Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.69 (APC)
 16,337 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This work studies the effect of water content on the aging of APC residues, with a liquid to solid ratio (L/S) of 0.25 or 10, aged with or without exposure to ambient air. After the residue was mixed with water, CaSO4 and (Na,K)Al3(SO4)2(OH)6 in the raw sample yielded ettringite. When CO2 were available, this ettringite was further transformed to gypsum, calcite and possibly gibbsite. Experimental data revealed that the concentrations of Pb, Zn, Cd, Hg, and Cu fell with age, whereas that of Cr increased. Given L/S=10, excess Ca2+ ions were present in the suspension, so a precipitate of primarily calcite crystals of sizes under 5 microm formed on the air-water surface. This layer significantly reduced the rates of decline of Pb, Zn, Cd and Hg contents, and also reduced the increasing rate of Cr content in the suspension. This result follows from the mass transfer barrier of CO2 added at the air-water surface and the occurrence of subsequent chemical reactions in the suspension. An estimate of the mass transfer rate revealed that the rate-controlling step with L/S=10 was the dissolution and diffusion of CO2 in the bulk solution. However, at L/S=0.25, the rate-limiting step was the dissolution of metals from ash particles. Water content is a very important process factor, whose distribution in the sample, and the resulting competition between carbonate ion flux and heavy metal flux, govern the reaction time required during the natural aging process.
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PMID:Aging of air pollution control residues from municipal solid waste incinerator: role of water content on metal carbonation. 1600 25

In vivo protective effects of s-allyl cysteine (SAC) and s-propyl cysteine (SPC) against acetaminophen-induced hepatotoxicity in Balb/cA mice were studied. SAC and SPC at 1g/L were added into drinking water for four weeks and followed by acetaminophen treatment. Acetaminophen treatment significantly depleted glutathione content, increased oxidation stress and elevated alanine aminotransferase (ALT) and aspartate aminotransferase (AST) activities (P < 0.05); however, the intake of SAC or SPC significantly alleviated glutathione depletion and the elevation of ALT and AST, enhanced glutathione peroxidase activity, and lowered malondialdehyde formation (P < 0.05). Plasma levels of C-reactive protein (CRP), von Willebrand factor (vWF), IL-6, IL-10 and TNF-alpha were significantly increased by acetaminophen treatment (P < 0.05); and SAC or SPC intake significantly suppressed acetaminophen-induced elevation of CRP, vWF and the three cytokines (P < 0.05). Acetaminophen treatment also significantly increased plasminogen activator inhibitor-1 (PAI-1) activity and plasma fibrinogen level, and decreased antithrombin III (AT-III) and protein C activities (P < 0.05). SAC or SPC intake alleviated AT-III and protein C reduction (P < 0.05); but did not affect PAI-1 activity and plasma fibrinogen level (P > 0.05). These data suggest that SAC and SPC are potential multiple-protective agents against acetaminophen-induced hepatotoxicity.
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PMID:Protective effect of s-allyl cysteine and s-propyl cysteine on acetaminophen-induced hepatotoxicity in mice. 1618 16

In this study, we investigated the effects of warfarin potassium on the incidence of the femoral head osteonecrosis in spontaneously hypertensive rats (SHR). Twenty-four SHRs were divided into two equal groups, one given normal water (water group) and another provided with water containing warfarin (warfarin group). We compared the two groups histologically and observed the incidence of osteonecrosis. We also studied 17 Wistar Kyoto rats (WKY) to compare with SHR. Coagulation time, platelet count, and protein C activity were measured. Immunohistochemistry was also performed using endothelial nitric oxide synthetase (eNOS) antibody to investigate the function of endothelial cells. The incidence of osteonecrosis was significantly less in the warfarin group (10.5%) than in the water group (52.6%). Coagulation time was significantly longer in the warfarin group than the water group. Platelet count and protein C activity were not statistically different between the warfarin group and the water group. Results of immunohistochemistry revealed that endothelial cells in the femoral head were positive for eNOS in WKY but not in SHR. Our results indicated that warfarin reduced the incidence of femoral head necrosis in SHR.
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PMID:Warfarin reduces the incidence of osteonecrosis of the femoral head in spontaneously hypertensive rats. 1622 76

Thrombovascular diseases result from imbalanced haemostasis and comprise important health problems in the aging population worldwide. The activity of enzymes pertaining to the coagulation cascade of mammalians exhibit several control mechanisms in order to maintain a proper balance between bleeding and thrombosis. For instance, human coagulation serine proteases carrying a F225 or Y225 are allosteric modulated by the binding of Na+ in a water-filled channel connected to the primary specificity pocket (S1 subsite) of these enzymes. We have characterized the structure, topography and lipophilicity of this channel in the ligand-free fast (sodium-bound) and slow (sodium-free) forms of thrombin, in the sole available structure of activated protein C and in several structures of the coagulation factors VIIa, IXa and Xa, differing in the nature of the bound inhibitor and in the occupancy of exosite-I as well as the Ca2+ and Na+ binding sites. Opposite to thrombin, the aqueous channels in all other coagulation enzymes sheltering a Na+ binding site do not have an aperture on the enzyme surface opposite to the S1 subsite entrance. In these enzymes, the lack of the three-residue insertion in loop 1 (183-189) as found in thrombin allied to compensatory mutations in the positions 187-185 and 222 effects a constriction in the water-filled channel that ends up by segregating the ion binding site from the S1 subsite. We also disclosed major topographical changes on the thrombin's surface upon sodium release and transition to the slow form that culminate in the narrowing of the S1 subsite entrance and, strikingly, in the loss of communication between the primary specificity pocket and the exosite-I. Such observation is in accordance with existing experimental data demonstrating thermodynamic linkage between these distant regions on the thrombin surface. Conformational changes in F34, L40, R73 and T74 were the main responsible for this effect. A path by which these changes in the vicinity of exosite-I could be transmitted to the S1 subsite and, consequently, to the sodium binding site is proposed.
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PMID:The Na+ binding channel of human coagulation proteases: novel insights on the structure and allosteric modulation revealed by molecular surface analysis. 1628 54

Interaction of the gamma-carboxyglutamic acid (Gla) domain of protein C with endothelial protein C receptor (EPCR) is a critical step for efficient activation of protein C, though interactions by mutants in the Gla domain of protein C with EPCR have been rarely evaluated. We identified a 44-year-old Japanese woman with a history of recurrent thromboembolism as an inherited missense mutation, the first such case reported in Japan, which involved a protein C Gla 25 mutation. Total protein C antigen and Gla protein C antigen levels in the proband were normal. Protein C activity measured with an anticoagulant assay was reduced, whereas that measured with an amidolytic assay was normal. She was therefore phenotypically diagnosed as type IIb protein C deficiency. Direct sequencing of the PCR fragments revealed a heterozygous G to A transition at nucleotide position 1462 in exon 3, which predicted an amino acid substitution of Glu 25 by Lys. Her mother and one son were also heterozygous for this mutation. A molecular dynamics simulation of Gla 25-->Lys/EPCR complex in water suggested that the affinity between the molecules was decreased compared to the wild type Gla domain/EPCR complex. Since Gla 25 has been shown to play an important role in protein C function, not only in membrane phospholipid binding but also in binding to EPCR, our findings provide new insight into the mechanism by which the Glu 25-->Lys mutation induces type IIb protein C deficiency in individuals.
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PMID:Protein C Sapporo (protein C Glu 25 --> Lys): a heterozygous missense mutation in the Gla domain provides new insight into the interaction between protein C and endothelial protein C receptor. 1636 34

Surfactant protein C (SP-C) is a membrane-associated protein essential for normal respiration. It has been found that the alpha-helix form of SP-C can undergo, under certain conditions, a transformation from an alpha-helix to a beta-strand conformation that closely resembles amyloid fibrils, which are possible contributors to the pathogenesis of pulmonary alveolar proteinosis. Molecular dynamics simulations using the NAMD2 package were performed for systems containing from one to seven SP-C molecules to study their behavior in water. The results of our simulations show that unfolding of the protein occurs at the amino terminal, and despite this unfolding, no transition from alpha-helix to beta-strand was observed.
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PMID:Molecular dynamics of surfactant protein C: from single molecule to heptameric aggregates. 1644 48

Several groups report stability results for freeze-dried whole plasma intended for use as a transfusion product [Hellstern P, Sachse H, Schwinn H, Oberfrank K. Manufacture and in vitro characterization of a solvent/detergent-treated human plasma. Vox Sang 1992;63:178-185; Trobisch H. Results of a quality-control study of lyophilized pooled plasmas which have been virally inactivated using a solvent detergent method (modified Horowitz procedure). Beitr Infusionsther 1991;28:92-109; Hugler P, Trobish H, Neuman H, Moller, Sirtl C, Derdak M, Laubenthal H. Quality control of three different conventional fresh-frozen plasma preparations and one new virus-inactivated lyophilized pooled plasma preparation. Klin Wochenschr 1991;69:157-161; Krutvacho T, Chuansumrit A, Isarangkura P, Pintadit P, Hathirat P, Chiewsilp P. Response of hemophilia with bleeding to fresh dry plasma. Southeast Asian J Trop Med Public Health 1993;24:169-173; Chuansumrit A, Krasaesub S, Angchaisuksiri P, Hathirat P, Isarangkura P. Survival analysis of patients with haemophilia at the International Haemophilia Training Centre, Bangkok, Thailand. Haemophilia 2004;10:542-549]. Plasma coagulation properties are substantially impaired in these freeze-dried plasmas, while pH levels are close to alkaline. In this work, plasma supplemented with 60mM sucrose, trehalose, mannitol, sorbitol or glycine was freeze-dried. The samples were subjected to forced degradation at 40 degrees C for 10 days in order to quickly evaluate the effectiveness of the different stabilizers. Initial PT, APTT and TT values were 14.4+/-0. 5s, 31.4+/-1.5s and 18.3+/-0.6s, respectively. At the end of the degradation period, PT, APTT and TT were substantially prolonged, and were 19.1+/-0. 5s, 43.1+/-0.6s and 26.1+/-1.0s, respectively. In the presence of glycine, at the end of the degradation period, PT, APTT and TT values remained close to the initial values and were 15.5+/-0. 4s, 35.7+/-0.9s and 19.4+/-0.2s, respectively. Percent activities of the coagulation factors V, VII, VIII, IX, X and the coagulation inhibitors protein C, protein S and antithrombin III were recorded. Factors V and VIII were most prone to degradation. Factor V and VIII activities, in control plasma, were approx. 44+/-3.5% and 58+/-2.3%, at the end of storage. In contrast, much higher factor V and VIII activities were maintained in the lyophilized glycine-supplemented plasma: approx. 60+/-3.5% and 74+/-7.0%, correspondingly. The most stable protein was protein C, which showed no signs of degradation under the testing conditions of this study. All tested stabilizers provided protection. Glycine, however, outperformed all tested polyols, providing superior preservation of plasma clotting properties. Thermograms of 60mM glycine in water and 60mM glycine in plasma show that, in the presence of plasma, glycine does not crystallize. The process of freeze-drying caused a complete loss of plasma pCO(2) (gas) and a substantial increase in plasma pH. Citric acid was found to be a suitable pH adjuster for lyophilized/rehydrated plasma.
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PMID:Freeze-dried whole plasma: evaluating sucrose, trehalose, sorbitol, mannitol and glycine as stabilizers. 1696 45

A study was conducted to investigate the bacteriological impact of using different volumes of water during immersion chilling of broiler carcasses. Market-aged broilers were processed, and carcasses were cut into left and right halves along the keel bone immediately after the final bird wash. One half of each carcass pair was individually chilled at 4 degrees C in a separate bag containing either 2.1 L/kg (low) or 16.8 L/kg (high) of distilled water. Carcass halves were submersed in a secondary chill tank containing approximately 150 L of an ice-water mix (0.6 degrees C). After chilling for 45 min, carcass halves were rinsed with 100 mL of sterile water for 1 min. Rinses and chill water were analyzed for total aerobic bacteria (APC), Escherichia coli, Enterobacteriaceae, and Campylobacter. After chilling with a low volume of water, counts were 3.7, 2.5, 2.6, and 2.1 log(10) cfu/mL of rinse for APC, E. coli, Enterobacteriaceae, and Campylobacter, respectively. When a high volume of chill water was used, counts were 3.2, 1.7, 1.6, and 1.8 log(10) cfu/mL of rinse for APC, E. coli, Enterobacteriaceae, and Campylobacter, respectively. There was no difference in bacterial counts per milliliter of chill water among treatments. These results show that using additional water during immersion chilling of inoculated broilers will remove more bacteria from the carcass surfaces, but numbers of bacteria per milliliter in the chiller water will remain constant. The bacteriological impact of using more water during commercial immersion chilling may not be enough to offset economic costs.
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PMID:Broiler carcass bacterial counts after immersion chilling using either a low or high volume of water. 1701 73

Effects of trisodium phosphate (TSP) and/or sodium chloride (NaCl) dipping on microbial quality and shelf life of chicken breasts were investigated during refrigeration. Chicken breasts were dipped in aqueous solution (w/v) of 10% TSP, 10% NaCl, combination of TSP and NaCl (7.5% + 7.5%) or distilled water (control) for 10 min, followed by tray-packaging storage at 2 degrees C. During storage, chicken breasts dipped in TSP maintained almost constant pH, while pH of control or NaCl-treated samples significantly increased (P<0.05). TSP dipping resulted in initial reduction of 0.48 and 0.91 log(10) CFU/g in aerobic plate counts and Enterobacteriaceae count, respectively, when compared with control. By storage day 6, APC of control chicken breasts reached 6.91 log(10) CFU/g, while TSP-treatment either alone or in combination with NaCl significantly delayed microbial growth (P<0.05) and extended shelf life of refrigerated chicken breasts up to 12 days, at which APC were 6.87 and 6.39, respectively, versus 9.58 log(10) CFU/g for control. Significant reductions in psychrotrophic and Enterobacteriaceae count were detected at the end of storage period in chicken breasts treated with TSP alone or in combination with NaCl, whereas such treatments had no significant effects on lactobacilli or mold and yeast populations.
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PMID:Effects of Trisodium Phosphate and Sodium Chloride Dipping on the Microbial Quality and Shelf Life of Refrigerated Tray-packaged Chicken Breasts. 1733 Jan 56

Short-term dextran sodium sulfate (DSS) treatment has been shown to notably accelerate colorectal tumor development in rats initiated with 1,2-dimethylhydrazine (DMH). In the present study, to clarify mechanisms underlying the DSS influence, time-course studies of histopathological and immunohistochemical characteristics and beta-catenin gene mutations in colorectal mucosa in early stages of this model were conducted. F344 males were given three subcutaneous injections of DMH (40 mg/kg body wt) within a week, followed by free access to drinking water containing 1% DSS for a week. At weeks 1, 4, 6 and 8 after the DSS treatment, rats were euthanized and colorectal samples were collected. At week 1, the colorectal mucosa demonstrated extensive erosion along with significant inflammatory cell infiltration and neighboring reactive hyperplasia. By week 4, the mucosal damage was repaired and regenerative mucosa, partly characterized by Paneth cell metaplasia and altered subcellular localization of beta-catenin, was apparent. Areas with Paneth cells/beta-catenin accumulation were significantly more likely to be accompanied by interstitial inflammation and 17 of 24 dysplastic foci were found in regenerative mucosa with Paneth cells. Furthermore, adenomas/carcinomas frequently featured various degrees of Paneth cell differentiation. Point mutations mainly in codons 34 and 41 of beta-catenin gene were detected in 6 of 27 samples of regenerative mucosa with Paneth cells and four of nine dysplastic foci/adenomas/carcinomas. These findings indicate that inflammation-associated regenerative mucosa with Paneth cell metaplasia and alteration in the APC/beta-catenin/Tcf signal transduction pathway are possibly involved in the acceleration of colorectal carcinogenesis in this DMH-DSS rat model.
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PMID:Significance of inflammation-associated regenerative mucosa characterized by Paneth cell metaplasia and beta-catenin accumulation for the onset of colorectal carcinogenesis in rats initiated with 1,2-dimethylhydrazine. 1751 83


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