{"title":"Structural characterization and antioxidative activity of low-molecular-weights beta-1,3-glucan from the residue of extracted Ganoderma lucidum fruiting bodies.","authors":"Pai-Feng Kao, Shwu-Huey Wang, Wei-Ting Hung, Yu-Han Liao, Chun-Mao Lin, Wen-Bin Yang","doi":"10.1155/2012/673764","DOIUrl":"https://doi.org/10.1155/2012/673764","url":null,"abstract":"<p><p>The major cell wall constituent of Ganoderma lucidum (G. lucidum) is β-1,3-glucan. This study examined the polysaccharide from the residues of alkaline-extracted fruiting bodies using high-performance anion-exchange chromatography (HPAEC), and it employed nuclear magnetic resonance (NMR) and mass spectrometry (MS) to confirm the structures. We have successfully isolated low-molecular-weight β-1,3-glucan (LMG), in high yields, from the waste residue of extracted fruiting bodies of G. lucidum. The 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide (MTT) assay evaluated the capability of LMG to suppress H₂O₂-induced cell death in RAW264.7 cells, identifying that LMG protected cells from H₂O₂-induced damage. LMG treatment decreased H₂O₂-induced intracellular reactive oxygen species (ROS) production. LMG also influenced sphingomyelinase (SMase) activity, stimulated by cell death to induce ceramide formation, and then increase cell ROS production. Estimation of the activities of neutral and acid SMases in vitro showed that LMG suppressed the activities of both neutral and acid SMases in a concentration-dependent manner. These results suggest that LMG, a water-soluble β-1,3-glucan recycled from extracted residue of G. lucidum, possesses antioxidant capability against H₂O₂-induced cell death by attenuating intracellular ROS and inhibiting SMase activity.</p>","PeriodicalId":15089,"journal":{"name":"Journal of Biomedicine and Biotechnology","volume":" ","pages":"673764"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/673764","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30340403","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Sameer B Shah, James M Love, Andrea O'Neill, Richard M Lovering, Robert J Bloch
{"title":"Influences of desmin and keratin 19 on passive biomechanical properties of mouse skeletal muscle.","authors":"Sameer B Shah, James M Love, Andrea O'Neill, Richard M Lovering, Robert J Bloch","doi":"10.1155/2012/704061","DOIUrl":"https://doi.org/10.1155/2012/704061","url":null,"abstract":"<p><p>In skeletal muscle fibers, forces must be transmitted between the plasma membrane and the intracellular contractile lattice, and within this lattice between adjacent myofibrils. Based on their prevalence, biomechanical properties and localization, desmin and keratin intermediate filaments (IFs) are likely to participate in structural connectivity and force transmission. We examined the passive load-bearing response of single fibers from the extensor digitorum longus (EDL) muscles of young (3 months) and aged (10 months) wild-type, desmin-null, K19-null, and desmin/K19 double-null mice. Though fibers are more compliant in all mutant genotypes compared to wild-type, the structural response of each genotype is distinct, suggesting multiple mechanisms by which desmin and keratin influence the biomechanical properties of myofibers. This work provides additional insight into the influences of IFs on structure-function relationships in skeletal muscle. It may also have implications for understanding the progression of desminopathies and other IF-related myopathies.</p>","PeriodicalId":15089,"journal":{"name":"Journal of Biomedicine and Biotechnology","volume":" ","pages":"704061"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/704061","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30421330","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Olivier Fisette, Patrick Lagüe, Stéphane Gagné, Sébastien Morin
{"title":"Synergistic applications of MD and NMR for the study of biological systems.","authors":"Olivier Fisette, Patrick Lagüe, Stéphane Gagné, Sébastien Morin","doi":"10.1155/2012/254208","DOIUrl":"https://doi.org/10.1155/2012/254208","url":null,"abstract":"<p><p>Modern biological sciences are becoming more and more multidisciplinary. At the same time, theoretical and computational approaches gain in reliability and their field of application widens. In this short paper, we discuss recent advances in the areas of solution nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics (MD) simulations that were made possible by the combination of both methods, that is, through their synergistic use. We present the main NMR observables and parameters that can be computed from simulations, and how they are used in a variety of complementary applications, including dynamics studies, model-free analysis, force field validation, and structural studies.</p>","PeriodicalId":15089,"journal":{"name":"Journal of Biomedicine and Biotechnology","volume":" ","pages":"254208"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/254208","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30447133","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Steven M Hira, Khaled Aledealat, Kan-Sheng Chen, Mark Field, Gerard J Sullivan, P Bryant Chase, Peng Xiong, Stephan von Molnár, Geoffrey F Strouse
{"title":"Detection of target ssDNA using a microfabricated Hall magnetometer with correlated optical readout.","authors":"Steven M Hira, Khaled Aledealat, Kan-Sheng Chen, Mark Field, Gerard J Sullivan, P Bryant Chase, Peng Xiong, Stephan von Molnár, Geoffrey F Strouse","doi":"10.1155/2012/492730","DOIUrl":"https://doi.org/10.1155/2012/492730","url":null,"abstract":"<p><p>Sensing biological agents at the genomic level, while enhancing the response time for biodetection over commonly used, optics-based techniques such as nucleic acid microarrays or enzyme-linked immunosorbent assays (ELISAs), is an important criterion for new biosensors. Here, we describe the successful detection of a 35-base, single-strand nucleic acid target by Hall-based magnetic transduction as a mimic for pathogenic DNA target detection. The detection platform has low background, large signal amplification following target binding and can discriminate a single, 350 nm superparamagnetic bead labeled with DNA. Detection of the target sequence was demonstrated at 364 pM (<2 target DNA strands per bead) target DNA in the presence of 36 μM nontarget (noncomplementary) DNA (<10 ppm target DNA) using optical microscopy detection on a GaAs Hall mimic. The use of Hall magnetometers as magnetic transduction biosensors holds promise for multiplexing applications that can greatly improve point-of-care (POC) diagnostics and subsequent medical care.</p>","PeriodicalId":15089,"journal":{"name":"Journal of Biomedicine and Biotechnology","volume":" ","pages":"492730"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/492730","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30569907","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Xuan-Yu Meng, Yu Xu, Hong-Xing Zhang, Mihaly Mezei, Meng Cui
{"title":"Predicting protein interactions by Brownian dynamics simulations.","authors":"Xuan-Yu Meng, Yu Xu, Hong-Xing Zhang, Mihaly Mezei, Meng Cui","doi":"10.1155/2012/121034","DOIUrl":"https://doi.org/10.1155/2012/121034","url":null,"abstract":"<p><p>We present a newly adapted Brownian-Dynamics (BD)-based protein docking method for predicting native protein complexes. The approach includes global BD conformational sampling, compact complex selection, and local energy minimization. In order to reduce the computational costs for energy evaluations, a shell-based grid force field was developed to represent the receptor protein and solvation effects. The performance of this BD protein docking approach has been evaluated on a test set of 24 crystal protein complexes. Reproduction of experimental structures in the test set indicates the adequate conformational sampling and accurate scoring of this BD protein docking approach. Furthermore, we have developed an approach to account for the flexibility of proteins, which has been successfully applied to reproduce the experimental complex structure from the structure of two unbounded proteins. These results indicate that this adapted BD protein docking approach can be useful for the prediction of protein-protein interactions.</p>","PeriodicalId":15089,"journal":{"name":"Journal of Biomedicine and Biotechnology","volume":" ","pages":"121034"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/121034","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30571512","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Jaime Corinaldi, Rania Nasrallah, Jordan Clark, Geneviève Paris, Pedro Miura, Bernard J Jasmin, Richard L Hébert
{"title":"Troglitazone induces extracellular matrix and cytoskeleton remodeling in mouse collecting duct cells.","authors":"Jaime Corinaldi, Rania Nasrallah, Jordan Clark, Geneviève Paris, Pedro Miura, Bernard J Jasmin, Richard L Hébert","doi":"10.1155/2012/507057","DOIUrl":"https://doi.org/10.1155/2012/507057","url":null,"abstract":"<p><p>Peroxisome proliferator-activated receptor (PPARγ) has been shown to have a protective role in the nephron through its ability to inhibit a transforming growth factor- (TGF-β) mediated fibrotic response. In contrast, PPARγ was also shown to induce a mesenchymal transformation in epithelial intestinal cells. A fibrotic response in the collecting duct has only recently been established; however, the entire collecting duct has not been fully examined. Inner medullary collecting duct cells (IMCD-K2) and mouse cortical collecting duct cells (M1), representing the cortical and medullary collecting duct, were exposed to 5-10 μM troglitazone for 24 hours. Troglitazone resulted in an elongated morphology, 60% decreases in E-cadherin and β-catenin, a 35% decrease in α-catenin, and a 1.5-fold increase in fibronectin. These effects were not reversed with PPARγ antagonists or affected with PPARγ overexpression. Our results indicate that troglitazone induced a mesenchymal-like transformation in M1 and IMCD-K2 epithelial cells independently of PPARγ.</p>","PeriodicalId":15089,"journal":{"name":"Journal of Biomedicine and Biotechnology","volume":" ","pages":"507057"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/507057","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30571518","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Daniel Roos, Rodrigo Seeger, Robson Puntel, Nilda Vargas Barbosa
{"title":"Role of calcium and mitochondria in MeHg-mediated cytotoxicity.","authors":"Daniel Roos, Rodrigo Seeger, Robson Puntel, Nilda Vargas Barbosa","doi":"10.1155/2012/248764","DOIUrl":"https://doi.org/10.1155/2012/248764","url":null,"abstract":"<p><p>Methylmercury (MeHg) mediated cytotoxicity is associated with loss of intracellular calcium (Ca²⁺) homeostasis. The imbalance in Ca²⁺ physiology is believed to be associated with dysregulation of Ca²⁺ intracellular stores and/or increased permeability of the biomembranes to this ion. In this paper we summarize the contribution of glutamate dyshomeostasis in intracellular Ca²⁺ overload and highlight the mitochondrial dysfunctions induced by MeHg via Ca²⁺ overload. Mitochondrial disturbances elicited by Ca²⁺ may involve several molecular events (i.e., alterations in the activity of the mitochondrial electron transport chain complexes, mitochondrial proton gradient dissipation, mitochondrial permeability transition pore (MPTP) opening, thiol depletion, failure of energy metabolism, reactive oxygen species overproduction) that could culminate in cell death. Here we will focus on the role of oxidative stress in these phenomena. Additionally, possible antioxidant therapies that could be effective in the treatment of MeHg intoxication are briefly discussed.</p>","PeriodicalId":15089,"journal":{"name":"Journal of Biomedicine and Biotechnology","volume":" ","pages":"248764"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/248764","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30863273","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Animal experimental study of the fully biodegradable atrial septal defect (ASD) occluder.","authors":"Yu-feng Zhu, Xin-miao Huang, Jiang Cao, Jian-qiang Hu, Yuan Bai, Hai-bing Jiang, Zhao-feng Li, Ying Chen, Wei Wang, Yong-wen Qin, Xian-xian Zhao","doi":"10.1155/2012/735989","DOIUrl":"https://doi.org/10.1155/2012/735989","url":null,"abstract":"<p><p>This study was conducted to evaluate the feasibility, safety, biocompatibility, and degradation features of a fully biodegradable occluder for closure of atrial septal defect (ASD) in an acute canine model. The ASD was created in 20 healthy mongrel dogs by the brockenbrough needle, and the fully biodegradable occluders were implanted by self-made delivery system. The success rate and complications were observed. Acute ASD models were successfully created in 18 dogs, and 16 occluders were successfully implanted in the ASD models. Animals were sacrificed at different times after procedure. The cardiac gross anatomy showed that all occluders were stable in the interatrial septum, no vegetation or thrombus formation was observed on the surface of all occluders. They were embedded into endogenous host tissue gradually at 12-week follow-up. Different periods of pathological observations suggested that the occluders degraded gradually over about 24 weeks and essentially became an integral part of the septum. Transcatheter closure of ASD in acute canine model using the fully biodegradable ASD occluder has the potential of a high successful rate of technique, excellent biocompatibility, and fewer complications with adequate, immediate, and short-term results.</p>","PeriodicalId":15089,"journal":{"name":"Journal of Biomedicine and Biotechnology","volume":" ","pages":"735989"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/735989","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30998261","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Maria Martha Corvi, Andres Mariano Alonso, Marina Cecilia Caballero
{"title":"Protein palmitoylation and pathogenesis in apicomplexan parasites.","authors":"Maria Martha Corvi, Andres Mariano Alonso, Marina Cecilia Caballero","doi":"10.1155/2012/483969","DOIUrl":"https://doi.org/10.1155/2012/483969","url":null,"abstract":"<p><p>Apicomplexan parasites comprise a broad variety of protozoan parasites, including Toxoplasma gondii, Plasmodium, Eimeria, and Cryptosporidium species. Being intracellular parasites, the success in establishing pathogenesis relies in their ability to infect a host-cell and replicate within it. Protein palmitoylation is known to affect many aspects of cell biology. Furthermore, palmitoylation has recently been shown to affect important processes in T. gondii such as replication, invasion, and gliding. Thus, this paper focuses on the importance of protein palmitoylation in the pathogenesis of apicomplexan parasites.</p>","PeriodicalId":15089,"journal":{"name":"Journal of Biomedicine and Biotechnology","volume":" ","pages":"483969"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/483969","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30998861","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Acanthus ebracteatus Vahl. ethanol extract enhancement of the efficacy of the collagen scaffold in wound closure: a study in a full-thickness-wound mouse model.","authors":"Jutamas Somchaichana, Tanom Bunaprasert, Suthiluk Patumraj","doi":"10.1155/2012/754527","DOIUrl":"https://doi.org/10.1155/2012/754527","url":null,"abstract":"<p><p>Acanthus ebracteatus Vahl. is a Thai herb that is effective in wound healing. We sought to quantitatively determine whether or not the combined application of Acanthus ebracteatus Vahl. and a collagen scaffold will increase wound closure and angiogenesis. Balb/c mice (body weight: 22-25 g) were anesthetized with sodium thiopental. The dorsal skin incision measuring 1.5 × 1.5 cm was made and then deepened using scissors to produce a full-thickness incision down to the level of the panniculus carnosus. The size of the wound was approximately 10% of the total body surface area. The collagen sheet was implanted onto the wound. Animals were divided into 4 major groups as follows: wound with normal saline (W-NSS), wound treated with 0.3 g/kg BW of Acanthus ebracteatus Vahl. extract (W-AE (0.3 g/kg.bw)), wound implanted with collagen scaffold (W-Coll), and wound implanted with collagen scaffold and treated with 0.3 g/kg BW of Acanthus ebracteatus Vahl. (W-Coll-AE combination). On day 14, the W-Coll-AE group showed decreased wound areas and increased capillary vascularity (CV) when compared to the other 3 groups, W-NSS, W-AE0.3, and W-Coll. In the present study, the combination of AE0.3 with collagen showed the best effect on skin angiogenesis and promoted wound closure with less neutrophil infiltration.</p>","PeriodicalId":15089,"journal":{"name":"Journal of Biomedicine and Biotechnology","volume":" ","pages":"754527"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/754527","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31000309","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}