Search results for "CONSERVE"

showing 10 items of 127 documents

BvCOLD1: A novel aquaporin from sugar beet (Beta vulgarisL.) involved in boron homeostasis and abiotic stress

2018

Beta vulgaris (sugar beet) is one of the most important industrial crops. Screening of a cDNA library for sugar beet genes able to confer cold tolerance upon overexpression in yeast identified a novel aquaporin, which we named BvCOLD1. The amino acid sequence of BvCOLD1 indicated that an acidic protein (pI 5.18) is similar to tonoplast intrinsic protein aquaporins. RNA expression analysis indicated that BvCOLD1 is expressed in all sugar beet organs. Confocal microscopy of a green fluorescent protein-tagged version localized BvCOLD1 in the endoplasmic reticulum in yeast and in plant cells. Experiments in yeast showed that BvCOLD1 has an important role in transporting several molecules, among…

0301 basic medicinePhysiologyAbiotic stressfungifood and beveragesAquaporinPlant ScienceAmaranthaceaeBiologybiology.organism_classificationYeastConserved sequence03 medical and health sciences030104 developmental biologyBiochemistryArabidopsisSugar beetPeptide sequencePlant, Cell & Environment
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Molecular evolution of antioxidant and hypoxia response in long-lived, cancer-resistant blind mole rats: The Nrf2-Keap1 pathway.

2015

The Nrf2-Keap1 pathway is crucial for the cellular antioxidant and hypoxia response in vertebrates. Deciphering its modifications in hypoxia-adapted animals will help understand its functionality under environmental stress and possibly allow for knowledge transfer into biomedical research. The blind mole rat Spalax, a long-lived cancer-resistant rodent, lives in burrows underground and is adapted to severely hypoxic conditions. Here we have conducted a bioinformatical survey of Spalax core genes from the Nrf2-Keap1 pathway on the coding sequence level in comparison to other hypoxia-tolerant and -sensitive rodents. We find strong sequence conservation across all genes, illustrating the pathw…

0301 basic medicineRodentSpalaxNF-E2-Related Factor 2Molecular Sequence DataConserved sequenceEvolution Molecular03 medical and health sciencesbiology.animalNeoplasmsGene expressionGeneticsAnimalsAmino Acid SequencePeptide sequenceGeneConserved SequenceGeneticsKelch-Like ECH-Associated Protein 1030102 biochemistry & molecular biologybiologyMole RatsIntracellular Signaling Peptides and ProteinsGeneral Medicinebiology.organism_classificationPhenotypeKEAP1Cell HypoxiaRatsOxidative Stress030104 developmental biologySequence AlignmentGene
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Protein-protein interactions can be predicted using coiled coil co-evolution patterns

2016

AbstractProtein-protein interactions are sometimes mediated by coiled coil structures. The evolutionary conservation of interacting orthologs in different species, along with the presence or absence of coiled coils in them, may help in the prediction of interacting pairs. Here, we illustrate how the presence of coiled coils in a protein can be exploited as a potential indicator for its interaction with another protein with coiled coils. The prediction capability of our strategy improves when restricting our dataset to highly reliable, known protein-protein interactions. Our study of the co-evolution of coiled coils demonstrates that pairs of interacting proteins can be distinguished from no…

0301 basic medicineStatistics and ProbabilityComputational biologyCorrelated evolutionGeneral Biochemistry Genetics and Molecular BiologyProtein Structure SecondaryProtein–protein interactionConserved sequenceEvolution Molecular03 medical and health sciencesProtein-protein interactionModelling and SimulationImmunology and Microbiology(all)Coiled coilGeneticsCoiled coilPhysicsMedicine(all)030102 biochemistry & molecular biologyGeneral Immunology and MicrobiologyAgricultural and Biological Sciences(all)Models GeneticBiochemistry Genetics and Molecular Biology(all)Applied MathematicsA proteinProteinsGeneral Medicine030104 developmental biologyModeling and SimulationGeneral Agricultural and Biological SciencesJournal of Theoretical Biology
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High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae)

2017

Lectins are carbohydrate-interacting proteins that play a pivotal role in multiple physiological and developmental aspects of all organisms. They can specifically interact with different bacterial and viral pathogens through carbohydrate-recognition domains (CRD). In addition, lectins are also of biotechnological interest because of their potential use as biosensors for capturing and identifying bacterial species. In this work, three C-type lectins from the Lepidoptera Spodoptera exigua were produced as recombinant proteins and their bacterial agglutination properties were characterized. The lowest protein concentration producing bacterial agglutination against a panel of different Gram+ an…

0301 basic medicineagglutinationlcsh:BiotechnologyClinical BiochemistryMicrobial Sensitivity TestsSpodopteraSpodopteraC-type lectin; agglutination; CRD; bacterial detection; <i>E. coli</i>ArticleMicrobiologylaw.inventionbacterial detectionLepidoptera genitalia03 medical and health sciences0302 clinical medicinelawC-type lectinlcsh:TP248.13-248.65Agglutination TestsExiguaEscherichia coliAnimalsLectins C-TypeAmino Acid SequenceConserved SequencePhylogenybiologyE. coliCRDGeneral Medicinebiology.organism_classificationImmunity InnateC-type lectinAgglutination (biology)030104 developmental biologyRecombinant DNANoctuidaeInsect ProteinsProtein concentration030215 immunologybiotechnology
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Ectodomain shedding of CD99 within highly conserved regions is mediated by the metalloprotease meprin β and promotes transendothelial cell migration.

2016

The adhesion molecule CD99 is essential for the transendothelial migration of leukocytes. In this study, we used biochemical and cellular assays to show that CD99 undergoes ectodomain shedding by the metalloprotease meprin β and subsequent intramembrane proteolysis by γ-secretase. The cleavage site in CD99 was identified by mass spectrometry within an acidic region highly conserved through different vertebrate species. This finding fits perfectly to the unique cleavage specificity of meprin β with a strong preference for aspartate residues and suggests coevolution of protease and substrate. We hypothesized that limited CD99 cleavage by meprin β would alter cellular transendothelial migratio…

0301 basic medicinemedicine.medical_treatmentProteolysis12E7 AntigenCleavage (embryo)Biochemistry03 medical and health sciencesCarcinoma Lewis LungMice0302 clinical medicineGeneticsmedicineAnimalsHumansMolecular BiologyConserved SequenceMetalloproteinaseProteasemedicine.diagnostic_testChemistryTransendothelial and Transepithelial MigrationLewis lung carcinomaMetalloendopeptidasesCell migrationMolecular biologyIn vitroMice Inbred C57BL030104 developmental biologyHEK293 CellsEctodomain030220 oncology & carcinogenesisProteolysisBiotechnologyHeLa CellsFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Genomic structure and functional characterization of the human ADAM10 promoter

2005

The ADAM10 gene encodes a membrane-bound disintegrin-metalloproteinase, which, after overexpression in an Alzheimer disease (AD) mouse model, prevents amyloid pathology and improves long-term potentiation and memory. Because enhancing ADAM10 expression appears to be a reasonable approach for treatment of AD, we functionally analyzed the ADAM10 gene. Both human and mouse ADAM10 genes comprise approximately 160 kbp, are composed of 16 exons, and are evolutionarily highly conserved within 500 bp upstream of either translation initiation site. By using luciferase reporter assays, we demonstrate that nucleotides -2179 to -1 upstream of the human ADAM10 translation initiation site represent a fun…

5' Flanking Region5' flanking regionTretinoinBiologyPolymorphism Single NucleotideBiochemistryCell LineConserved sequenceADAM10 ProteinMiceOpen Reading FramesExonAlzheimer DiseaseGeneticsAnimalsHumansPromoter Regions GeneticMolecular BiologyTranscription factorGeneConserved SequenceExpressed Sequence TagsIntronMembrane ProteinsPromoterExonsMolecular biologyIntronsADAM ProteinsOpen reading frameMutagenesis Site-DirectedAmyloid Precursor Protein SecretasesBiotechnologyThe FASEB Journal
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A series of West European patients with severe cardiac and skeletal myopathy associated with a de novo R406W mutation in desmin.

2003

Desminopathy is a familial or sporadic cardiac and skeletal muscular dystrophy associated with mutations in desmin. We have previously characterized a de novo desmin R406W mutation in a patient of European origin with early onset muscle weakness in the lower extremities and atrioventricular conduction block requiring a permanent pacemaker. The disease relentlessly progressed resulting in severe incapacity within 5 years after onset. We have now identified three other patients with early onset rapidly progressive cardiac and skeletal myopathy caused by this same desmin R406W mutation. The mutation was present in each studied patient, but not in their parents or other unaffected family member…

AdultMaleModels Molecularmedicine.medical_specialtyPathologyNeurologyHeart diseaseAdolescentAmino Acid MotifsCardiomyopathymacromolecular substancesDiseaseBiologyProtein Structure SecondaryDesmin03 medical and health sciences0302 clinical medicineMuscular DiseasesmedicineHumansMuscular dystrophyMyopathyMuscle SkeletalConserved Sequence030304 developmental biology0303 health sciencesMuscle WeaknessBase SequenceMyocardiumMuscle weaknessAnatomymedicine.diseasePedigreeEuropeHeart BlockNeurologyAmino Acid SubstitutionMutationDisease ProgressionDesminFemaleNeurology (clinical)medicine.symptomCardiomyopathies030217 neurology & neurosurgeryJournal of neurology
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De novo mutation in a male patient with Fabry disease: a case report

2014

Abstract Background Fabry disease is an X-linked inherited metabolic condition where the deficit of the α-galactosidase A enzyme, encoded by the GLA gene, leads to glycosphingolipid storage, mainly globotriaosylceramide. To date, more than 600 mutations have been identified in human GLA gene that are responsible for FD, including missense and nonsense mutations, small and large deletions. Such mutations are usually inherited, and cases of de novo onset occur rarely. Case presentation In this article we report an interesting case of a 44-year-old male patient suffering from a severe form of Fabry disease, with negative family history. The patient showed signs such as cornea verticillata, ang…

AdultMaleProtein Foldingα-galactosidase ADe novo mutationNonsense mutationD165H mutationGlobotriaosylceramideMutation MissenseCase ReportBiologymedicine.disease_causeGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundGermline mutationmedicineMissense mutationHumansPoint MutationThrombophiliaEnzyme Replacement TherapyAmino Acid SequenceChildGLA geneConserved SequenceGerm-Line MutationMedicine(all)GeneticsMutationFabry diseaseSequence Homology Amino AcidBiochemistry Genetics and Molecular Biology(all)Point mutationGeneral MedicineEnzyme replacement therapymedicine.diseaseFabry diseasePedigreeStrokechemistryAmino Acid Substitutionalpha-GalactosidaseKidney Failure ChronicFemaleSymptom AssessmentSequence AlignmentBMC Research Notes
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Oxygen binding properties of non-mammalian nerve globins

2006

Oxygen-binding globins occur in the nervous systems of both invertebrates and vertebrates. While the function of invertebrate nerve haemoglobins as oxygen stores that extend neural excitability under hypoxia has been convincingly demonstrated, the physiological role of vertebrate neuroglobins is less well understood. Here we provide a detailed analysis of the oxygenation characteristics of nerve haemoglobins from an annelid (Aphrodite aculeata), a nemertean (Cerebratulus lacteus) and a bivalve (Spisula solidissima) and of neuroglobin from zebrafish (Danio rerio). The functional differences have been related to haem coordination: the haem is pentacoordinate (as in human haemoglobin and myogl…

AnnelidaDanioNeuroglobinNerve Tissue ProteinsCooperativityBiochemistryHemoglobinschemistry.chemical_compoundJournal ArticleAnimalsGlobinNerve TissueMolecular BiologyConserved SequenceZebrafishAnnelidbiologyResearch Support Non-U.S. Gov'tTemperatureHexacoordinateCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationGlobinsOxygenMyoglobinchemistryBiochemistryNeuroglobinOxygen binding
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Neuroglobin and cytoglobin: fresh blood to the vertebrate globin family

2002

Neuroglobin and cytoglobin are two recently discovered members of the vertebrate globin family. Both are intracellular proteins endowed with hexacoordinated heme-Fe atoms, in their ferrous and ferric forms, and display O2 affinities comparable with that of myoglobin. Neuroglobin, which is predominantly expressed in nerve cells, is thought to protect neurons from hypoxic–ischemic injury. It is of ancient evolutionary origin, and is homologous to nerve globins of invertebrates. Cytoglobin is expressed in many different tissues, although at varying levels. It shares common ancestry with myoglobin, and can be traced to early vertebrate evolution. The physiological roles of neuroglobin and cytog…

AnnelidaMolecular Sequence DataNeuroglobinNerve Tissue ProteinsHemeReview ArticleBiochemistryMicechemistry.chemical_compoundbiology.animalGeneticsAnimalsHumansAmino Acid SequenceGlobinMolecular BiologyHemeZebrafishConserved SequenceZebrafishBrain ChemistrybiologyCytoglobinCytoglobinBrainVertebratebiology.organism_classificationMolecular biologyGlobinsCell biologyOxygenMyoglobinchemistryNeuroglobinSequence AlignmentFunction (biology)EMBO reports
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