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Search Results: 1 - 10 of 369 matches for " phosphorylation "
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Myristoylated Alanine-Rich C Kinase Substrate Accelerates TNF-α-Induced Apoptosis in SH-SY5Y Cells in a Caspases-6 and/or -7-Dependent Manner  [PDF]
Atsuhiro Tanabe, Mitsuya Shiraishi, Yasuharu Sasaki
Advances in Bioscience and Biotechnology (ABB) , 2015, DOI: 10.4236/abb.2015.68060
Abstract: Cell proliferation, differentiation, and the elimination of unnecessary cells by apoptosis occur in the development of the nervous system. It is reported that brain dysplasia appears as the results of myristoylated alanine-rich C kinase substrate (MARCKS) knockout or the mutant mouse. We therefore expect that MARCKS participates in the development of the nervous system. However, the mechanism underlying such participation has not been identified. In this study, we observed the effects of the overexpression of MARCKS or unphosphorylatable MARCKS on cell proliferation and TNF-α-induced apoptosis in neuroblastoma SH-SY5Y cells. Furthermore, we restrained MARCKS expression by the RNAi method. In the results, MARCKS-overexpressing cells and not unphosphorylatable MARCKS-overexpressing cells showed increased cell proliferation rates. On the other hand, the RNAi decreased the proliferation of MARCKS-knocked down SH-SY5Y cells. These results indicated that MARCKS-overexpressing cells were more sensitive to TNF-α than normal SH-SY5Y cells. Moreover, in MARCKS-overexpressing cells TNF-α-induced apoptosis was inhibited by caspase-6 and -7 inhibitors but not by caspase-3 inhibitor. These results suggested that MARCKS participated in TNF-α-induced apoptosis in a caspase-6 and/or -7-dependent manner.
Influence of thiol stress on oxidative phosphorylation and generation of ROS in Streptomyces coelicolor  [PDF]
Hemendra J. Vekaria, Ratna Prabha Chivukula
Journal of Biophysical Chemistry (JBPC) , 2010, DOI: 10.4236/jbpc.2010.13020
Abstract: Thiols play very important role in the intracellular redox homeostasis. Imbalance in the redox status leads to changes in the intracellular metabolism including respiration. Thiol stress, a reductive type of stress can also cause redox imbalance. When Gram-positive bacterium Strep- tomyces coelicolor was exposed to thiol stress, catalaseA was induced. Induction of catalaseA is the consequence of elevation of ROS (reactive oxygen species). The two major sources of reactive oxygen species are Fenton reaction and slippage of electrons from electron transport chain during respiration. Hence, the effect of thiol stress was checked on the rate of oxidative phosphorylation in S. coelicolor. We found correlation in the increase of oxidative phosphorylation rate and the generation of ROS, subsequently leading to induction of catalase. It was observed that thiol stress does not affect the functionality of the individual complexes of the ETC, but still there was an increase in the overall respiration, which may lead to generation of more ROS leading to induction of catalase.
Protein phosphorylation pathways disruption by pesticides  [PDF]
Gladis Magnarelli, Teresa Fonovich
Advances in Biological Chemistry (ABC) , 2013, DOI: 10.4236/abc.2013.35050
Abstract: Phosphosites in the human proteome represent an excellent source of potential biomarkers of pesticide toxicity. In fact, experimental animal models as well as in vitro studies have revealed phosphorylation disruption associated to metabolic regulation, hormone signaling, neuronal function and differentiation, cell survival and death. Due to their estrogen-mimicking ability, pesticides are considered as prime etiological suspects of increasing tumor incidence. Evidences of alterations in the signal transduction pathways involved in the tumor progression stage of pesticides were also provided. Despite progress in understanding the effect of pesticides on the human phosphorproteome and their health outcomes, it remains a complex issue to be studied. By now, the potential impact of pesticides in epigenetic phosphorylation pathways remains poorly explored. In addition, studies involving pesticides mixtures effects are needed. This review updates and provides a comprehensive discussion on the molecular and biochemical events underlying protein phosphorylation pathway disruption caused by pesticides most frequently detected in human tissues and fluids, such as organochlorine pesticides and organophosphates. The link between epidemiological studies and experimental approaches is also considered. Future challenges, such as micro-array phosphoproteome studies to complement gene expression arrays to understand the mechanisms involved in pesticide toxicology are briefly discussed.
Tyrosine phosphorylation of monocyte-derived macrophage proteins in buffalo (Bubalus bubalis): A potential phenotype of natural resistance  [PDF]
Maria Miarelli, Federica Signorelli, Giovanna de Matteis
Open Journal of Animal Sciences (OJAS) , 2013, DOI: 10.4236/ojas.2013.32019
Abstract:

The aim of this work was to explore the possibility of using the presence of tyrosine-phosphorylated macrophage proteins as a phenotype of natural resistance. Tyrosine-phosphorylation of macrophage proteins was investigated in 18 buffaloes, that carried either the resistant, or the non-resistant, Natural Resistance-Associated Macrophage Protein one (NRAMP1) genotype, that various authors have associated with susceptibility to intracellular bacterial diseases. Monocyte-derived macrophages were Interferon-gamma (IFN-γ) stimulated and tyrosine-phosphorylation was assessed by Western blotting. Evidence of phosphorylation after IFN-γ stimulation was shown by 75% of the buffaloes carriers of the resistant genotype, and by 20% of the carriers of the non-resistant genotype (Chisquare value between the groups = 5.44; P = 0.02). The study of the Proteoma of monocyte-derived macrophages might open the way to the genetic control of disease resistance.

Improved Protein Phosphorylation Site Prediction by a New Combination of Feature Set and Feature Selection  [PDF]
Favorisen Rosyking Lumbanraja, Ngoc Giang Nguyen, Dau Phan, Mohammad Reza Faisal, Bahriddin Abapihi, Bedy Purnama, Mera Kartika Delimayanti, Mamoru Kubo, Kenji Satou
Journal of Biomedical Science and Engineering (JBiSE) , 2018, DOI: 10.4236/jbise.2018.116013
Abstract: Phosphorylation of protein is an important post-translational modification that enables activation of various enzymes and receptors included in signaling pathways. To reduce the cost of identifying phosphorylation site by laborious experiments, computational prediction of it has been actively studied. In this study, by adopting a new set of features and applying feature selection by Random Forest with grid search before training by Support Vector Machine, our method achieved better or comparable performance of phosphorylation site prediction for two different data sets.
Modifica??o química e física do amido de quirera de arroz para aproveitamento na indústria de alimentos
Limberger, Valéria Maria;Silva, Leila Picolli da;Emanuelli, Tatiana;Comarela, Carine Gláucia;Patias, Luciana Dalpieve;
Química Nova , 2008, DOI: 10.1590/S0100-40422008000100018
Abstract: the study evaluated the efficiency of chemical (phosphorylation) and physical (extrusion) modifications of the starch of broken rice. results demonstrated a reduction in the moisture content of extruded and phosphorylated broken rice and an increase in the ash content of phosphorylated broken rice. both phosphorylation and extrusion increased cold water binding capacity, swelling power, and solubility. extruded and phosphorylated pastes were stable under refrigeration, but only extruded paste was stable when submitted to freezing. phosphorylated paste had the lowest viscosity and the highest stability during heating, while the extruded one gelatinized without heating, but had higher losses during heating.
Epidermal Growth Factor Stimulates Extracellular-Signal Regulated Kinase Phosphorylation of a Novel Site on Cytoplasmic Dynein Intermediate Chain 2
Ashok K. Pullikuth,Aysun Ozdemir,Daviel Cardenas,Evangeline Bailey,Nicholas E. Sherman,K. Kevin Pfister,Andrew D. Catling
International Journal of Molecular Sciences , 2013, DOI: 10.3390/ijms14023595
Abstract: Extracellular-signal regulated kinase (ERK) signaling is required for a multitude of physiological and patho-physiological processes. However, the identities of the proteins that ERK phosphorylates to elicit these responses are incompletely known. Using an affinity purification methodology of general utility, here we identify cytoplasmic dynein intermediate chain 2 (DYNC1I-2, IC-2) as a novel substrate for ERK following epidermal growth factor receptor stimulation of fibroblasts. IC-2 is a subunit of cytoplasmic dynein, a minus-end directed motor protein necessary for transport of diverse cargos along microtubules. Emerging data support the hypothesis that post-translational modification regulates dynein but the signaling mechanisms used are currently unknown. We find that ERK phosphorylates IC-2 on a novel, highly conserved Serine residue proximal to the binding site for the p150 Glued subunit of the cargo adapter dynactin. Surprisingly, neither constitutive phosphorylation nor a phosphomimetic substitution of this Serine influences binding of p150 Glued to IC-2. These data suggest that ERK phosphorylation of IC-2 regulates dynein function through mechanisms other than its interaction with dynactin.
Protein phosphorylation pattern in the immune cells of leprosy affected individuals
Karuna Devi Sagili,1 Renuka Raju,1 Venkat Rami Reddy,2 Anandaraj M.P.J.S,1 Sujai Suneetha,3 Lavanya Moses Suneetha.3
Journal of Infection in Developing Countries , 2008,
Abstract: Background: Leprosy is an infectious disease in which the susceptibility to the pathogen Mycobacterium leprae and the clinical manifestations are attributed to host immune cell response. Receptor mediated events and signalling in the immune cells are mediated by protein phosphorylation. The main signalling pathways and protein kinases known to be involved in the regulation of immune cells are cAMP dependent kinases, calcium/calmodulin dependent kinases, protein kinase C and mitogen activatedprotein kinases. The cumulative consequence of alterations in signalling pathways can be evaluated by intrinsic cellular protein phosphorylation by -P32 ATP. The present study was designed to assess the protein phosphorylation in the immune cells of leprosy patients as compared with normal individuals.Methodology: Lymphocyte protein phosphorylation was conducted in 15 leprosy patients and 9 normal individuals. Protein phosphorylation of lymphocytes was carried out in the presence/absence of protein kinase modulators. The phosphorylation patterns were documented and analysed consequent to SDS-PAGE, staining, destaining, drying and autoradiography.Results: The major phosphorylated proteins in lymphocytes were of molecular weights 20-22, 24-29, 30-35, 43, 46-50 and 66- 68 kDa. In general, the major phosphorylated proteins were similar in the controls and in the patients. The phosphorylatability of these proteins varied with different modulators. Variations in the phosphorylation pattern were observed in 25% of the leprosy patients where there was a decrease of the 66kDa protein and a decrease of 20-22kDa protein phosphorylation.Conclusion: The observed alterations in the protein phosphorylation pattern could be due to alteration in kinases and/or their substrates or due to the effect of M. leprae on immune cells.
PHOSPHORYLATION/DEPHOSPHORYLATION OF MITOCHONDRIAL PROTEINS IN REDOX-SIGNALLING OF HIGHER PLANTS UNDER ABIOTIC STRESS CONDITIONS
Subota I.Yu.,A.Sh. Arziev,A.I. Katyshev,M.V. Koulintchenko
Journal of Stress Physiology & Biochemistry , 2012,
Abstract: We studied an impact of the widely spread intra-cellular signals Ca2+ and сAMP on activity of the protein phosphorylation in maize mitochondria. The use of the isolated mitochondria is a convenient model system for investigation of the different physiological processes, for example for simulation of the different stress conditions. The treatment of maize mitochondria with high concentration of calcium ions which mimics the initial stage of apoptosis led to an increase of the phosphorylation level of some proteins and to an additional phosphorylation of the 59 and 66 kDa proteins. The treatment of the mitoplasts, i.e., the mitochondria devoid of the outer membrane with calcium ions insignificantly induced the activity of protein phosphorylation. It is assumed that the outer membrane is essential for Ca2+ signal transduction to plant mitochondria. We also identified a 94 kDa protein involved in phosphorylation of the mitochondrial proteins. This protein might be a single-subunit protein kinase or one of the subunits of the protein kinase complex. Antimycin A and KCN which are the inhibitors of mitochondria respiration increased the phosphorylation activity of the mitochondrial polypeptides. The effect of this inhibitors was similar both in in organello system and at the level of the whole plant. It should be noticed that at the level of the whole plant the effect of KCN on activity of the mitochondrial protein phosphorylation was more essential. Some considerable differences were found both at the level of protein phosphorylation and in electrophoresis patterns representing the intact mitochondria, the mitoplasts and the outer membrane fraction. The activity of protein phosphorylation in mitoplasts and the outer membrane fraction was extremely high compared to the phosphorylation activity of the mitochondrial proteins. This could be explained by the higher level of “substrate phosphoprotein phosphatase” in the outer membrane of mitochondria. This phosphoprotein phosphatase primarily dephosphorylates the protein of the inner membrane. When the proteins of the outer membrane were added together with the phosphorylated mitoplast proteins, the activity of phosphorylation effectively decreased. Thus, the phosphoprotein phosphatases of the outer membrane could dephosphorylate the inner membrane proteins and vice versa, the inner membrane phosphatases dephosphorylate the outer membrane proteins. Mn-SOD is the first line protection enzyme of the mitochondrial DNA, as this enzyme scavenges superoxide anion and severely reduces the toxic influences of ROS. Till now
Characterization of the role of Smu1 in nuclear localization of splicing factors in the mammalian temperature-sensitive mutant  [PDF]
Kimihiko Sugaya, Yoshie Ishihara, Keiko Sugaya, Sonoe Inoue
American Journal of Molecular Biology (AJMB) , 2013, DOI: 10.4236/ajmb.2013.31005
Abstract: A temperature-sensitive (ts) mutant of the CHO-K1 cell line, tsTM18, grows at 340C but not at 390C. Smu1 is the gene responsible for ts defects of tsTM18 cells. Previously, we found that the Smu1 ts defect altered the localization (as indicated by enlargement of speckles) of SRSF1 (SF2/ASF) in tsTM18 cells cultured at 390C, suggesting a functional association between Smu1 and SRSF1. Speckles are subnuclear structures that may function as storage/assembly/ modification compartments to supply splicing factors to active transcription sites. The effect of the ts defect of Smu1 on the localization of other factors related to splicing has not been characterized yet. The mechanisms underlying the enlargement of speckles of SRSF1 remain unclear. In the present study, we found that the ts defect of Smu1 affected the nuclear localization of a splicing factor, SRSF2 (SC35), and factors involved in the exon-exon junction complex, Y14 and ALY. Reverse transcription-polymerase chain reaction (RT-PCR) analysis revealed that the ts defect of Smu1 affected alternative splicing of endogenous Clk1/ Sty and SRSF2 genes. Mammalian Clk family
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