coagulation activity by cancer procoagulant was inhibited by 5 mM
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Platelet receptor mediated factor X activation by factor IXa  High affinity factor IXa receptors induced by factor VIII are deficient on platelets in Scott syndrome

Platelet receptor mediated factor X activation by factor IXa High affinity factor IXa receptors induced by factor VIII are deficient on platelets in Scott syndrome

We have studied factor IXa binding and factor X activation with normal platelets and with platelets obtained from a patient with a bleeding disorder and an isolated deficiency of platelet procoagulant activity termed Scott syndrome. In the absence of factor VIIIa and factor X, normal, thrombin-treated platelets exposed 560 +/- 35 sites for factor IXa with a Kd of 2.75 +/- 0.27 mM, compared with 461 +/- 60 sites per patient platelet with Kd of 3.2 +/- 0.33 nM. The addition of factor VIIIa and factor X resulted in a decrease in the Kd for normal platelets to 0.68 nM but had no effect on the Kd for patient platelets. The concentrations of factor IXa required for half-maximal rates of factor X activation for normal (0.52 nM) and patient platelets (2.5 nM) were similar to those determined from equilibrium binding studies. Kinetic parameters for factor X activation by factor IXa showed that the Km and Kcat were identical for normal and patient platelets in the absence of factor VIIIa. In the presence of factor VIIIa, and kcat for patient platelets (163 min-1) was only 33% of that for normal platelets (491 min-1): This result can be explained by the difference in affinity for factor IXa between normal and patient platelets in the presence of factor VIIIa, suggesting impaired factor VIIIa […]
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Role of human factor VIII in factor X activation

Role of human factor VIII in factor X activation

The cofactor function of human Factor VIII in Factor X activation was investigated by an initial-rate assay of 3H-Factor X activation in the presence of human factor IXa, Ca2+, and either phospholipid or fresh washed human platelets. Purified Factor VIII that has not been activated by thrombin or Factor Xa supports Factor X activation after a lag of several

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 RIVAROXABAN: AN ORAL DIRECT INHIBITOR OF FACTOR X-A

 RIVAROXABAN: AN ORAL DIRECT INHIBITOR OF FACTOR X-A

The activation of factor X to factor Xa (FXa) plays a central role in blood coagulation—it converts prothrombin (factor II) to thrombin (factor IIa), which leads to the conversion of fibrinogen to fibrin and the formation of a clot. In vivo, this process is initiated by tissue factor (TF), which, in conjunction with factor VIIa (FVIIa), activates FXa directly or via propagation of the tenase complex (factor VIIIa + IXa) on an activated platelet membrane. The prothrombinase complex is then formed on the platelet surface by FXa and platelet- derived factor Va (Figure. 1). Incorporation of FXa into the prothrombinase complex increases the rate of thrombin generation by several orders of magnitude—the prothrombinase complex is 300 000 fold more efficient at catalyzing the conversion of prothrombin (factor II) to thrombin (factor IIa) than free FXa, emphasizing the importance of platelet function for thrombin generation. In vitro studies demonstrated that although heparins inhibit free FXa, FXa incorporated into the prothrombinase complex is protected from inhibition by antithrombin and by antithrombin-dependent heparins (independent of their molecular size). Selective
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The activation of factor X and prothrombin by recombinant factor VIIa in vivo is mediated by tissue factor

The activation of factor X and prothrombin by recombinant factor VIIa in vivo is mediated by tissue factor

mechanism occurs via Factor VIIa-dependent activation of Factor X, but direct proof has not been available for the participation of tissue factor in this pathway. To examine this issue, we infused relatively high concentrations of recombinant Factor VIIa (approximately 50 micrograms/kg body wt) into normal chimpanzees and observed significant increases in the plasma levels of Factor IX activation peptide, Factor X activation peptide, and prothrombin activation fragment F1+2. Metabolic turnover studies with radiolabeled Factor IX activation peptide, Factor X activation peptide, and F1+2 indicate that elevated levels of the activation peptides are due to accelerated conversion of the three coagulation system zymogens into serine proteases. The administration of a potent monoclonal antibody to tissue factor, which immediately neutralizes function of the Factor VIIa-tissue factor complex in vitro, abolishes the activation of Factor X and prothrombin mediated by the infused recombinant protein, and also suppresses basal level activation of Factor IX and Factor X. The above results suggest that recombinant Factor VIIa functions as a prohemostatic agent by interacting with
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The transcription factor X-box binding protein-1 in neurodegenerative diseases

The transcription factor X-box binding protein-1 in neurodegenerative diseases

demonstrated that DJ-1 expression is under control of parkin (PK) another protein involved in familial recessive cases of PD. Parkin, which has been largely studied for its role as an E3-ubiquitin ligase [67] possesses another function as a transcription factor [68,69]. Thus, we established that parkin represses the transactivation of the p53 promoter [68]. Interestingly we showed that p53 acts as an upstream negative regulator of XBP-1 [40]. Furthermore, we identified a XBP-1 consensus binding motif within the DJ-1 promoter sequence that is con- served in several species. Overall, our data suggested that parkin could control DJ-1 expression through a cascade involving two intermediates transcription factors p53 and XBP-1 [70]. Moreover, we have shown that this indirect control of DJ-1 by parkin can be abrogated by autosomal recessive parkin mutations implicated in familial cases of PD [40].
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Acquired Factor X Deficiency in a Negro Boy

Acquired Factor X Deficiency in a Negro Boy

mild fever and stiffness and swelling of the right hand developed. The patient’s physician gave him penicillin. Later that day the left hand and right knee became swollen and painful. Ab[r]

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X linked primary ciliary dyskinesia due to mutations in the cytoplasmic axonemal dynein assembly factor PIH1D3

X linked primary ciliary dyskinesia due to mutations in the cytoplasmic axonemal dynein assembly factor PIH1D3

PIH1D3 mutations cause PCD. A number of approaches were used by three molecular genetics laboratories (London, Geneva and Paris) to identify novel mutations causing PCD: next-generation sequencing (NGS) of whole exomes of affected individuals from 76 families, a targeted gene panel in affected individuals from 133 families and whole-genome SNP-array analyses in a male patient with intellectual disability and two male siblings from a consanguineous union. The identification of putative mutations in the X-linked gene PIH1D3 in different patients prompted us to screen this gene by Sanger sequencing in a cohort of 32 independent male patients; this targeted screening identified a high proportion of affected families, with four males from three families carrying PIH1D3 mutations (9.5% (3/32) of independent cases screened). Overall, these studies led to the identification of PIH1D3 molecular defects in affected males from nine independent families, which were all family-unique (Fig. 1a; Supplementary Figs 1 and 2): three nonsense mutations (c.127G4T, p.Glu43* in PCD12 II:1; c.266G4A, p.Trp89* in PCD392 II:1; c.511C4T, p.Gln171* in DCP1218), two frameshift mutations (c.263_268delinsG, p.Ile88Argfs*12 in DCP894; c.489_492del; p.Ile164Leufs*11 in GVA30 II:1), one missense change (c.397G4T, p.Asp133Tyr in DCP68), as well as genomic deletions containing the PIH1D3 gene (1.93-Mb, 3.27-Mb and 3.73-Mb deletions in DCP603/DCP1747, DCP1337 and DCP855, respectively). The complement of genes contained within the latter, larger deletions are listed in Supplementary Table 1. In the NGS screening no other variants of interest were detected, and all the nine identified PIH1D3 variants were unique, having never been previously reported and being absent from all available databases of normal human variation (ExAC, 1000G, EVS). The nonsense, frameshift and deletion mutations are all predicted as protein disrupting and Fig. 1b shows a high level of conservation of Asp133 which is located within a key surface domain of PIH1D3, as described further below.
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In vitro invasive ability of X and V factor dependent Haemophilus species across different cell types

In vitro invasive ability of X and V factor dependent Haemophilus species across different cell types

H. haemolyticus is very closely related to NTHi and shares the same upper respiratory tract niche. It is easy to distinguish NTHi and H. haemolyticus from other Haemophilus species due to requirement of both X and V blood derivatives for their in vitro growth, but it is a tedious task to discriminate these two on a phenotypic basis, as they possess very similar colony morphology and biochemical activity. Traditionally, the presence or absence of haemolysis on horse blood agar could be used to discriminate the two species; however, with the emergence of non-haemolytic strains of H. haemolyticus, the reliability of this marker is immensely hampered (Murphy et al., 2007; Sandstedt et al., 2008). Retrospective analysis by molecular detection methods have confirmed many instances where H. haemolyticus was erroneously identified as NTHi (Murphy et al., 2007). In one study, retrospective analysis of 490 phenotypic NTHi isolates by molecular methods demonstrated that 39.5% (102/156) of NTHi isolates from COPD patients and 27.3% (12/32) NTHi isolates recovered from the nasopharynx of children were actually non-haemolytic H. haemolyticus. Other studies also reported similar misidentification cases where 20.8% of presumptive NTHi recovered from throats of children and 16-21% of presumptive NTHi from lung specimens were identified as H. haemolyticus (Mukundan et al., 2007; Xie et al., 2006).
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Crystallization and preliminary X-ray analysis of the sporulation factor SpoIIAA in its native and phosphorylated forms

Crystallization and preliminary X-ray analysis of the sporulation factor SpoIIAA in its native and phosphorylated forms

Sporulation in Bacillus begins with an asymmetric cell division producing two progeny with identical chromosomes but different developmental fates. As such, it is a simple example of cellular differentiation. The establishment of cell type is controlled by a series of alternate RNA polymerase sigma subunits. The ®rst compartment- speci®c sigma factor is F , whose activity is controlled by SpoIIAB, an anti-sigma factor, and SpoIIAA, an anti-sigma factor antagonist which is phosphorylated by the kinase activity of SpoIIAB. Here, the preliminary crystallographic analysis of SpoIIAA and phosphoryl- ated SpoIIAA from B. sphaericus in forms suitable for high- resolution structure determination are reported.
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x < y iff x < y, or x and y are incomparable and x χ(x,y) < y χ(x,y).

x < y iff x < y, or x and y are incomparable and x χ(x,y) < y χ(x,y).

To prove the second assertion, let A be a collection of subsets of X with fip, and let C be the collection of all proper filters on X which contain A . Clearly the filter generated by A is proper, so C 6= ∅. We consider C as a partially ordered set under inclusion. Any subset D of C which is a chain has an upper bound in C , namely S D

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READ ONLY. Adopting Agency BSC SFM. Adopt Entire Chapter X X X X X X X X X Adopt Entire Chapter as amended (amended sections listed below)

READ ONLY. Adopting Agency BSC SFM. Adopt Entire Chapter X X X X X X X X X Adopt Entire Chapter as amended (amended sections listed below)

Storm drainage systems shall be permitted to be sized by storm water flow rates, using the gallons per minute per square foot (L/s/m 2 ) of rainfall listed in Table D.. 1.1 for the local[r]

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4)(x) du(x) = n-' E?(zi(x)) du(x),

4)(x) du(x) = n-' E?(zi(x)) du(x),

Using a functional equation fulfilled by the generating function, the author shows that the Hausdorff dimension of the maximal measure is a real analytical function of the coeffic[r]

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