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Shirin Hasan Nayeem Bilal Shoa Naqvi Ghulam Md Ashraf Nida Suhail Sadhana Sharma Naheed Banu 《Biological trace element research》2011,142(3):589-597
Brain is a target of stress along with the immune, metabolic, and cardiovascular systems of the body. In the present work,
the preventive roles of a multivitamin–mineral supplement and vitamins (E + C) in chronic unpredictable stress (CUS)-induced
oxidative damage were studied in the brain and heart of Swiss albino mice. Thirty-two mice were randomized to one of the following
groups: control + vehicle, CUS + vehicle, CUS + multivitamin–mineral, and CUS + vitamins (E + C). CUS was applied for 4 weeks,
and multivitamin–mineral and vitamins (E + C) were administered orally for the same period. CUS led to a negative impact on
all the biochemical parameters analyzed. Elevation in malondialdehyde and reduction in glutathione levels were found. The
activities of superoxide dismutase, catalase, glutathione S-transferase, and glutathione reductase were decreased. Treatment with multivitamin–mineral and vitamins (E + C) brought these
parameters to near normal levels. Multivitamin–mineral was found more restitutive than combined vitamins (E + C) doses. The
present study hypothesizes that supplementation with a multivitamin–mineral may prove more effective than vitamin treatment
alone in the alleviation of oxidative damage in brain and heart during periods of chronic stress. 相似文献
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Fleming K Kelley LA Islam SA MacCallum RM Muller A Pazos F Sternberg MJ 《Philosophical transactions of the Royal Society of London. Series B, Biological sciences》2006,361(1467):441-451
This paper reports two studies to model the inter-relationships between protein sequence, structure and function. First, an automated pipeline to provide a structural annotation of proteomes in the major genomes is described. The results are stored in a database at Imperial College, London (3D-GENOMICS) that can be accessed at www.sbg.bio.ic.ac.uk. Analysis of the assignments to structural superfamilies provides evolutionary insights. 3D-GENOMICS is being integrated with related proteome annotation data at University College London and the European Bioinformatics Institute in a project known as e-protein (http://www.e-protein.org/). The second topic is motivated by the developments in structural genomics projects in which the structure of a protein is determined prior to knowledge of its function. We have developed a new approach PHUNCTIONER that uses the gene ontology (GO) classification to supervise the extraction of the sequence signal responsible for protein function from a structure-based sequence alignment. Using GO we can obtain profiles for a range of specificities described in the ontology. In the region of low sequence similarity (around 15%), our method is more accurate than assignment from the closest structural homologue. The method is also able to identify the specific residues associated with the function of the protein family. 相似文献
77.
Walls KC Coskun P Gallegos-Perez JL Zadourian N Freude K Rasool S Blurton-Jones M Green KN Laferla FM 《The Journal of biological chemistry》2012,287(36):30317-30327
Alzheimer disease (AD) is a complex disorder that involves numerous cellular and subcellular alterations including impairments in mitochondrial homeostasis. To better understand the role of mitochondrial dysfunction in the pathogenesis of AD, we analyzed brains from clinically well-characterized human subjects and from the 3xTg-AD mouse model of AD. We find Aβ and critical components of the γ-secretase complex, presenilin-1, -2, and nicastrin, accumulate in the mitochondria. We used a proteomics approach to identify binding partners and show that heat shock protein 60 (HSP60), a molecular chaperone localized to mitochondria and the plasma membrane, specifically associates with APP. We next generated stable neural cell lines expressing human wild-type or Swedish APP, and provide corroborating in vitro evidence that HSP60 mediates translocation of APP to the mitochondria. Viral-mediated shRNA knockdown of HSP60 attenuates APP and Aβ mislocalization to the mitochondria. Our findings identify a novel interaction between APP and HSP60, which accounts for its translocation to the mitochondria. 相似文献
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Oncofetal splice-pattern of the human H19 gene 总被引:1,自引:0,他引:1
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Construction of a modified vector for efficient purification of recombinant Mycobacterium tuberculosis proteins expressed in Escherichia coli 总被引:5,自引:0,他引:5
A major problem in assessing the vaccine and diagnostic potential of various proteins encoded by Mycobacterium tuberculosis genome is the inability to produce large quantities of these proteins, even when Escherichia coli or other heterologous systems are employed for recombinant protein production. To overcome these barriers, we have constructed a modified expression vector, using pGEX-4T-1 vector as the backbone. In addition to the features offered by the pGEX-4T vectors, the new vector allowed easy purification of recombinant proteins on the highly versatile Ni-NTA-agarose affinity matrix. The utility of the new vector was demonstrated by expressing and purifying, to near homogeneity, two M. tuberculosis proteins, i.e., Rv3872 (a member of the multi-gene PE subfamily) and Rv3873 (a member of the multi-gene PPE subfamily), which are encoded by the RD1 region of M. tuberculosis. The proteins encoded by rv3872 and rv3873 were expressed at high levels as fusion proteins with glutathione-S-transferase in E. coli. The recombinant Rv3872 and Rv3873 proteins were purified and isolated free of the fusion partner (GST) by affinity purification on glutathione-Sepharose and/or Ni-NTA-agarose affinity matrix and cleavage of the purified fusion proteins by thrombin protease. The recombinant Rv3872 protein was nearly homogeneous (more than 95% pure) while Rv3873 preparation was more than 90% pure. The recombinant Rv3872 and Rv3873 proteins were immunologically active and reacted with antibodies in sera from TB patients. Our results demonstrate the utility of the newly constructed expression vector with two affinity tags for efficient expression and purification of recombinant M. tuberculosis proteins expressed in E. coli, which could be used for further diagnostic and immunological studies. 相似文献