35 research outputs found

    Differential proteomic analysis of the reactivated p53 via Nutlin-3a, in 3 different types of human lymphomas

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    Purpose: The identification and quantification of protein expression levels of nutlin-3A-induced p53 stabilization and activation in human lymphoma. Methods: The Isotope Coded Protein Label (ICPL) technique was followed by nano-Liquid Chromatography coupled on-line with Mass Spectrometry (nLC-MS/MS). Results: Reliable identification & differential quantitative determination of human lymphoma proteome profile, revealing alterations in the HSPs relative expression levels

    Dissecting human lymphoma using an integrated network analysis

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    Lymphomas are cancers that originate in the lymphatic system. Despite the heterogeneity, lymphomas are characterized by the deregulation of the p53-signaling pathway. This study describes a systems-wide network analysis of the key mal-functioning p53-centered network of interactions involved in lymphoma pathogenesis through integration of transcriptomic and proteomic data

    Deciphering the role of autophagy and exosomes in human lymphoma

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    The orchestrated homeostatic action of autophagy and exosome biogenesis provides a potential causal relation with lymphomagenesis. This study aims to characterize the differently expressed proteins associated with both above-mentioned pathways, as well as to explore their potential implication in therapeutic response controlling lymphomagenesis via N3a-induced re-activated p53 in different lymphoma subtypes

    Establishment of computational biology in Greece and Cyprus: Past, present, and future.

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    We review the establishment of computational biology in Greece and Cyprus from its inception to date and issue recommendations for future development. We compare output to other countries of similar geography, economy, and size—based on publication counts recorded in the literature—and predict future growth based on those counts as well as national priority areas. Our analysis may be pertinent to wider national or regional communities with challenges and opportunities emerging from the rapid expansion of the field and related industries. Our recommendations suggest a 2-fold growth margin for the 2 countries, as a realistic expectation for further expansion of the field and the development of a credible roadmap of national priorities, both in terms of research and infrastructure funding

    Mosquitoes cloak their legs to resist insecticides

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    Malaria incidence has halved since the year 2000, with 80% of the reduction attributable to the use of insecticides. However, insecticide resistance is now widespread, is rapidly increasing in spectrum and intensity across Africa, and may be contributing to the increase of malaria incidence in 2018. The role of detoxification enzymes and target site mutations has been documented in the major malaria vector Anopheles gambiae; however, the emergence of striking resistant phenotypes suggests the occurrence of additional mechanisms. By comparing legs, the most relevant insect tissue for insecticide uptake, we show that resistant mosquitoes largely remodel their leg cuticles via enhanced deposition of cuticular proteins and chitin, corroborating a leg-thickening phenotype. Moreover, we show that resistant female mosquitoes seal their leg cuticles with higher total and different relative amounts of cuticular hydrocarbons, compared with susceptible ones. The structural and functional alterations in Anopheles female mosquito legs are associated with a reduced uptake of insecticides, substantially contributing to the resistance phenotype.Fil: Balabanidou, Vasileia. Institute of Molecular Biology And Biotechnology. Foundation For Research And Technology; GreciaFil: Kefi, Mary. University of Crete; Grecia. Institute Of Molecular Biology And Biotechnology, Foundation For Research And Technology; GreciaFil: Aivaliotis, Michalis. Institute Of Molecular Biology And Biotechnology, Foundation For Research And Technology; Grecia. Aristotle University of Thessaloniki; GreciaFil: Koidou, Venetia. Institute Of Molecular Biology And Biotechnology, Foundation For Research And Technology; Grecia. University of Crete; GreciaFil: Girotti, Juan Roberto. Consejo Nacional de Investigaciones CientĂ­ficas y TĂ©cnicas. Centro CientĂ­fico TecnolĂłgico Conicet - La Plata. Instituto de Investigaciones BioquĂ­micas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias MĂ©dicas. Instituto de Investigaciones BioquĂ­micas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Mijailovsky, Sergio Javier. Consejo Nacional de Investigaciones CientĂ­ficas y TĂ©cnicas. Centro CientĂ­fico TecnolĂłgico Conicet - La Plata. Instituto de Investigaciones BioquĂ­micas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias MĂ©dicas. Instituto de Investigaciones BioquĂ­micas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Patricia JuĂĄrez, M.. Consejo Nacional de Investigaciones CientĂ­ficas y TĂ©cnicas. Centro CientĂ­fico TecnolĂłgico Conicet - La Plata. Instituto de Investigaciones BioquĂ­micas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias MĂ©dicas. Instituto de Investigaciones BioquĂ­micas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Papadogiorgaki, Eva. University of Crete; GreciaFil: Chalepakis, George. University of Crete; GreciaFil: Kampouraki, Anastasia. Institute Of Molecular Biology And Biotechnology, Foundation For Research And Technology; Grecia. Agricultural University of Athens; GreciaFil: Nikolaou, Christoforos. Institute Of Molecular Biology And Biotechnology, Foundation For Research And Technology; Grecia. University of Crete; GreciaFil: Ranson, Hilary. Liverpool School of Tropical Medicine; Reino UnidoFil: Vontas, John. Institute Of Molecular Biology And Biotechnology, Foundation For Research And Technology; Grecia. Agricultural University of Athens; Greci

    Ser/Thr/Tyr Protein Phosphorylation in the Archaeon Halobacterium salinarum—A Representative of the Third Domain of Life

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    In the quest for the origin and evolution of protein phosphorylation, the major regulatory post-translational modification in eukaryotes, the members of archaea, the “third domain of life”, play a protagonistic role. A plethora of studies have demonstrated that archaeal proteins are subject to post-translational modification by covalent phosphorylation, but little is known concerning the identities of the proteins affected, the impact on their functionality, the physiological roles of archaeal protein phosphorylation/dephosphorylation, and the protein kinases/phosphatases involved. These limited studies led to the initial hypothesis that archaea, similarly to other prokaryotes, use mainly histidine/aspartate phosphorylation, in their two-component systems representing a paradigm of prokaryotic signal transduction, while eukaryotes mostly use Ser/Thr/Tyr phosphorylation for creating highly sophisticated regulatory networks. In antithesis to the above hypothesis, several studies showed that Ser/Thr/Tyr phosphorylation is also common in the bacterial cell, and here we present the first genome-wide phosphoproteomic analysis of the model organism of archaea, Halobacterium salinarum, proving the existence/conservation of Ser/Thr/Tyr phosphorylation in the “third domain” of life, allowing a better understanding of the origin and evolution of the so-called “Nature's premier” mechanism for regulating the functional properties of proteins

    Membrane proteome of the green sulfur bacterium Chlorobium tepidum (syn. Chlorobaculum tepidum) analyzed by gel-based and gel-free methods

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    Chlorobium tepidum is a Gram-negative bacterium of the green sulfur phylum (Chlorobia). Chlorobia are obligate anaerobic photolithoautotrophs that are widely distributed in aquatic environments where anoxic layers containing reduced sulfur compounds are exposed to light. The envelope of C. tepidum is a complex organelle composed of the outer membrane, the periplasm-peptidoglycan layer, and the cytoplasmic membrane. In addition to the outer and plasma membranes, C. tepidum contains chlorosomes attached to the cytoplasmic side of the plasma membrane. Each cellular compartment has a unique set of proteins, called sub-proteome. An important aim of proteome analysis is to study the level of the expressed genes and their response to environmental changes. Membrane protein studies are of primary importance to understand how nutrients are transported inside the cell, how toxic molecules are exported, and the mechanisms of photosynthesis and energy metabolism

    Subtyping on Live Lymphoma Cell Lines by Raman Spectroscopy

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    Raman spectroscopy is a well-defined spectroscopic technique sensitive to the molecular vibrations of materials, since it provides fingerprint-like information regarding the molecular structure of the analyzed samples. It has been extensively used for non-destructive and label-free cell characterization, particularly in the qualitative and quantitative estimation of amino acids, lipids, nucleic acids, and carbohydrates. Lymphoma cell classification is a crucial task for accurate and prompt lymphoma diagnosis, prognosis, and treatment. Currently, it is mostly based on limited information and requires costly and time-consuming approaches. In this work, we are proposing a fast characterization and differentiation methodology of lymphoma cell subtypes based on Raman spectroscopy. The study was performed in the temperature range of 15–37 °C to identify the best cell measurement conditions. The proposed methodology is fast, accurate, and requires minimal sample preparation, resulting in a potentially promising, non-invasive strategy for early and accurate cell lymphoma characterization

    The protein interaction network of a taxis signal transduction system in a halophilic archaeon

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    BACKGROUND: The taxis signaling system of the extreme halophilic archaeon Halobacterium (Hbt.) salinarum differs in several aspects from its model bacterial counterparts Escherichia coli and Bacillus subtilis. We studied the protein interactions in the Hbt. salinarum taxis signaling system to gain an understanding of its structure, to gain knowledge about its known components and to search for new members. RESULTS: The interaction analysis revealed that the core signaling proteins are involved in different protein complexes and our data provide evidence for dynamic interchanges between them. Fifteen of the eighteen taxis receptors (halobacterial transducers, Htrs) can be assigned to four different groups depending on their interactions with the core signaling proteins. Only one of these groups, which contains six of the eight Htrs with known signals, shows the composition expected for signaling complexes (receptor, kinase CheA, adaptor CheW, response regulator CheY). From the two Hbt. salinarum CheW proteins, only CheW1 is engaged in signaling complexes with Htrs and CheA, whereas CheW2 interacts with Htrs but not with CheA. CheY connects the core signaling structure to a subnetwork consisting of the two CheF proteins (which build a link to the flagellar apparatus), CheD (the hub of the subnetwork), two CheC complexes and the receptor methylesterase CheB. CONCLUSIONS: Based on our findings, we propose two hypotheses. First, Hbt. salinarum might have the capability to dynamically adjust the impact of certain Htrs or Htr clusters depending on its current needs or environmental conditions. Secondly, we propose a hypothetical feedback loop from the response regulator to Htr methylation made from the CheC proteins, CheD and CheB, which might contribute to adaptation analogous to the CheC/CheD system of B. subtilis
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