23 results on '"Nadezhda V. Popova"'
Search Results
2. The Functional Role of Extracellular Matrix Proteins in Cancer
- Author
-
Nadezhda V. Popova and Manfred Jücker
- Subjects
collagen ,Cancer Research ,tenascin ,Oncology ,fibronectin ,extracellular matrix ,tumor microenvironment ,matrix metalloproteinases ,Neoplasms. Tumors. Oncology. Including cancer and carcinogens ,tumor progression ,Review ,RC254-282 ,matrikines - Abstract
Simple Summary Extracellular matrix is a three-dimensional network of macromolecules that provide structural and biochemical support to surrounding cells. Extracellular matrix plays a critical role in the development and progression of cancer. The extracellular matrix of the tumor is very different from the matrix of the normal tissue. Mainly fibroblasts produce and regulate matrix remodeling, but in cancer, the tumor matrix also originates from cancer cells. We describe the mechanisms of how the protein composition and structure of the extracellular matrix changes during cancer progression and how abnormal matrix deregulates the behavior of stromal cells and influences cancer progression. Abstract The extracellular matrix (ECM) is highly dynamic as it is constantly deposited, remodeled and degraded to maintain tissue homeostasis. ECM is a major structural component of the tumor microenvironment, and cancer development and progression require its extensive reorganization. Cancerized ECM is biochemically different in its composition and is stiffer compared to normal ECM. The abnormal ECM affects cancer progression by directly promoting cell proliferation, survival, migration and differentiation. The restructured extracellular matrix and its degradation fragments (matrikines) also modulate the signaling cascades mediated by the interaction with cell-surface receptors, deregulate the stromal cell behavior and lead to emergence of an oncogenic microenvironment. Here, we summarize the current state of understanding how the composition and structure of ECM changes during cancer progression. We also describe the functional role of key proteins, especially tenascin C and fibronectin, and signaling molecules involved in the formation of the tumor microenvironment, as well as the signaling pathways that they activate in cancer cells. more...
- Published
- 2022
Catalog
3. Fishing as an important source of food in the Arctic and subarctic zones of Yakutia
- Author
-
Ludmila N. Markova, Alexey F. Abramov, and Nadezhda V. Popova
- Subjects
Agriculture (General) ,Ecology (disciplines) ,Fishing ,0211 other engineering and technologies ,02 engineering and technology ,010501 environmental sciences ,01 natural sciences ,Arctic cisco ,S1-972 ,Plant science ,arctic ,arctic cisco ,heavy metals ,0105 earth and related environmental sciences ,fish ,021110 strategic, defence & security studies ,biology ,Agriculture ,Heavy metals ,biology.organism_classification ,Subarctic climate ,The arctic ,Fishery ,Arctic ,yakutia ,Environmental science ,General Agricultural and Biological Sciences - Abstract
The peculiarity of natural conditions of Yakutia plays an important role in the formation of economic activities of its population. A significant number of rivers and lakes are a favorable condition for the development and preservation of traditional fishing. Currently, more than 89% of the commercial fish catch is produced in the lower reaches of the large northern rivers and lakes in the Arctic and subarctic zones of Yakutia. The main part of this catch is whitefish species, which are valued for their fat content, protein content, culinary, and taste qualities. Fish is a valuable food product for the population of Yakutia. This article presents the results of the study on the nutritional value and the content of heavy metals in the Arctic cisco meat. The high content of fat and protein in the studied samples shows that the Arctic cisco meat belongs to high-protein and high-calorie products and has a high biological value. It was found that on average, the level of toxic metals in the Arctic cisco meat does not exceed the norms accepted in Russia for fish products. The data obtained suggest that the content of heavy metals in fish is due to the peculiarities of living conditions and environmental pollution. Over the past decades, the volume of fish production in Yakutia has been declining due to the socioeconomic and climatic factors. Due to the anthropogenic pollution of water in rivers and lakes by oil products and effluents and waste from various sectors of the economy, especially the mining industry, there is a reduction in the fish resources and there is a need to monitor the environmental condition of the fishing reservoirs and the fish food quality. more...
- Published
- 2020
- Full Text
- View/download PDF
4. METHOD FOR OBTAINING A PROTEIN-VITAMIN CONCENTRATE FOR DISEASE PREVENTION IN FARM ANIMALS
- Author
-
Margarita S. Savvinova, Nadezhda V. Popova, Alexsandra I. Pavlova, Galina P. Protodyakonova, and Zinaida G. Tatarinova
- Subjects
Vitamin ,chemistry.chemical_compound ,Multidisciplinary ,chemistry ,business.industry ,Medicine ,Physiology ,A protein ,Disease prevention ,General Chemistry ,Pharmacy ,business ,Education - Abstract
Regional feed supplies in Yakutia include hay stocks, succulent feeds, as well as own production and import of concentrated feeds to the republic. Main winter feeds include hay, silage, and haylage; in summer grass of natural pastures is available. Annual provision of livestock with nutrients reaches 60-65% of normal, which is a limiting factor for the development of the genetic potential of local cattle breeds in Yakutia. Understanding of general patterns in digestive processes and physiological and biochemical mechanisms of assimilation of nutrients was based on the results of the studies of domestic ruminant animals (cattle, sheep). Issues of increasing feed security remain urgent for agro-industrial production. The authors describe in detail a method of obtaining a protein-vitamin concentrate having pharmacological properties. Most of these processes involve gas components, liquid or solid substances. Complex hydrodynamic, thermal, and mass exchange processes occur simultaneously in fermenters. A method for expanding the production of feed protein using a combination of hydrodynamic and mass transfer characteristics and parameters with simultaneous optimization of the fermenter design and its operation modes is proposed, taking into account minimum energy consumption for oxygen dissolution and biomass production, based on technical capacity. Various types of devices are currently available; basically, they provide oxygen supply, as it is an integral part of device design, for the cultivation of microorganisms based on microbial synthesis. It should be emphasized that a fermenter is the main device of any microbiological production and largely determines its economic effectiveness. The obtained results will allow considerable acceleration of finalizing works for the development and improvement of perspective fermenter designs. more...
- Published
- 2019
- Full Text
- View/download PDF
5. The Role of mTOR Signaling as a Therapeutic Target in Cancer
- Author
-
Nadezhda V. Popova and Manfred Jücker
- Subjects
Cell ,mTORC1 ,Review ,Mechanistic Target of Rapamycin Complex 1 ,medicine.disease_cause ,PI3K ,Catalysis ,Inorganic Chemistry ,lcsh:Chemistry ,Phosphatidylinositol 3-Kinases ,Neoplasms ,medicine ,Autophagy ,Humans ,cancer ,Molecular Targeted Therapy ,Physical and Theoretical Chemistry ,Molecular Biology ,Protein kinase B ,lcsh:QH301-705.5 ,Protein Kinase Inhibitors ,Spectroscopy ,PI3K/AKT/mTOR pathway ,Cell Proliferation ,Mutation ,Clinical Trials as Topic ,therapy ,Cell growth ,business.industry ,TOR Serine-Threonine Kinases ,AKT ,Organic Chemistry ,Cancer ,General Medicine ,medicine.disease ,Computer Science Applications ,medicine.anatomical_structure ,Treatment Outcome ,lcsh:Biology (General) ,lcsh:QD1-999 ,Drug Resistance, Neoplasm ,Cancer research ,mTOR ,Phosphatidylinositol 3-Kinase ,mutation ,business ,Proto-Oncogene Proteins c-akt ,Signal Transduction - Abstract
The aim of this review was to summarize current available information about the role of phosphatidylinositol-3-kinase (PI3K)/AKT/mammalian target of rapamycin (mTOR) signaling in cancer as a potential target for new therapy options. The mTOR and PI3K/AKT/mTORC1 (mTOR complex 1) signaling are critical for the regulation of many fundamental cell processes including protein synthesis, cell growth, metabolism, survival, catabolism, and autophagy, and deregulated mTOR signaling is implicated in cancer, metabolic dysregulation, and the aging process. In this review, we summarize the information about the structure and function of the mTOR pathway and discuss the mechanisms of its deregulation in human cancers including genetic alterations of PI3K/AKT/mTOR pathway components. We also present recent data regarding the PI3K/AKT/mTOR inhibitors in clinical studies and the treatment of cancer, as well the attendant problems of resistance and adverse effects. more...
- Published
- 2021
6. Autophosphorylation of Orphan Receptor ERBB2 Can Be Induced by Extracellular Treatment with Mildly Alkaline Media
- Author
-
Nadezhda V. Popova, Alexander G. Petrenko, Natalia A. Chachina, I. E. Deyev, O. V. Serova, and Elena A Gantsova
- Subjects
0301 basic medicine ,alkaline medium ,Receptor, ErbB-2 ,Alkalies ,Catalysis ,Receptor tyrosine kinase ,Inorganic Chemistry ,lcsh:Chemistry ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Cell Line, Tumor ,Extracellular ,Humans ,ERBB3 ,pH sensor ,Epidermal growth factor receptor ,Physical and Theoretical Chemistry ,Phosphorylation ,Receptor ,skin and connective tissue diseases ,Molecular Biology ,lcsh:QH301-705.5 ,neoplasms ,Spectroscopy ,Orphan receptor ,biology ,Communication ,Organic Chemistry ,Autophosphorylation ,tyrosine phosphorylation ,Tyrosine phosphorylation ,General Medicine ,Computer Science Applications ,Cell biology ,Culture Media ,030104 developmental biology ,HEK293 Cells ,chemistry ,lcsh:Biology (General) ,lcsh:QD1-999 ,030220 oncology & carcinogenesis ,biology.protein ,receptor tyrosine kinase - Abstract
ErbB2 is an oncogene receptor tyrosine kinase linked to breast cancer. It is a member of the epidermal growth factor receptor (EGFR) minifamily. ErbB2 is currently viewed as an orphan receptor since, by itself, it does not bind EGF-like ligands and can be activated only when overexpressed in malignant cells or complexed with ErbB3, another member of the EGFR minifamily. Here, we report that ErbB2 can be activated by extracellular application of mildly alkaline (pH 8–9) media to ErbB2-transfected cells. We also show that the activation of the ErbB2 receptor by alkali is dose-dependent and buffer-independent. The endogenous ErbB2 receptor of A431 cell line can also undergo alkali-dependent autophosphorylation. Thus, we describe a novel ligand-independent mechanism of ErbB2 receptor activation. more...
- Published
- 2019
7. Synthetic Fluorophores for Visualizing Biomolecules in Living Systems
- Author
-
Vladimir I. Martynov, Nadezhda V. Popova, Alexander G. Petrenko, I. E. Deyev, and Alexey A. Pakhomov
- Subjects
chemistry.chemical_classification ,Fluorophore ,010405 organic chemistry ,Computer science ,Biomolecule ,Nanotechnology ,010402 general chemistry ,01 natural sciences ,Biochemistry ,Fluorescence ,0104 chemical sciences ,Living systems ,chemistry.chemical_compound ,chemistry ,Fluorescence microscope ,Molecular Medicine ,Fluorescent protein ,Molecular Biology ,Biotechnology - Abstract
The last decade has witnessed significant advance in the imaging of living systems using fluorescent markers. This progress has been primarily associated with the discovery of different spectral variants of fluorescent proteins. However, the fluorescent protein technology has its own limitations and, in some cases, the use of low-molecular-weight fluorophores is preferable. In this review, we describe the arsenal of synthetic fluorescent tools that are currently in researchers hands and span virtually the entire spectrum, from the UV to visible and, further, to the near-infrared region. An overview of recent advances in site-directed introduction of synthetic fluorophores into target cellular objects is provided. Application of these fluorescent probes to the solution of a wide range of biological problems, in particular, to the determination of local ion concentrations and pH in living systems, is discussed. more...
- Published
- 2016
- Full Text
- View/download PDF
8. Determination of Alkali-Sensing Parts of the Insulin Receptor-Related Receptor Using the Bioinformatic Approach
- Author
-
Nadezhda V. Popova, Alexander G. Petrenko, and I. E. Deyev
- Subjects
biology ,phosphorylation ,receptor ,Insulin ,medicine.medical_treatment ,Xenopus ,alkaline pH ,biology.organism_classification ,Biochemistry ,Receptor tyrosine kinase ,Insulin receptor ,Growth factor receptor ,biology.protein ,Extracellular ,medicine ,Molecular Medicine ,Receptor ,Molecular Biology ,Insulin Receptor-Related Receptor ,Research Article ,Biotechnology - Abstract
IRR (insulin receptor-related receptor) is a receptor tyrosine kinase belonging to the insulin receptor family, which also includes insulin receptor and IGF-IR receptor. We have previously shown that IRR is activated by extracellular fluid with pH 7.9 and regulates excess alkali excretion in the body. We performed a bioinformatic analysis of the pH-sensitive potential of all three members of the insulin receptor family of various animal species (from frog to man) and their chimeras with swapping of different domains in the extracellular region. An analysis using the AcalPred program showed that insulin receptor family proteins are divided into two classes: one class with the optimal working pH in the acidic medium (virtually all insulin receptor and insulin-like growth factor receptor orthologs, except for the IGF-IR ortholog from Xenopus laevis) and the second class with the optimal working pH in the alkaline medium (all IRR orthologs). The program had predicted that the most noticeable effect on the pH-sensitive property of IRR would be caused by the replacement of the L1 and C domains in its extracellular region, as well as the replacement of the second and third fibronectin repeats. It had also been assumed that replacement of the L2 domain would have the least significant effect on the alkaline sensitivity of IRR. To test the in silico predictions, we obtained three constructs with swapping of the L1C domains, the third L2 domain, and all three domains L1CL2 of IRR with similar domains of the insulin-like growth factor receptor. We found that replacement of the L1C and L1CL2 domains reduces the receptors ability to be activated with alkaline pH, thus increasing the half-maximal effective concentration by about 100%. Replacement of the L2 domain increased the half-maximal effective concentration by 40%. Thus, our results indicate the high predictive potential of the AcalPred algorithm, not only for the pH-sensitive enzymes, but also for pH-sensitive receptors. more...
- Published
- 2015
- Full Text
- View/download PDF
9. Alkaline pH induces IRR-mediated phosphorylation of IRS-1 and actin cytoskeleton remodeling in a pancreatic beta cell line
- Author
-
Alexander G. Petrenko, Marì Regoli, Eugenio Bertelli, O. V. Serova, Nadezhda V. Popova, I. E. Deyev, and Svetlana Zhenilo
- Subjects
Male ,0301 basic medicine ,medicine.medical_specialty ,Linsitinib ,Receptor tyrosine kinase ,Biology ,Biochemistry ,Cell Line ,Rats, Sprague-Dawley ,Mice ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Protein phosphorylation ,Insulin-Secreting Cells ,Internal medicine ,Insulin receptor substrate ,Insulin Secretion ,Membrane proteins ,medicine ,Animals ,Insulin ,pancreas ,Phosphorylation ,Protein kinase B ,Alkaline pH ,Pancreatic islets ,General Medicine ,Hydrogen-Ion Concentration ,Receptor, Insulin ,Rats ,IRS1 ,Cell biology ,Actin Cytoskeleton ,Insulin receptor ,Receptor tyrosine kinase, Protein phosphorylation, Membrane proteins, Insulin, Alkaline pH, pancreas ,030104 developmental biology ,Endocrinology ,medicine.anatomical_structure ,chemistry ,Insulin Receptor Substrate Proteins ,biology.protein ,Beta cell ,Pancreas ,030217 neurology & neurosurgery ,Signal Transduction - Abstract
Secretion of mildly alkaline (pH 8.0-8.5) juice to intestines is one of the key functions of the pancreas. Recent reports indicate that the pancreatic duct system containing the alkaline juice may adjoin the endocrine cells of pancreatic islets. We have previously identified the insulin receptor-related receptor (IRR) that is expressed in islets as a sensor of mildly alkaline extracellular media. In this study, we show that those islet cells that are in contact with the excretory ducts are also IRR-expressing cells. We further analyzed the effects of alkaline media on pancreatic beta cell line MIN6. Activation of endogenous IRR but not of the insulin receptor was detected that could be inhibited with linsitinib. The IRR autophosphorylation correlated with pH-dependent linsitinib-sensitive activation of insulin receptor substrate 1 (IRS-1), the primary adaptor in the insulin signaling pathway. However, in contrast with insulin stimulation, no protein kinase B (Akt/PKB) phosphorylation was detected as a result of alkali treatment. We observed overexpression of several early response genes (EGR2, IER2, FOSB, EGR1 and NPAS4) upon alkali treatment of MIN6 cells but those were IRR-independent. The alkaline medium but not insulin also triggered actin cytoskeleton remodeling that was blocked by pre-incubation with linsitinib. We propose that the activation of IRR by alkali might be part of a local loop of signaling between the exocrine and endocrine parts of the pancreas where alkalinization of the juice facilitate insulin release that increases the volume of secreted juice to control its pH and bicabonate content. more...
- Published
- 2017
10. Association of adaptor protein TRIP8b with clathrin
- Author
-
Nadezhda V. Popova, I. E. Deyev, and Alexander G. Petrenko
- Subjects
Cellular and Molecular Neuroscience ,biology ,Vesicle ,Insulin-like growth factor 2 receptor ,biology.protein ,Signal transducing adaptor protein ,Clathrin adaptor proteins ,Clathrin binding ,Endocytosis ,Biochemistry ,Clathrin ,Clathrin coat ,Cell biology - Abstract
TPR-containing Rab8b-interacting protein (TRIP8b) is a brain-specific hydrophilic cytosolic protein that contains tetratricopeptide repeats (TPRs). Previous studies revealed interaction of this protein via its TPR-containing domain with Rab8b small GTPase, hyperpolarization-activated cyclic nucleotide-regulated channel (HCN) channels and G protein-coupled receptor calcium-independent receptor of α-latrotoxin. We identified clathrin as a major component of eluates from the TRIP8b affinity matrix. In the present study, by in vitro-binding analysis we demonstrate a direct interaction between clathrin and TRIP8b. The clathrin-binding site was localized in the N-terminal (non-TPR containing) part of the TRIP8b molecule that contains two short motifs involved in the clathrin binding. In transfected HEK293 cells, co-expression of HCN1 with TRIP8b resulted in translocation of the channels from the cell surface to large intracellular puncta where both TRIP8b and clathrin were concentrated. These puncta co-localized partially with an early endosome marker and strongly overlapped with lysosome staining reagent. When HCN1 was co-expressed with a clathrin-non-binding mutant of TRIP8b, clathrin did not translocate to HCN1 and TRIP8b-containing puncta, suggesting that TRIP8b interacts with HCN and clathrin independently. We found TRIP8b present in the fraction of clathrin-coated vesicles purified from brain tissues. Stripping the clathrin coat proteins from the vesicles with Tris alkaline buffer resulted in concomitant release of TRIP8b. Our data suggest complex regulatory functions of TRIP8b in neuronal endocytosis through independent interaction with membrane proteins and components of the clathrin coat. more...
- Published
- 2011
- Full Text
- View/download PDF
11. Insulin Receptor-Related Receptor as an Extracellular Alkali Sensor
- Author
-
Sergey Zozulya, E. B. Burova, Eugenio Bertelli, Pascal Houillier, I. E. Deyev, Dmitry I. Rzhevsky, Arkady N. Murashev, O. V. Serova, Nadezhda V. Popova, Alexander G. Petrenko, Roman G. Efremov, Anastasiya A. Berchatova, Anton O. Chugunov, Dominique Eladari, N. N. Nikolsky, Konstantin P. Vassilenko, and Fabien Sohet more...
- Subjects
kidney ,insulin receptor-related receptor ,intercalated cells ,alkalosis ,acid-base balance ,Physiology ,Metabolic alkalosis ,Kidney ,Mice ,Xenopus laevis ,0302 clinical medicine ,Phosphorylation ,Receptor ,Mice, Knockout ,Orphan receptor ,0303 health sciences ,Hydrogen-Ion Concentration ,population characteristics ,Signal transduction ,Tyrosine kinase ,Signal Transduction ,medicine.medical_specialty ,Recombinant Fusion Proteins ,Biology ,Article ,Cell Line ,03 medical and health sciences ,Internal medicine ,parasitic diseases ,Extracellular ,medicine ,Animals ,Humans ,Molecular Biology ,Insulin Receptor-Related Receptor ,030304 developmental biology ,Cell Biology ,medicine.disease ,Receptor, Insulin ,Culture Media ,Protein Structure, Tertiary ,Rats ,Mice, Inbred C57BL ,Insulin receptor ,Sodium Bicarbonate ,Endocrinology ,Mutagenesis, Site-Directed ,biology.protein ,Protein Processing, Post-Translational ,030217 neurology & neurosurgery - Abstract
SummaryThe insulin receptor-related receptor (IRR), an orphan receptor tyrosine kinase of the insulin receptor family, can be activated by alkaline media both in vitro and in vivo at pH >7.9. The alkali-sensing property of IRR is conserved in frog, mouse, and human. IRR activation is specific, dose-dependent and quickly reversible and demonstrates positive cooperativity. It also triggers receptor conformational changes and elicits intracellular signaling. The pH sensitivity of IRR is primarily defined by its L1F extracellular domains. IRR is predominantly expressed in organs that come in contact with mildly alkaline media. In particular, IRR is expressed in the cell subsets of the kidney that secrete bicarbonate into urine. Disruption of IRR in mice impairs the renal response to alkali loading attested by development of metabolic alkalosis and decreased urinary bicarbonate excretion in response to this challenge. We therefore postulate that IRR is an alkali sensor that functions in the kidney to manage metabolic bicarbonate excess. more...
- Published
- 2011
- Full Text
- View/download PDF
12. Identification of proteins in complexes with α-latrotoxin receptors
- Author
-
I. E. Deyev, Nadezhda V. Popova, Alexander G. Petrenko, and O. V. Serova
- Subjects
Brain Chemistry ,Receptors, Peptide ,Latrotoxin ,Cell Membrane ,Organic Chemistry ,Neurexin ,Brain ,Spider Venoms ,Biological Transport ,Nerve Tissue Proteins ,Biology ,Endocytosis ,complex mixtures ,Biochemistry ,Synaptic vesicle ,Rats ,Cell biology ,Affinity chromatography ,Cytoplasm ,Animals ,Synaptic Vesicles ,Receptor ,Intracellular - Abstract
A thorough analysis of proteins capable of interacting with presynaptic receptors of alpha-latrotoxin was carried out. The protein components of receptor complexes were isolated from rat brain membranes by affinity chromatography on immobilized alpha-latrotoxin and antibodies to the cytoplasmic moiety of the calcium-independent receptor of alpha-latrotoxin (CIRL) followed by analysis by mass spectrometry. Several proteins were identified, with structural proteins, intracellular signal proteins, and proteins involved in the endocytosis and transport of synaptic vesicles being among them. more...
- Published
- 2008
- Full Text
- View/download PDF
13. Analysis of proteins interacting with TRIP8b adapter
- Author
-
A. N. Plotnikov, Nadezhda V. Popova, R. Kh. Ziganshin, I. E. Deyev, and Alexander G. Petrenko
- Subjects
biology ,Latrotoxin ,Membrane Proteins ,Signal transducing adaptor protein ,General Medicine ,Endocytosis ,Models, Biological ,Biochemistry ,Clathrin ,Exocytosis ,Rats ,Cell biology ,Tetratricopeptide ,Affinity chromatography ,Multiprotein Complexes ,Two-Hybrid System Techniques ,COS Cells ,Chlorocebus aethiops ,biology.protein ,Animals ,Humans ,Carrier Proteins ,Receptor ,Protein Binding - Abstract
Calcium-independent receptor of latrotoxin (CIRL) is an orphan heptahelical receptor implicated in regulation of exocytosis. To characterize molecular mechanisms of CIRL functioning, we searched for its intracellular partners using the yeast two-hybrid SR system with the cytoplasmic C-terminal fragment of CIRL as bait. One of the interacting proteins was identified as TRIP8b, a putative cytosolic adapter protein with multiple tetratricopeptide repeats. To understand functional significance of CIRL-TRIP8b interaction, we further isolated TRIP8b-interacting proteins by affinity chromatography of brain extracts on immobilized recombinant TRIP8b. Sixteen proteins were identified by mass spectrometry in the purified preparations. Clathrin and subunits of AP2 complex appeared to be the major TRIP8b-interacting proteins. Our data suggest a role of TRIP8b in receptor-mediated endocytosis. more...
- Published
- 2008
- Full Text
- View/download PDF
14. Poly(A)-binding Protein Positively Affects YB-1 mRNA Translation through Specific Interaction with YB-1 mRNA
- Author
-
Maxim A. Skabkin, Nadezhda V. Popova, Dmitry N. Lyabin, Lev P. Ovchinnikov, Luiz O. F. Penalva, and Olga V. Skabkina
- Subjects
Sucrose ,DNA, Complementary ,Reticulocytes ,Time Factors ,Ultraviolet Rays ,Immunoblotting ,Biology ,Inhibitory postsynaptic potential ,Poly(A)-Binding Proteins ,Biochemistry ,P-bodies ,Gene expression ,Poly(A)-binding protein ,Protein biosynthesis ,Animals ,RNA, Messenger ,Molecular Biology ,Messenger RNA ,Cell-Free System ,Dose-Response Relationship, Drug ,Temperature ,Nuclear Proteins ,Translation (biology) ,Cell Biology ,Blotting, Northern ,Precipitin Tests ,Molecular biology ,Globins ,DNA-Binding Proteins ,NFI Transcription Factors ,Gene Expression Regulation ,Cytoplasm ,Protein Biosynthesis ,CCAAT-Enhancer-Binding Proteins ,Codon, Terminator ,biology.protein ,Electrophoresis, Polyacrylamide Gel ,Rabbits ,Y-Box-Binding Protein 1 ,Plasmids ,Protein Binding ,Transcription Factors - Abstract
The major protein of cytoplasmic mRNPs from rabbit reticulocytes, YB-1, is a member of an ancient family of proteins containing a common structural feature, cold-shock domain. In eukaryotes, this family is represented by multifunctional mRNA/Y-box DNA-binding proteins that control gene expression at different stages. To address possible post-transcriptional regulation of YB-1 gene expression, we examined effects of exogenous 5'- and 3'-untranslatable region-containing fragments of YB-1 mRNA on its translation and stability in a cell-free system. The addition of the 3' mRNA fragment as well as its subfragment I shut off protein synthesis at the initiation stage without affecting mRNA stability. UV cross-linking revealed four proteins (69, 50, 46, and 44 kDa) that specifically interacted with the 3' mRNA fragment; the inhibitory subfragment I bound two of them, 69- and 50-kDa proteins. We have identified these proteins as PABP (poly(A)-binding protein) (69 kDa) and YB-1 (50 kDa) and demonstrated that titrating out of PABP by poly(A) strongly and specifically inhibits YB-1 mRNA cap(+)poly(A)(-) translation in a cell-free system. Thus, PABP is capable of positively affecting YB-1 mRNA translation in a poly(A) tail-independent manner. more...
- Published
- 2003
- Full Text
- View/download PDF
15. Interaction of calcium-independent latrotoxin receptor with intracellular adapter protein TRIP8b
- Author
-
A. N. Plotnikov, Alexander G. Petrenko, I. E. Deev, and Nadezhda V. Popova
- Subjects
DNA, Complementary ,Receptors, Peptide ,Latrotoxin ,Biophysics ,Calcium independent ,Biochemistry ,Receptors, G-Protein-Coupled ,Peroxins ,Chlorocebus aethiops ,Escherichia coli ,Animals ,Humans ,Receptor ,Phylogeny ,Chemistry ,Brain ,Membrane Proteins ,Signal transducing adaptor protein ,General Chemistry ,General Medicine ,Rats ,Cell biology ,COS Cells ,Calcium ,Intracellular ,Protein Binding - Published
- 2007
- Full Text
- View/download PDF
16. Structural determinants of the insulin receptor-related receptor activation by alkali
- Author
-
I. E. Deyev, Egor S. Zhevlenev, Alla V. Mitrofanova, O. V. Serova, Nikita Radionov, Alexander G. Petrenko, Nadezhda V. Popova, and Anastasiya A. Berchatova
- Subjects
Stereochemistry ,Mutant ,Mutation, Missense ,Alkalies ,medicine.disease_cause ,Biochemistry ,Protein Structure, Secondary ,Membrane Biology ,parasitic diseases ,medicine ,Humans ,Molecular Biology ,Insulin Receptor-Related Receptor ,Protein secondary structure ,Alanine ,Mutation ,biology ,Chemistry ,Cooperative binding ,Cell Biology ,Receptor, Insulin ,Protein Structure, Tertiary ,Insulin receptor ,HEK293 Cells ,Ectodomain ,biology.protein ,population characteristics - Abstract
IRR is a member of the insulin receptor (IR) family that does not have any known agonist of a peptide nature but can be activated by mildly alkaline medium and was thus proposed to function as an extracellular pH sensor. IRR activation by alkali is defined by its N-terminal extracellular region. To reveal key structural elements involved in alkali sensing, we developed an in vitro method to quantify activity of IRR and its mutants. Replacing the IRR L1C domains (residues 1–333) or L2 domain (residues 334–462) or both with the homologous fragments of IR reduced the receptor activity to 35, 64, and 7% percent, respectively. Within L1C domains, five amino acid residues (Leu-135, Gly-188, Arg-244, and vicinal His-318 and Lys-319) were identified as IRR-specific by species conservation analysis of the IR family. These residues are exposed and located in junctions between secondary structure folds. The quintuple mutation of these residues to alanine had the same negative effect as the entire L1C domain replacement, whereas none of the single mutations was as effective. Separate mutations of these five residues and of L2 produced partial negative effects that were additive. The pH dependence of cell-expressed mutants (L1C and L2 swap, L2 plus triple LGR mutation, and L2 plus quintuple LGRHK mutation) was shifted toward alkalinity and, in contrast with IRR, did not show significant positive cooperativity. Our data suggest that IRR activation is not based on a single residue deprotonation in the IRR ectodomain but rather involves synergistic conformational changes at multiple points. more...
- Published
- 2013
17. Clathrin-mediated endocytosis and adaptor proteins
- Author
-
Nadezhda V. Popova, Alexander G. Petrenko, and I. E. Deyev
- Subjects
biology ,media_common.quotation_subject ,Signal transducing adaptor protein ,Receptor-mediated endocytosis ,Endocytosis ,Biochemistry ,Clathrin ,Cell biology ,Cytoplasm ,biology.protein ,Molecular Medicine ,Clathrin adaptor proteins ,Internalization ,Receptor ,Molecular Biology ,Biotechnology ,media_common - Abstract
Macromolecules gain access to the cytoplasm of eukaryotic cells using one of several ways of which clathrin-dependent endocytosis is the most researched. Although the mechanism of clathrin-mediated endocytosis is well understood in general, novel adaptor proteins that play various roles in ensuring specific regulation of the mentioned process are being discovered all the time. This review provides a detailed account of the mechanism of clathrin-mediated internalization of activated G protein-coupled receptors, as well as a description of the major proteins involved in this process. more...
- Published
- 2013
18. Analysis of structural determinants of alkali sensor IRR positive cooperativity
- Author
-
Nadezhda V. Popova, I. E. Deyev, and Alexander G. Petrenko
- Subjects
business.industry ,Chemistry ,Peptide mapping ,Biophysics ,Cooperative binding ,General Chemistry ,General Medicine ,Hydrogen-Ion Concentration ,Alkali metal ,Biochemistry ,Peptide Mapping ,Receptor, Insulin ,Protein Structure, Tertiary ,Structure-Activity Relationship ,Text mining ,HEK293 Cells ,Structure–activity relationship ,Humans ,business - Published
- 2012
19. Association of adaptor protein TRIP8b with clathrin
- Author
-
Nadezhda V, Popova, Igor E, Deyev, and Alexander G, Petrenko
- Subjects
Potassium Channels ,Blotting, Western ,Cyclic Nucleotide-Gated Cation Channels ,Membrane Proteins ,DNA ,Exons ,Immunohistochemistry ,Clathrin ,Endocytosis ,Mass Spectrometry ,Article ,Cell Line ,Rats ,Escherichia coli ,Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels ,Animals ,Point Mutation ,Electrophoresis, Polyacrylamide Gel ,Plasmids ,Protein Binding ,Subcellular Fractions - Abstract
TPR-containing Rab8b-interacting protein (TRIP8b) is a brain-specific hydrophilic cytosolic protein that contains tetratricopeptide repeats (TPRs). Previous studies revealed interaction of this protein via its TPR-containing domain with Rab8b small GTPase, hyperpolarization-activated cyclic nucleotide-regulated channel (HCN) channels and G protein-coupled receptor calcium-independent receptor of α-latrotoxin. We identified clathrin as a major component of eluates from the TRIP8b affinity matrix. In the present study, by in vitro-binding analysis we demonstrate a direct interaction between clathrin and TRIP8b. The clathrin-binding site was localized in the N-terminal (non-TPR containing) part of the TRIP8b molecule that contains two short motifs involved in the clathrin binding. In transfected HEK293 cells, co-expression of HCN1 with TRIP8b resulted in translocation of the channels from the cell surface to large intracellular puncta where both TRIP8b and clathrin were concentrated. These puncta co-localized partially with an early endosome marker and strongly overlapped with lysosome staining reagent. When HCN1 was co-expressed with a clathrin-non-binding mutant of TRIP8b, clathrin did not translocate to HCN1 and TRIP8b-containing puncta, suggesting that TRIP8b interacts with HCN and clathrin independently. We found TRIP8b present in the fraction of clathrin-coated vesicles purified from brain tissues. Stripping the clathrin coat proteins from the vesicles with Tris alkaline buffer resulted in concomitant release of TRIP8b. Our data suggest complex regulatory functions of TRIP8b in neuronal endocytosis through independent interaction with membrane proteins and components of the clathrin coat. more...
- Published
- 2011
20. Deficient response to experimentally induced alkalosis in mice with the inactivated insrr gene
- Author
-
Alexander G. Petrenko, Nadezhda V. Popova, Arkady N. Murashev, Anastasiya A. Berchatova, Dmitry I. Rzhevsky, O. V. Serova, and I. E. Deyev
- Subjects
medicine.medical_specialty ,Alkalosis ,Chemistry ,Insulin ,medicine.medical_treatment ,Mutant ,Metabolic alkalosis ,medicine.disease ,Biochemistry ,Phenotype ,Endocrinology ,INSRR Gene ,Internal medicine ,Knockout mouse ,medicine ,Molecular Medicine ,Receptor ,Molecular Biology ,Biotechnology - Abstract
Currently, the molecular mechanisms of the acid-base equilibrium maintenance in the body remain poorly understood. The development of alkalosis under various pathological conditions poses an immediate threat to human life. Understanding the physiological mechanisms of alkalosis compensation may stimulate the development of new therapeutic approaches and new drugs for treatment. It was previously shown that the orphan insulin receptor-related receptor (IRR) is activated by mildly alkaline media. In this study, we analyzed mutant mice with targeted inactivation of the insrr gene encoding IRR, and revealed their phenotype related to disorders of the acid-base equilibrium. Higher concentrations of bicarbonate and CO 2 were found in the blood of insrr knockout mice in response to metabolic alkalosis. more...
- Published
- 2011
21. Association of the subunits of the calcium-independent receptor of α-latrotoxin
- Author
-
O. V. Serova, Nadezhda V. Popova, Alexander G. Petrenko, and I. E. Deyev
- Subjects
Receptors, Peptide ,Latrotoxin ,Protein subunit ,Molecular Sequence Data ,Biophysics ,Spider Venoms ,Biology ,Biochemistry ,Receptors, G-Protein-Coupled ,Latrophilin 1 ,Chlorocebus aethiops ,Animals ,Humans ,Immunoprecipitation ,5-HT5A receptor ,Amino Acid Sequence ,Receptor ,Molecular Biology ,G protein-coupled receptor ,Thrombin ,Cell Biology ,Cell biology ,Transmembrane domain ,Protein Subunits ,Ectodomain ,COS Cells ,Protein Multimerization - Abstract
CIRL-1 also called latrophilin 1 or CL belongs to the family of adhesion G protein-coupled receptors (GPCRs). As all members of adhesion GPSR family CIRL-1 consists of two heterologous subunits, extracellular hydrophilic p120 and heptahelical membrane protein p85. Both CIRL-1 subunits are encoded by one gene but as a result of intracellular proteolysis of precursor, mature receptor has two-subunit structure. It was also shown that a minor portion of the CIRL-1 receptor complexes dissociates, producing the soluble receptor ectodomain, and this dissociation is due to the second cleavage at the site between the site of primary proteolysis and the first transmembrane domain. Recently model of independent localization p120 and p85 on the cell surface was proposed. In this article we evaluated the amount of p120-p85 complex still presented on the cellular membrane and confirmed that on cell surface major amount of mature CIRL-1 presented as a p120-p85 subunit complex. more...
- Published
- 2010
22. YB-1 promotes microtubule assembly in vitro through interaction with tubulin and microtubules
- Author
-
N. A. Shanina, Anne Tarrade, Alain Mechulam, V.D. Vasiliev, Nadezhda V. Popova, Olga V. Skabkina, Lev P. Ovchinnikov, Flavio Toma, Patrick A. Curmi, Vandana Joshi, Elena S. Nadezhdina, David Pastré, Sonia Baconnais, Konstantin G. Chernov, Judith Melki, Structure et activité des biomolécules normales et pathologiques (SABNP), Université d'Évry-Val-d'Essonne (UEVE)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institute of Protein Research, Russian Academy of Sciences, Pushchino, Lomonosov Moscow State University (MSU), Interactions moléculaires et cancer (IMC (UMR 8126)), Signalisation, noyaux et innovations en cancérologie (UMR8126), Centre National de la Recherche Scientifique (CNRS)-Institut Gustave Roussy (IGR)-Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS)-Institut Gustave Roussy (IGR)-Université Paris-Sud - Paris 11 (UP11), Institute of Protein Research, Russian Academy of Sciences [Moscow] (RAS), Hadassah University Hospital, and Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR)-Centre National de la Recherche Scientifique (CNRS) more...
- Subjects
Microtubule-associated protein ,[SDV]Life Sciences [q-bio] ,lcsh:Animal biochemistry ,RNA-binding protein ,Microscopy, Atomic Force ,Microtubules ,Biochemistry ,Chromatography, Affinity ,lcsh:Biochemistry ,03 medical and health sciences ,Tubulin ,Microtubule ,Transcription (biology) ,Gene expression ,Animals ,Humans ,lcsh:QD415-436 ,RNA, Messenger ,Molecular Biology ,lcsh:QP501-801 ,030304 developmental biology ,0303 health sciences ,biology ,Tissue Extracts ,030302 biochemistry & molecular biology ,Nuclear Proteins ,RNA-Binding Proteins ,RNA ,Translation (biology) ,Peptide Fragments ,3. Good health ,Cell biology ,DNA-Binding Proteins ,Ribonucleoproteins ,biology.protein ,Rabbits ,Y-Box-Binding Protein 1 ,Microtubule-Associated Proteins ,Research Article - Abstract
Background YB-1 is a major regulator of gene expression in eukaryotic cells. In addition to its role in transcription, YB-1 plays a key role in translation and stabilization of mRNAs. Results We show here that YB-1 interacts with tubulin and microtubules and stimulates microtubule assembly in vitro. High resolution imaging via electron and atomic force microscopy revealed that microtubules assembled in the presence of YB-1 exhibited a normal single wall ultrastructure and indicated that YB-1 most probably coats the outer microtubule wall. Furthermore, we found that YB-1 also promotes the assembly of MAPs-tubulin and subtilisin-treated tubulin. Finally, we demonstrated that tubulin interferes with RNA:YB-1 complexes. Conclusion These results suggest that YB-1 may regulate microtubule assembly in vivo and that its interaction with tubulin may contribute to the control of mRNA translation. more...
- Published
- 2008
- Full Text
- View/download PDF
23. Effect of changes in ambient pH on phosphorylation of cellular proteins
- Author
-
I. E. Deev, E. Zh. Kurmangaliev, E. B. Burova, Yu. S. Galagan, N. N. Nikol’skii, Alexander G. Petrenko, O. V. Serova, Sergey Zozulya, K. P. Vasilenko, and Nadezhda V. Popova
- Subjects
Chemistry ,MAP Kinase Signaling System ,Phospholipase C gamma ,Biophysics ,General Chemistry ,General Medicine ,Hydrogen-Ion Concentration ,Phosphoproteins ,Biochemistry ,Receptor, Insulin ,Cell biology ,Cell Line ,Oncogene Protein v-akt ,Protein Subunits ,STAT Transcription Factors ,Phosphorylation ,Animals ,Humans ,Tyrosine ,Electrophoresis, Polyacrylamide Gel ,Cellular proteins - Published
- 2006
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.