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Search Results: 1 - 10 of 595 matches for " proteomics "
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Seyed Hassan Moghaddamnia
Journal of Paramedical Sciences , 2010,
Proteomic Profile Modification of Anaplastic Medulloblastoma after in-Vivo Radiotherapy: A Case Study  [PDF]
C. Zanini, D. Baci, G. Mandili, M. Leone, I. Morra, M. Forni
Journal of Cancer Therapy (JCT) , 2010, DOI: 10.4236/jct.2010.12017
Abstract: Medulloblastoma (MDB) is an aggressive tumor of Central Nervous System (CNS). Radiotherapy after radical surgery has an important role in treatment of standard and high risk patients and is followed by intensive chemotherapy. To explore modifications of protein expression induced by in vivo radiotherapy proteomic analysis was performed on a case of Anaplastic MDB. 2D-gel electrophoresis and MALDI-TOF mass spectrometry detected qualitative differences of protein expression in Anaplastic MDB at diagnosis and in relapse after radiotherapy. Relevant proteomic data were confirmed by western blot and Real-Time PCR analysis, validating the presence of Sthatmin 1 (STMN1), Heat shock protein 60 (HSP60), HSP27 and Disulfide Isomerase (ER60) among the six proteins present in both samples. The most relevant modification induced by radiotherapy was a drastic reduction of the total number of proteins (60.6%) and the appearance of few new proteins. The modifications and the striking simplification of proteins expressed by the tumor after radiotherapy may allow to tailor subsequent chemotherapy on a rational basis. A proteomic guided chemotherapy may be of great benefit to patients.
Proteomic progress in studying tuberculosis from 2010 to 2011  [PDF]
Lijun Zhang, Douglas Lowrie, Honghao Zhou
Journal of Biophysical Chemistry (JBPC) , 2011, DOI: 10.4236/jbpc.2011.24045
Abstract: It is well accepted that rapid and early detection of Mycobacterium tuberculosis infection and understanding the mechanism of microbiologyhost interaction. Herein, we review the recently published papers related to TB proteomics from 2010 to 2011, including new technologies used in TB proteome research, diagnosis biomarkers of TB-associated diseases, disease pathogenesis and antigens for drug development. Through this review, we wish to offer some help for TB diagnosis and treatment.
Characterization of Angiotensin-Converting Enzyme before and after Cryopreservation of Gir Semen  [PDF]
Fernando H. G. Furtado, Fábio J. C. Faria, Elisvania F. Santos, Ricardo G. Almeida, Deiler S. Costa
Agricultural Sciences (AS) , 2019, DOI: 10.4236/as.2019.105049
Abstract: The aim of this study was to characterize the angiotensin-converting enzyme (ACE) in Gir semen before and after cryopreservation. The ejaculate of five sexually mature bulls was used. After collection, one 1-mL aliquot of fresh semen was analyzed immediately, and the rest of the semen was cryopreserved in liquid nitrogen for subsequent analysis. Freshly collected semen and thawed cryopreserved semen were centrifuged twice with Tyrode’s albumin lactate pyruvate medium (TALP) to remove plasma and extender, respectively. Samples were then subjected to western blotting, immunocytochemistry, and enzymatic activity techniques. At least one 100 kDa band was observed in every bull analyzed using western blotting with an anti-ACE monoclonal antibody, and band intensity decreased by 70% (p < 0.05) after cryopreservation. Immunocytochemistry showed periacrosomal ACE localization, and the area stained by the fluorescent antibody significantly decreased (p < 0.05) after cryopreservation. Enzyme activity was evaluated using FAPGG substrate hydrolysis, which was significantly lower (p < 0.05) in cryopreserved semen than in fresh semen. Therefore, the process of cryopreservation decreases ACE band intensity and enzyme activity in Gir bull semen, and reduces the stained area in immunocytochemistry.
An in vitro infection model system to study proteins expressed during interaction of mycobacterium with murine macrophages  [PDF]
Neelja Singhal, Prashant Sharma, Bhavnesh Kumar, Utpal Sengupta, Krishnamurthy Venkatesan, Deepa Bisht
Advances in Bioscience and Biotechnology (ABB) , 2010, DOI: 10.4236/abb.2010.13025
Abstract: Resurgence of mycobacterial diseases particularly tuberculosis has caused a renewed interest to unravel the strategies employed by mycobacteria for intracellular survival. In spite of advancement in mycobacterial research, our knowledge about genes and their corresponding functional proteins involved during the interaction of mycobacterium with host’s macrophages is fragmentary. This study pertains to development of a suitable in vitro model using murine macrophages and Mycobacterium bovis BCG to study proteins expressed during macrophage-myco bacterium interactions. Peritoneal macrophages from BALB/c mice were infected with M. bovis BCG and intracellular replication was assessed by {3H} thymi- dine uptake assay which was maximal when macrophage to mycobacterium ratio was 1:10. SDS-PAGE was employed to study the proteins expressed and selected proteins were subjected to mass spectrometry. Seven proteins found to be upregulated during macrophage-mycobacterium interaction were identified by MALDI-TOF. The results indicate that the present in vitro infection model was able to support the growth of M. bovis BCG in murine macrophages and is an ideal model to determine the pattern of functions of gene expression during the interaction of mycobacterium with macrophages. The differentially expressed proteins will help in understanding the mycobacterial molecular basis of adaptation to intracellular macrophage environment.
Characterization of proteins in cryopreserved and non-cryopreserved seminal plasma of dairy bulls of dif-fering fertility  [PDF]
JF Odhiambo, RA Dailey
Open Journal of Animal Sciences (OJAS) , 2011, DOI: 10.4236/ojas.2011.12005
Abstract: Seminal plasma is composed of secretions from accessory sex glands, which are mixed with sperm at ejaculation and contribute the majority of semen volume. Seminal plasma is considered a transport and support medium for sperm in the female reproductive tract. Because seminal plasma is not required for fertilization, the importance of its constituents to the establishment of normal pregnancy has been overlooked. Four seminal plasma proteins, Osteopontin, Sper-madhesin Z13, BSP 30 kDa and Phospholipase A2, have been identified as markers of fertility in dairy bulls (Cancel et al., 1997; Moura et al., 2006, 2007). The objective of the present study was to characterize the expression patterns of these proteins and other proteins found to be of interest in seminal plasma of cryopreserved and non-cryopreserved bull semen. Seminal plasma samples were obtained from 16 mature Hol-stein-Friesian bulls at Select Sires Inc. Samples were divided into two groups based on assigned fertility score expressed as the percentage point deviation (PD) of the bull’s non-return rate (NRR) from the average NRR of all bulls in the Select Sires Inc. reproductive management program. Group 1 (high fertility bulls, n = 8) 1.9 ≤ PD ≤ 2.7%, and group 2 (low fertility bulls, n = 8) -6.5 ≤ PD ≤ 1.8 %. Additionally, the samples were categorized as processed (cryopreserved) or unprocessed (non-cryopreserved) for protein analysis. Protein expression was analyzed by 2-D fluorescence difference gel electrophoresis (2D-DIGETM). Protein spots were picked from a reference gel, analyzed by mass spectrometry and, subsequently identified by MS/MS ion searches performed on the SwissProt database. Protein expression did not differ (P > 0.05) with fertility grouping but displayed two distinct patterns among the processing groups: majority of the functional proteins were highly expressed in seminal plasma of non-cryopreserved semen while the cryopreserved semen contained mainly structural/extender derived proteins. Functional proteins identified included Spermadhesin Z13, BSP A1/2, BSP 30 kDa, Nucleobindin-1 and metalloproteinase inhibitor 2. Some of these proteins have been identified as anti-fertility or fertility enhancing agents in males. Whether this alteration in protein expression after processing might affect semen fertility is worthy of further evaluation.
Proteomics and Its Applications in Diagnosis of Auto Immune Diseases  [PDF]
Gebrehiwot Gebretsadik, M. K. C. Menon
Open Journal of Immunology (OJI) , 2016, DOI: 10.4236/oji.2016.61003
Abstract: Although the proteomics and its applications in detecting autoimmune diseases are a prominently discussed issue, this review will focus particularly some prominent aspects regarding clinical utility of these techniques in prognosis, diagnosis, and treatment of these diseases. The impact of immunofluorescent techniques, enzyme immunoassays and use of proteomics biomarkers in the characterization of the auto immune diseases is briefly discussed. The necessity of adopting existing technologies of protein chemistry, predisposition testing, targeted monitoring and prevention of diseases through nutrition coupled with lifestyle changes will be focused as modern diagnostic tools in realizing the changeover from isolated medicine to personalized medicine. Use of biological fluids, in order to identify low abundance proteins as biomarkers in detecting autoimmune diseases is attempted in the study of serum/plasma proteomics.
Global Proteomics of the Extremophile Black Fungus Cryomyces antarcticus Using 2D-Electrophoresis  [PDF]
Kristina Zakharova, Katja Sterflinger, Ebrahim Razzazi-Fazeli, Katharina Noebauer, Gorji Marzban
Natural Science (NS) , 2014, DOI: 10.4236/ns.2014.612090

The microcolonial black fungus Cryomyces antarcticus is an extremophile organism growing on and in rock in the Antarctic desert. Ecological plasticity and stress tolerance make it a perfect model organism for astrobiology. 2D-gel electrophoresis and MALDI-TOF/TOF mass spectrometry were performed to explore the protein repertoire, which allows the fungus to survive in the harsh environment. Only a limited number of proteins could be identified by using sequence homologies in public databases. Due to the rather low identification rate by sequence homology, this study reveals that a major part of the proteome of C. antarcticus varies significantly from other fungal species.

Molecular Weight Determination of a Protease Extracted from Mucor pusillus: Comparison Methods  [PDF]
Nouani Abdelouahab, Belhamiche Nabila, Slamani Roza, Belbraouet Slimane, Dako Etienne, Audet Pascal, Bellal Mohand Mouloud
Food and Nutrition Sciences (FNS) , 2015, DOI: 10.4236/fns.2015.63035
Abstract: Mucor pepsin, a protease used in milk coagulation, is purified by ion-exchange and by molecular exclusion on Sephadex G100. The molecular weight (MW) is determined by polyacrylamide gel electrophoresis under denaturing conditions in presence of sodium dodecyl sulfate (SDS) and by molecular exclusion chromatography. Approximate evaluation of molecular mass was conducted by elution of known MW proteins (BSA: 67 kDa, pepsin: 35 kDa and trypsin: 23.8 kDa) on Sephadex G-100 under the same conditions as the experimental sample. The electrophoretic profile shows that the active fraction studied appears as a single homogeneous band (monomeric form). According to the curve calibration, the molecular mass of the coagulant fraction is about 48 kDa. For Mucor, the observed MW value seems to be enigmatic. However, this result is confirmed by a proteomic analysis with close MW values obtained using conventional techniques. The protease studied by the Scafold ver. Software 2.0 and the analysis of the protein similarities indicate a MW of 46 kDa and the protease sequence of 427 amino acids.
Prognostic and Predictive Protein Biomarkers in Laryngeal Squamous Cell Carcinoma—A Systematic Review  [PDF]
Matthew M. Kwok, Paul Goodyear
International Journal of Otolaryngology and Head & Neck Surgery (IJOHNS) , 2015, DOI: 10.4236/ijohns.2015.43031
Abstract: Background: Despite recent advances in clinical management of laryngeal squamous cell carcinoma (LSCC), the overall 5-year survival continues to be poor. Consequently, biomarkers of treatment response will need to be identified. Proteomic strategies are one way to attempt to identify such biomarkers. Methods: The Medline, Embase and Cochrane Library databases were systematically searched until 1st March 2014 using the terms “larynx”, “squamous cell carcinoma”, “proteomic”, and “biomarker”. Articles which met inclusion criteria were assessed for the type of biomarker investigated, the proteomic technique used, and whether any validation had been performed. Results: Six studies identified biomarkers, including UCRP, ceramides, uPA, MT1-MMP, stratifin, transferrin, albumin, S100 calcium-binding protein A9, stathmin, enolase, PLAU, IGFBP7, MMP14, THBS1, and transthyretin. Transferrin was the only biomarker to appear in more than one study. Conclusions: Our review identified several potential biomarkers of outcome in LSCC. Well designed studies will need to further validate their use in the future.
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