Search results for "Neuroglobin"

showing 4 items of 54 documents

Human neuroglobin: crystals and preliminary X-ray diffraction analysis

2002

Neuroglobin, a recently discovered member of the haemoglobin superfamily, is primarily expressed in the brain of humans and other vertebrates, where it has been proposed to enhance O(2) supply in response to hypoxia or ischaemia, protecting the neuron from hypoxic injury. Neuroglobin is the first example of a vertebrate haemoglobin in which a hexacoordinate haem geometry has been detected. A triple mutant (replacing three Cys residues) of human neuroglobin (151 amino acids) has been expressed in Escherichia coli, purified and crystallized in two crystal forms, the best of which diffracts to 1.95 A resolution using synchrotron radiation. The crystals belong to space group P2(1), with unit-ce…

chemistry.chemical_classificationCrystallographyProtein moleculesResolution (electron density)HexacoordinateNeuroglobinNerve Tissue ProteinsGeneral MedicineBiologymedicine.disease_causeRecombinant ProteinsAmino acidGlobinsCrystalCrystallographychemistryX-Ray DiffractionStructural BiologyNeuroglobinX-ray crystallographymedicineHumansEscherichia coli
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Regulation and Role of Neuroglobin and Cytoglobin Under Hypoxia

2007

Neuroglobin (Ngb) and cytoglobin (Cygb) are two novel members of the globin superfamily that are ubiquitously present in vertebrates. Their exact physiological roles are still uncertain. Here we review the expression of Ngb and Cygb, with particular emphasis on their regulation and potential role under hypoxia. Ngb expression is confined to neurons and some endocrine tissues. At the subcellular level, Ngb is associated with the presence of mitochondria and thus linked to the oxidative metabolism. Hypoxia or ischemic insults most likely do not strongly increase Ngb levels in the rodent brain. This might be explained by the fact that most mammals are not adapted to low oxygen levels. In zebra…

chemistry.chemical_classificationReactive oxygen speciesCell typeCytoglobinRespiratory chainBiologyMitochondrionbiology.organism_classificationCell biologyBiochemistrychemistryNeuroglobinGlobinZebrafish
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Protection of islets in culture by delivery of oxygen binding neuroglobin via protein transduction.

2005

Islet transplantation has become an accepted method to treat type 1 diabetes. To succeed and achieve normal levels of glucose in transplant recipients, the quality of the transplanted islets is of the utmost importance. Lack of oxygen during organ procurement, islet isolation, and subsequent culture triggers apoptosis or necrosis and loss of islet function, causing the yield and quality to diminish. A promising candidate for cytoprotection against oxygen deprivation is neuroglobin (Ngb). Ngb is a recently described member of globin family and is expressed in neurons, retina, and pancreatic islets. To overexpress this protein in the islets and study its ability to protect them, we utilized p…

endocrine systemmedicine.medical_specialtyendocrine system diseasesCell SurvivalIslets of Langerhans TransplantationNeuroglobinNerve Tissue ProteinsCell SeparationBiologyTransduction (genetics)AutomationIslets of LangerhansOxygen ConsumptionInternal medicinemedicineHumansCells CulturedTransplantationgeographygeography.geographical_feature_categoryMicroscopy ConfocalPancreatic isletsBinding proteinIsletFlow CytometryCytoprotectionCell HypoxiaCell biologyGlobinsTransplantationProtein TransportEndocrinologymedicine.anatomical_structureNeuroglobinGene Products tatSurgeryOxygen bindingTransplantation proceedings
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Globins and hypoxia adaptation in the goldfish, Carassius auratus

2008

Goldfish (Carassius auratus) may survive in aquatic environments with low oxygen partial pressures. We investigated the contribution of respiratory proteins to hypoxia tolerance in C. auratus. We determined the complete coding sequence of hemoglobin α and β and myoglobin, as well as partial cDNAs from neuroglobin and cytoglobin. Like the common carp (Cyprinus carpio), C. auratus possesses two paralogous myoglobin genes that duplicated within the cyprinid lineage. Myoglobin is also expressed in nonmuscle tissues. By means of quantitative real-time RT-PCR, we determined the changes in mRNA levels of hemoglobin, myoglobin, neuroglobin and cytoglobin in goldfish exposed to prolonged hypoxia (48…

inorganic chemicalsbiologyCytoglobinCell Biologybiology.organism_classificationBiochemistryMolecular biologySuperoxide dismutasechemistry.chemical_compoundMyoglobinchemistryNeuroglobinLactate dehydrogenasebiology.proteinHemoglobinGlobinMolecular BiologyZebrafishFEBS Journal
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