Search results for "Hemolymph"

showing 10 items of 126 documents

9 Å cryo-EM structure and molecular model of a gastropod hemocyanin didecamer (KLH1) reveals the architecture of the asymmetric collar

2008

Hemocyanins are blue copper proteins that transport oxygen in the hemolymph of many arthropods and molluscs. Molluscan hemocyanins are decamers, didecamers or multidecamers of a 350–400 kDa polypeptide subunit that is subdivided into seven or eight different functional units (FUs, each with a single copper active site). The quaternary structure is a semi-hollow cylinder consisting of a wall and a collar. Recently, we published a 9 A cryo-EM structure and molecular model of a cephalopod hemocyanin decamer (NpH, from Nautilus pompilius) that answered many hitherto unsolved questions concerning the quaternary structure of molluscan hemocyanin. Notably, it revealed the twisted pathway of the 10…

Molecular modelbiologyChemistryStereochemistryCopper proteinmedicine.medical_treatmentProtein subunitActive siteHemocyaninAnatomybiology.organism_classificationCephalopodHemolymphbiology.proteinmedicineProtein quaternary structure
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Variations in haemolymph ionized calcium concentrations in the crustacean Orchestia cavimana during a moult cycle

1993

Abstract Measurements of ionized calcium concentration in the haemolymph of the semi-terrestrial crustacean Orchestia cavimana were taken during the 14 successive moulting stages by ion-selective electrode direct potentiometry on pooled samples. Ionized calcium showed major variations associated with the moult cycle. Titres were low and relatively stable in intermoult and early premoult, then progressively increased during mid and late premoult to reach maximal values just at exuviation, and rapidly fell down during the postmoult. The variations of the ionized fraction showed a close correlation with those of the calcaemia (= total fraction), suggesting the presence of efficient haemolympha…

MudaCalcium metabolismbiologyPhysiologyEcologychemistry.chemical_elementCalciumOrchestiabiology.organism_classificationCrustaceanAnimal sciencechemistryOrchestia cavimanaInsect ScienceHemolymphMoultingJournal of Insect Physiology
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Coordination and Integration of Metabolism in Insect Flight*

1997

Abstract Insect flight is the most energy-demanding activity of animals. It requires the coordination and cooperation of many tissues, with the nervous system and neurohormones controlling the performance and energy metabolism of muscles, and of the fat body, ensuring that the muscles and nerves are supplied with essential fuels throughout flight. Muscle metabolism can be based on several different fuels, the proportions of which vary according to the insect species and the stage in flight activity. Octopamine, which acts as neurotransmitter, neuromodulator or neurohormone in insects, has a central role in flight. It is present in brain, ventral ganglia and nerves, supplying peripheral tiss…

Nervous systemPhysiologyOctopamine (drug)BiologyBiochemistryInsect flightchemistry.chemical_compoundmedicine.anatomical_structureFructose 26-bisphosphatechemistryBiochemistryHemolymphmedicinemedicine.symptomNeurohormonesMolecular BiologyMuscle contractionPhosphofructokinaseComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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In Vitro Release of Lectins From Phallusia mamillata Hemocytes After Their Fractionation on a Density Gradient

1993

Hemocytes were fractionated by centrifugation on a discontinuous Percoll density gradient from the hemolymph of Phallusia mamillata. Results obtained from microcultures of the fractionated hemocytes, sugar-inhibition experiments, SDS-PAGE, and immunoblotting indicate that “compartment cells” release cellular-type (CL) lectins that are specific for α-lactose and lactulose. The released lectins have the same properties as the CL lectins that were previously isolated from sonicated unfractionated hemocytes, but they differ in terms of some molecular and immunological properties from the lectins (SL) purified from the serum. SLs were never found in the supernatants from microcultures of the fra…

PhallusiabiologyDensity gradientfungiLectinGeneral MedicineFractionationbiology.organism_classificationMolecular biologyIn vitroHemolymphbiology.proteinAnimal Science and ZoologyCentrifugationTunicate hemocyte cells populationPercoll
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The regulation of trehalose metabolism in insects.

1996

Trehalose is a non-reducing disaccharide comprising two glucose molecules. It is present in high concentration as the main haemolymph (blood) sugar in insects. The synthesis of trehalose in the fat body (an organ analogous in function to a combination of liver and adipose tissue in vertebrates) is stimulated by neuropeptides (hypertrehalosaemic hormones), released from the corpora cardiaca, a neurohaemal organ associated with the brain. The peptides cause a decrease in the content of fructose 2,6-bisphosphate in fat body cells. Fructose 2,6-bisphosphate, acting synergistically with AMP, is a potent activator of the glycolytic enzyme 6-phosphofructokinase-1 and a strong inhibitor of the gluc…

PharmacologyInsectaMolecular Sequence DataTrehalase activityAdipose tissueTrehaloseFructoseCell BiologyBiologyTrehaloseCellular and Molecular Neurosciencechemistry.chemical_compoundFructose 26-bisphosphatechemistryBiochemistryCarbohydrate SequenceHemolymphMolecular MedicineAnimalsGlycolysisAmino Acid SequenceTrehalaseMolecular BiologyExperientia
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Crystal cell pattern modification in a melanotic tumor strain of Drosophila melanogaster.

1988

3rd instar larvae of the melanotic tumor tu-pb strain of Drosophila melanogaster hold a lower number of free-circulating crystal cells in their hemolymph than the wild type ones. This pattern could result from an abnormal retention of mature crystal cells in the hematopoietic organs, as the strong hemocyte melanization inside the lymph glands of heat-treated tu-pb larvae seems to demonstrate. Melanotic tumor formation and modification of the crystal cell pattern may be related.

Pharmacologyanimal structuresStrain (chemistry)biologyfungiWild typeTemperatureCell Biologybiology.organism_classificationCell biologyCellular and Molecular NeuroscienceHaematopoiesisDrosophila melanogasterGenesHemolymphImmunologyHemolymphMelanogasterMolecular MedicineInstarAnimalsLymphDrosophila melanogasterMolecular BiologyMelanomaExperientia
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The Pandinus imperator haemolymph lipoprotein, an unusual phosphatidylserine carrying lipoprotein.

2009

The haemolymph lipoprotein of the scorpion, Pandinus imperator was isolated and characterised. Contrary to the lipoproteins of insects and the discoidal HDL-lipoproteins of a crayfish and polychaete, the Pandinus lipoprotein consists of three instead of two apoproteins (apoPiLp I = 230 kDa, apoPiLp II = 130 kDa and apoPiLp III = 120 kDa). The apolipoproteins are arranged in varying stoichiometries as judged by cross-linking experiments. In lipoprotein samples from individual animals, the two smaller subunits occurred in a 1:1 stoichiometry, while the relative amount of the 230 kDa peptide varied. The lipoprotein is a slightly heart-shaped HDL with a diameter of approximately 15 nm. It is pr…

PhosphatidylethanolamineMolecular massLipoproteinsBiological TransportPhosphatidylserinePhosphatidylserinesBiologybiology.organism_classificationBiochemistryMolecular WeightScorpionsPandinuschemistry.chemical_compoundHigh-density lipoproteinBiochemistrychemistryInsect SciencePhosphatidylcholineHemolymphHemolymphAnimalsInsect Proteinslipids (amino acids peptides and proteins)Molecular BiologyLipoproteinInsect biochemistry and molecular biology
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Temperature adaptation influences the aggregation state of hemocyanin from Astacus leptodactylus.

2000

When Astacus leptodactylus were kept at various temperatures for several weeks, different ratios between di-hexameric and hexameric hemocyanins were observed in their hemolymph. The higher the temperature the more hexamers were present. This long-term adaptation to different temperatures or/and to temperature-induced pH-shifts as observed in the hemolymph has different effects on the expression of subunit types building up hexamers and those which covalently link two hexamers within the di-hexamers. The oxygen binding behaviour of di-hexameric hemocyanins from cold and warm adapted animals do not show differences with respect to affinity, Bohr effect and cooperativity.

PhysiologyEcologymedicine.medical_treatmentProtein subunitTemperatureCooperativityHemocyaninBohr effectmacromolecular substancesBiologyHydrogen-Ion ConcentrationAstacus leptodactylusbiology.organism_classificationBiochemistryAdaptation PhysiologicalCrustaceaHemolymphHemocyaninsmedicineBiophysicsAnimalsElectrophoresis Polyacrylamide GelAdaptationMolecular BiologyOxygen bindingComparative biochemistry and physiology. Part A, Molecularintegrative physiology
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Origin and evolution of arthropod hemocyanins and related proteins.

2002

Arthropod hemocyanins are large, multimeric, (n x 6) copper-containing proteins that deliver oxygen in the haemolymph of many chelicerate, crustacean, myriapod, and also possibly some insect species. The arthropod hemocyanins belong to a large protein superfamily that also includes the arthropod phenoloxidases, certain crustacean and insect storage proteins (pseudo-hemocyanins and hexamerins), and the insect hexamerin receptors. Here I summarise the present knowledge of the origin, functional adaptations, and evolution of these proteins. Arthropod and mollusc hemocyanins are, if at all, only distantly related. As early as in the arthropod stem line, the hemocyanins emerged from a phenoloxid…

Physiologymedia_common.quotation_subjectProtein subunitmedicine.medical_treatmentchemical and pharmacologic phenomenaInsectBiochemistryEvolution MolecularEndocrinologyPhylogeneticsHemolymphmedicineAnimalsArthropodsEcology Evolution Behavior and SystematicsPhylogenymedia_commonbiologyfungihemic and immune systemsHemocyaninAnatomyProtein superfamilybiology.organism_classificationEvolutionary biologyHemocyaninsAnimal Science and ZoologyChelicerataArthropodJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology
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A new automated plunger for cryopreparation of proteins in defined - even oxygen free - atmospheres

2009

We study the structure and function of hemocyanins. They are giant extracellular oxygen carriers in the hemolymph of many molluscs and arthropods. Since some of these blue, copper-containing proteins show the highest cooperativity in nature (h = 10), one of our goals is to understand the chemomechanical interaction between the different substructures during allosteric oxygen binding.

PlungerchemistryAllosteric regulationHemolymphExtracellularBiophysicsAnalytical chemistrychemistry.chemical_elementCooperativityBiologyOxygenOxygen bindingStructure and function
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