Acoustic images of gel dosimetry phantoms

AbstractThis work presents Vibro-acoustography (VA) as a tool to visualize absorbed dose in a polymer gel dosimetry phantom. VA relies on the mechanical excitation introduced by the acoustic radiation force of focused modulated ultrasound in a small region of the object. A hydrophone or microphone is used to measure the sound emitted from the object in response to the excitation, and by using the amplitude or phase of this signal, an image of the object can be generated. To study the phenomena of dose distribution in a gel dosimetry phantom, continuous wave (CW), tone burst and multi-frequency VA were used to image this phantom. The phantom was designed using ‘MAGIC’ gel polymer with addition of glass microspheres at 2% w/w having an average diameter range between 40–75 μm. The gel was irradiated using conventional 10 MeV X-rays from a linear accelerator. The field size in the surface of the phantom was 1.0×1.0 cm2 and a source-surface distance (SSD) of 100 cm. The irradiated volume corresponds to an approximately 8.0 cm3, where a dose of 50 gray was delivered to the gel. Polymer gel dosimeters are sensitive to radiation-induced chemical changes that occur in the irradiated polymer. VA images of the gel dosimeter showed the irradiate area. It is concluded that VA imaging has potential to visualize dose distribution in a polymer gel dosimeter

Proteome Analysis of Leptospira interrogans Virulent Strain

Leptospirosis is a worldwide zoonotic infection of human and veterinary concern. Caused by pathogenic spirochetes of the genus Leptospira, the disease presents greater incidence in tropical and subtropical regions. The identification of proteins that could be involved in the bacteria host interactions may facilitate the search for immune protective antigens. We report the proteomic analysis of Leptospira interrogans serovar Pomona virulent strain LPF cultured from kidney and liver of infected hamsters. Total protein extracts were separated by two-dimensional gel electrophoresis (2-DE), 895 spots were analyzed by MALDI-TOF mass spectrometry (MS), and 286 were identified as leptospiral proteins, corresponding to 108 distinct proteins. These proteins are allocated in all the bacterial cell compartments and are distributed in every functional category. Furthermore, the previously described, known outer membrane proteins, OmpL1, LipL21, LipL31, LipL32/Hap-1, LipL41, LipL45, LipL46, LruA/LipL71, and OmpA-like protein Loa22 were all recognized. Most importantly, this research work identified 27 novel leptospiral proteins annotated as hypothetical open reading frames (ORFs). We report for the first time an array of proteins of the Leptospira expressed by virulent, low-passage strain. We believe that our studies, together with the genome data will enlighten our understanding of the disease

Human fallopian tube: a new source of multipotent adult mesenchymal stem cells discarded in surgical procedures

<p>Abstract</p> <p>Background</p> <p>The possibility of using stem cells for regenerative medicine has opened a new field of investigation. The search for sources to obtain multipotent stem cells from discarded tissues or through non-invasive procedures is of great interest. It has been shown that mesenchymal stem cells (MSCs) obtained from umbilical cords, dental pulp and adipose tissue, which are all biological discards, are able to differentiate into muscle, fat, bone and cartilage cell lineages. The aim of this study was to isolate, expand, characterize and assess the differentiation potential of MSCs from human fallopian tubes (hFTs).</p> <p>Methods</p> <p>Lineages of hFTs were expanded, had their karyotype analyzed, were characterized by flow cytometry and underwent <it>in vitro </it>adipogenic, chondrogenic, osteogenic, and myogenic differentiation.</p> <p>Results</p> <p>Here we show for the first time that hFTs, which are discarded after some gynecological procedures, are a rich additional source of MSCs, which we designated as <it>human tube MSCs </it>(htMSCs).</p> <p>Conclusion</p> <p>Human tube MSCs can be easily isolated, expanded <it>in vitro</it>, present a mesenchymal profile and are able to differentiate into muscle, fat, cartilage and bone <it>in vitro</it>.</p

A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells

It has been reported previously that activation of vascular endothelium by outer membrane proteins of the spirochetes Borrelia sp. and Treponema sp. resulted in enhanced expression of endothelial cell adhesion molecules. To investigate the role of leptospiral proteins in this process, a predicted lipoprotein encoded by the gene LIC10365 was selected, which belongs to a paralogous family that presents a domain of unknown function, DUF1565. The LIC10365 gene was cloned and the protein expressed in Escherichia coli C43 (DE3) strain using the vector pAE. The recombinant protein tagged with N-terminal hexahistidine was purified by metal-charged chromatography and was used to assess its ability to activate cultured human umbilical vein endothelial cells. The rLIC10365 activated endothelium in such a manner that E-selectin and intercellular adhesion molecule 1 (ICAM-1) became upregulated in a dose-dependent fashion. The LIC10365-encoded protein was identified in vivo in the renal tubules of animal during experimental infection with Leptospira interrogans. Collectively, these results implicate the LIC10365-coding protein of L. interrogans as a potential effector molecule in the promotion of a host inflammatory response. This is the first report of a leptospiral protein capable of up-regulating the expression of endothelial cell adhesion molecules ICAM-1 and E-selectin.Instituto de Biotecnologia y Biologia Molecula

A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells

It has been reported previously that activation of vascular endothelium by outer membrane proteins of the spirochetes Borrelia sp. and Treponema sp. resulted in enhanced expression of endothelial cell adhesion molecules. To investigate the role of leptospiral proteins in this process, a predicted lipoprotein encoded by the gene LIC10365 was selected, which belongs to a paralogous family that presents a domain of unknown function, DUF1565. The LIC10365 gene was cloned and the protein expressed in Escherichia coli C43 (DE3) strain using the vector pAE. The recombinant protein tagged with N-terminal hexahistidine was purified by metal-charged chromatography and was used to assess its ability to activate cultured human umbilical vein endothelial cells. The rLIC10365 activated endothelium in such a manner that E-selectin and intercellular adhesion molecule 1 (ICAM-1) became upregulated in a dose-dependent fashion. The LIC10365-encoded protein was identified in vivo in the renal tubules of animal during experimental infection with Leptospira interrogans. Collectively, these results implicate the LIC10365-coding protein of L. interrogans as a potential effector molecule in the promotion of a host inflammatory response. This is the first report of a leptospiral protein capable of up-regulating the expression of endothelial cell adhesion molecules ICAM-1 and E-selectin.Instituto de Biotecnologia y Biologia Molecula

Features of two proteins of Leptospira interrogans with potential role in host-pathogen interactions

Background: Leptospirosis is considered a re-emerging infectious disease caused by pathogenic spirochaetes of the genus Leptospira. Pathogenic leptospires have the ability to survive and disseminate to multiple organs after penetrating the host. Leptospires were shown to express surface proteins that interact with the extracellular matrix (ECM) and to plasminogen (PLG). This study examined the interaction of two putative leptospiral proteins with laminin, collagen Type I, collagen Type IV, cellular fibronectin, plasma fibronectin, PLG, factor H and C4bp. Results: We show that two leptospiral proteins encoded by LIC11834 and LIC12253 genes interact with laminin in a dose - dependent and saturable mode, with dissociation equilibrium constants (K-D) of 367.5 and 415.4 nM, respectively. These proteins were named Lsa33 and Lsa25 (Leptospiral surface adhesin) for LIC11834 and LIC12253, respectively. Metaperiodate - treated laminin reduced Lsa25 - laminin interaction, suggesting that sugar moieties of this ligand participate in this interaction. The Lsa33 is also PLG - binding receptor, with a K-D of 23.53 nM, capable of generating plasmin in the presence of an activator. Although in a weak manner, both proteins interact with C4bp, a regulator of complement classical route. In silico analysis together with proteinase K and immunoflorescence data suggest that these proteins might be surface exposed. Moreover, the recombinant proteins partially inhibited leptospiral adherence to immobilized laminin and PLG. Conclusions: We believe that these multifunctional proteins have the potential to participate in the interaction of leptospires to hosts by mediating adhesion and by helping the bacteria to escape the immune system and to overcome tissue barriers. To our knowledge, Lsa33 is the first leptospiral protein described to date with the capability of binding laminin, PLG and C4bp in vitro.FAPESPFAPESPCNPqCNPqFundacao Butantan, BrazilFundacao Butantan, Brazi

A novel leptospiral protein increases ICAM-1 and E-selectin expression in human umbilical vein endothelial cells

It has been reported previously that activation of vascular endothelium by outer membrane proteins of the spirochetes Borrelia sp. and Treponema sp. resulted in enhanced expression of endothelial cell adhesion molecules. To investigate the role of leptospiral proteins in this process, a predicted lipoprotein encoded by the gene LIC10365 was selected, which belongs to a paralogous family that presents a domain of unknown function, DUF1565. The LIC10365 gene was cloned and the protein expressed in Escherichia coli C43 (DE3) strain using the vector pAE. The recombinant protein tagged with N-terminal hexahistidine was purified by metal-charged chromatography and was used to assess its ability to activate cultured human umbilical vein endothelial cells. The rLIC10365 activated endothelium in such a manner that E-selectin and intercellular adhesion molecule 1 (ICAM-1) became upregulated in a dose-dependent fashion. The LIC10365-encoded protein was identified in vivo in the renal tubules of animal during experimental infection with Leptospira interrogans. Collectively, these results implicate the LIC10365-coding protein of L. interrogans as a potential effector molecule in the promotion of a host inflammatory response. This is the first report of a leptospiral protein capable of up-regulating the expression of endothelial cell adhesion molecules ICAM-1 and E-selectin.Instituto de Biotecnologia y Biologia Molecula

Effect of Nickel Nanocatalyst Loading on Supercritical Water Gasification of Coconut Shell

Impregnation of metal catalysts into biomass before thermochemical conversion may provide benefits of increased selective reactivity to obtain desirable products. In this work, coconut shells impregnated with increasing loadings of nickel were successfully prepared using a room-temperature impregnation method using a nickel salt solution at 1 and 2 molar (M) concentrations. The physicochemical characterization of the 2 M impregnated sample revealed the presence of 5.6 wt% of nickel with a particle size of 13.5 nm. The nickel-impregnated samples’ supercritical water gasification (SCWG) was conducted with biomass loading ranging from 20 wt% to 30 wt%, at temperatures between 400 °C and 500 °C, and residence times from 20 to 60 min. Higher nickel loading, higher temperatures and longer reaction times promoted the production of H2 and CO2 up to 15 and 79 mol%. Higher nickel loading also led to an increased Hydrogen Gasification Efficiency value of up to 133%. The analysis of hydrochars suggested that increasing nickel loading enhanced the reduction in nickel ions to the Ni0 nanoparticles, leading to higher H2. Additionally, the chemical composition of the liquid product showed the significant ability of nickel to promote lignin decomposition into phenol, facilitating the phenol hydrogenation reaction and subsequent gas production