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1.
Waste Manag ; 33(11): 2250-6, 2013 Nov.
Article in English | MEDLINE | ID: mdl-23932080

ABSTRACT

Rice straw can be used as a renewable fuel for heat and power generation. It is a viable mean of replacing fossil fuels and preventing pollution caused by open burning, especially in the areas where this residual biomass is generated. Nevertheless, the thermal conversion of rice straw can cause some operating problems such as slag formation, which negatively affects thermal conversion systems. So, the main objective of this research is studying the combustion behavior of rice straw samples collected from various regions by applying thermogravimetric analysis (TGA) and differential scanning calorimetry (DSC). In addition, the thermal behavior of ashes from rice straw was also analyzed in order to detect their melting points, and ash sintering was detected at different temperatures within the range between 550 and 1000°C. Since washing rice straw with water could reduce the content of undesirable inorganic compounds related to the ash fusibility, samples of washed rice straw were analyzed under combustion conditions to investigate its differences regarding the thermal behavior of rice straw. The results showed that rice straw washing led to a significant improvement in its thermal behavior, since it reduced the ash contents and sintering formation.


Subject(s)
Biofuels/analysis , Oryza/chemistry , Thermogravimetry , Water
2.
Waste Manag ; 33(11): 2245-9, 2013 Nov.
Article in English | MEDLINE | ID: mdl-23916844

ABSTRACT

The heterogeneity of biomass makes it difficult if not impossible to make sweeping generalizations concerning thermochemical treatment systems and the optimal equipment to be used in them. Chemical differences in the structural components of the biomass (cellulose, hemicellulose, and lignin) have a direct impact on its chemical reactivity. The aim of this research was to study the influence of the organic components of the raw material from olive trees (leaves, pruning residues, and wood) in the combustion behavior of this biomass, as well as to find the component responsible for the higher ash content of olive leaves. Accordingly, the study used a thermogravimetric analyzer to monitor the different states and complex transitions that occurred in the biomass as the temperature varied. The decomposition rates of the different samples were analyzed in order to establish a link between each combustion phase and the composition of the raw materials. Two methods were used to determine the hemicellulose and cellulose contents of biomass from olive trees. Significant differences among the results obtained by the different methods were observed, as well as important variations regarding the chemical composition and consequently the thermal behavior of the raw materials tested.


Subject(s)
Biofuels/analysis , Biomass , Olea/chemistry , Lignin/analysis , Plant Leaves/chemistry , Polysaccharides/analysis , Thermogravimetry , Wood/chemistry
3.
Oncogene ; 32(34): 4052-6, 2013 Aug 22.
Article in English | MEDLINE | ID: mdl-22986535

ABSTRACT

Current genetic evidence in mice indicates that SIRT1 has potent tumor suppressor activity in a variety of cancer models, with no evidence yet for SIRT1 oncogenic activity in vivo. We report here that transgenic Sirt1 expression is oncogenic in murine thyroid and prostate carcinogenesis initiated by Pten-deficiency. Based on mRNA expression analyses of pre-tumoral murine thyroids, we find that SIRT1 increases c-MYC transcriptional programs. Moreover, we show higher c-MYC protein levels in murine thyroid cancers from Sirt1 transgenic mice. Similarly, SIRT1 is overexpressed in human thyroid cancers and it is positively correlated with c-MYC protein levels. Finally, we show in cultured thyroid cancer cells that SIRT1 stabilizes c-MYC protein. These results implicate SIRT1 as a new candidate target for the treatment of thyroid carcinomas.


Subject(s)
Cell Transformation, Neoplastic/genetics , PTEN Phosphohydrolase/genetics , Sirtuin 1/genetics , Thyroid Gland/metabolism , Thyroid Neoplasms/genetics , Animals , Cell Line, Tumor , Cell Transformation, Neoplastic/metabolism , Female , Gene Expression Regulation, Neoplastic , Humans , Immunohistochemistry , Male , Mice , Mice, Knockout , Mice, Transgenic , PTEN Phosphohydrolase/deficiency , Proto-Oncogene Proteins c-myc/genetics , Proto-Oncogene Proteins c-myc/metabolism , RNA Interference , Reverse Transcriptase Polymerase Chain Reaction , Sirtuin 1/metabolism , Thyroid Gland/pathology , Thyroid Neoplasms/metabolism , Thyroid Neoplasms/pathology
5.
6.
J Virol ; 75(22): 10815-28, 2001 Nov.
Article in English | MEDLINE | ID: mdl-11602723

ABSTRACT

Infectious bursal disease virus (IBDV), a member of the Birnaviridae family, is a double-stranded RNA virus. The IBDV capsid is formed by two major structural proteins, VP2 and VP3, which assemble to form a T=13 markedly nonspherical capsid. During viral infection, VP2 is initially synthesized as a precursor, called VPX, whose C end is proteolytically processed to the mature form during capsid assembly. We have computed three-dimensional maps of IBDV capsid and virus-like particles built up by VP2 alone by using electron cryomicroscopy and image-processing techniques. The IBDV single-shelled capsid is characterized by the presence of 260 protruding trimers on the outer surface. Five classes of trimers can be distinguished according to their different local environments. When VP2 is expressed alone in insect cells, dodecahedral particles form spontaneously; these may be assembled into larger, fragile icosahedral capsids built up by 12 dodecahedral capsids. Each dodecahedral capsid is an empty T=1 shell composed of 20 trimeric clusters of VP2. Structural comparison between IBDV capsids and capsids consisting of VP2 alone allowed the determination of the major capsid protein locations and the interactions between them. Whereas VP2 forms the outer protruding trimers, VP3 is found as trimers on the inner surface and may be responsible for stabilizing functions. Since elimination of the C-terminal region of VPX is correlated with the assembly of T=1 capsids, this domain might be involved (either alone or in cooperation with VP3) in the induction of different conformations of VP2 during capsid morphogenesis.


Subject(s)
Infectious bursal disease virus/physiology , Viral Structural Proteins/physiology , Virus Assembly , Animals , Capsid/analysis , Capsid/physiology , Chick Embryo , Infectious bursal disease virus/immunology , Microscopy, Electron , Viral Structural Proteins/analysis , Viral Structural Proteins/chemistry , Viral Vaccines/immunology
7.
Virology ; 277(2): 345-57, 2000 Nov 25.
Article in English | MEDLINE | ID: mdl-11080482

ABSTRACT

Infectious bursal disease virus (IBDV) encodes a 17-kDa nonstructural polypeptide known as VP5. This polypeptide is not essential for virus replication in vitro but it plays an important role in in vivo dissemination and pathogenesis. We have characterized the expression of VP5 in three eukaryotic systems: (i) IBDV-infected chicken embryo fibroblasts; (ii) BSC-1 cells infected with a recombinant vaccinia virus vector; and (iii) Cos-1 cells transiently transfected with a plasmid vector. Immunofluorescence analyses showed that upon expression VP5 accumulates within the plasma membrane. This finding was consistent with sequence-based topology predictions, indicating that VP5 is a class II membrane protein with a cytoplasmic N-terminus and an extracellular C-terminal domain. Brefeldin A treatment of VP5-expressing cells prevented the accumulation of this polypeptide in the plasma membrane, thus showing the requirement of an active exocytic pathway to reach that compartment. Expression of VP5 was shown to be highly cytotoxic. Induction of VP5 expression resulted in the alteration of cell morphology, the disruption of the plasma membrane, and a drastic reduction of cell viability. VP5-induced cytotoxicity was prevented by blocking its transport to the membrane with Brefeldin A. Our findings suggest that VP5 plays an important role in the release of the IBDV progeny.


Subject(s)
Cell Membrane/metabolism , Infectious bursal disease virus/pathogenicity , Viral Nonstructural Proteins/metabolism , Amino Acid Sequence , Animals , Antiviral Agents/pharmacology , Blotting, Western , Brefeldin A/pharmacology , COS Cells , Cell Death , Cell Membrane/drug effects , Cell Membrane Permeability/drug effects , Cells, Cultured , Chick Embryo , Fibroblasts , Immunohistochemistry , Molecular Sequence Data , Transformation, Genetic , Viral Nonstructural Proteins/analysis , Viral Nonstructural Proteins/genetics
8.
J Virol ; 73(8): 6973-83, 1999 Aug.
Article in English | MEDLINE | ID: mdl-10400796

ABSTRACT

A cDNA corresponding to the coding region of VP1, the putative RNA-dependent RNA polymerase, of infectious bursal disease virus (IBDV) was cloned and inserted into the genome of a vaccinia virus inducible expression vector. The molecular mass and antigenic reactivity of VP1 expressed in mammalian cells are identical to those of its counterpart expressed in IBDV-infected cells. The results presented here demonstrate that VP1 is efficiently incorporated into IBDV virus-like particles (VLPs) produced in mammalian cells coexpressing the IBDV polyprotein and VP1. Incorporation of VP1 into VLPs requires neither the presence of IBDV RNAs nor that of the nonstructural polypeptide VP5. Immunofluorescence, confocal laser scanning microscopy, and immunoprecipitation analyses conclusively showed that VP1 forms complexes with the structural polypeptide VP3. Formation of VP1-VP3 complexes is likely to be a key step for the morphogenesis of IBDV particles.


Subject(s)
Capsid/metabolism , Infectious bursal disease virus/enzymology , RNA-Dependent RNA Polymerase/metabolism , Viral Structural Proteins/metabolism , Virus Assembly , Animals , Capsid Proteins , Cell Line , Chlorocebus aethiops , Gene Expression , HeLa Cells , Humans , Infectious bursal disease virus/physiology , Proteins/metabolism , RNA-Dependent RNA Polymerase/genetics , Subcellular Fractions , Viral Structural Proteins/genetics , Virion
9.
Am J Gastroenterol ; 90(3): 471-4, 1995 Mar.
Article in English | MEDLINE | ID: mdl-7872288

ABSTRACT

Patients with hereditary angioedema have episodes of local swelling, usually affecting the face, extremities, upper airway, and gastrointestinal tract. Only infrequently does it cause recurrent abdominal pain (with or without ascites); however, because it has potentially life-threatening complications, an early diagnosis is important. We describe a case of type I hereditary angioedema (a quantitative deficit of C1 inhibitor), the sole initial symptom of which was severe recurrent and self-limited abdominal pain, accompanied by ascites during these episodes. During a 4-yr period of treatment with danazol, the patient was virtually asymptomatic, despite levels of C4 and C1 inhibitor that remained below normal limits, and there have been no major side effects that could be attributed to treatment with androgens.


Subject(s)
Abdominal Pain/genetics , Angioedema/genetics , Ascites/genetics , Complement C1 Inactivator Proteins/deficiency , Adult , Angioedema/drug therapy , Danazol/therapeutic use , Female , Humans , Pedigree
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