Search results for "Blood Protein"

showing 10 items of 175 documents

Exposure to increased ambient ultraviolet B radiation has negative effects on growth, condition and immune function of juvenile Atlantic salmon (Salm…

2008

Atlantic salmon (Salmo salar) parr were exposed in two outdoor experiments, ranging in duration from 52 to 137 days, to spectral treatments: (1) natural sunlight (=present ambient UVB level), (2) solar radiation supplemented with enhanced UVB radiation from lamps simulating 20% or 8% stratospheric ozone loss or (3) UVB-depleted sunlight achieved by screening with Mylar-D film. The growth, condition and immune function of the salmon were quantified after treatments. Exposure to enhanced UVB radiation retarded growth, and decreased hematocrit value and plasma protein concentration. Further, enhanced UVB radiation affected plasma immunoglobulin concentration. The results demonstrate that juven…

Ultraviolet Raysanimal diseasesSalmo salarImmunoglobulinsBiologyHematocritBiochemistryAnimal scienceImmune systemRetarded growthmedicineJuvenileAnimalsPhysical and Theoretical ChemistrySalmoskin and connective tissue diseasesGrowth DisordersSunlightintegumentary systemmedicine.diagnostic_testEcologyGeneral Medicinebiology.organism_classificationBlood proteinsUltraviolet B radiationHematocritSpectrophotometry UltravioletPhotochemistry and photobiology
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Heparin-binding protein targeted to mitochondrial compartments protects endothelial cells from apoptosis.

1999

Neutrophil-borne heparin-binding protein (HBP) is a multifunctional protein involved in the progression of inflammation. HBP is stored in neutrophil granules and released upon stimulation of the cells in proximity to endothelial cells. HBP affects endothelial cells in multiple ways; however, the molecular and cellular mechanisms underlying the interaction of HBP with these cells are unknown. Affinity isolation and enzymatic degradation demonstrated that HBP released from human neutrophils binds to endothelial cell-surface proteoglycans, such as syndecans and glypican. Flow cytometry indicated that a significant fraction of proteoglycan-bound HBP is taken up by the endothelial cells, and we …

Umbilical VeinsEndotheliumCell SurvivalNeutrophilsmedia_common.quotation_subjectmedicine.medical_treatmentInflammationApoptosisBiologyFibroblast growth factorLeukotriene B4ArticleChromatography AffinityFlow cytometryParacrine CommunicationLeukocytesmedicineAnimalsHumansInternalizationCells Culturedmedia_commonInflammationmedicine.diagnostic_testHeparinMonocyteGrowth factorBiological TransportGeneral MedicineBlood ProteinsMolecular biologyRecombinant ProteinsMitochondriaN-Formylmethionine Leucyl-PhenylalanineKineticsmedicine.anatomical_structureApoptosisCommentaryTetradecanoylphorbol AcetateProteoglycansEndothelium Vascularmedicine.symptomCarrier ProteinsAntimicrobial Cationic PeptidesThe Journal of clinical investigation
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Nonradical oxidants of the phagocyte type induce the activation of plasmatic single chain- urokinase

1991

Single chain- urokinase (scu-PA) is the proenzyme of the plasminogen activator urokinase (tcu-PA). In human blood scu-PA is of great stability. Activated phagocytes generate large amounts of single chain- urokinase and of reactive oxidants (chloramines and HOCl). Since these cells participate in physiologic fibrinolysis, we were interested in the interaction between plasmatic scu-PA and chloramines. The oxidants dose dependently induce the activation of plasmatic scu-PA. Optimal activation of scu-PA occurs at about 3-5 mmol/l of chloramine-T. The findings suggest a control mechanism of scu-PA stability/activity by oxidatively modifiable plasma proteins, such as alpha-2-antiplasmin. The oxid…

UrokinasePhagocytemedicine.medical_treatmentchemistry.chemical_elementHematologyBlood proteinsOxygenEnzyme activatormedicine.anatomical_structureBiochemistrychemistryFibrinolysismedicineAutacoidPlasminogen activatormedicine.drugThrombosis Research
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Hereditary combined deficiency of the vitamin K-dependent clotting factors

2010

Abstract Hereditary combined vitamin K-dependent clotting factors deficiency (VKCFD) is a rare congenital bleeding disorder resulting from variably decreased levels of coagulation factors II, VII, IX and X as well as natural anticoagulants protein C, protein S and protein Z. The spectrum of bleeding symptoms ranges from mild to severe with onset in the neonatal period in severe cases. The bleeding symptoms are often life-threatening, occur both spontaneously and in a surgical setting, and usually involve the skin and mucosae. A range of non-haemostatic symptoms are often present, including developmental and skeletal anomalies. VKCFD is an autosomal recessive disorder caused by mutations in …

Vitaminmedicine.medical_specialtyVitamin KCoagulation Factor Deficiencylcsh:MedicineReviewGastroenterologyProtein SProtein SSettore MED/15 - Malattie Del Sanguechemistry.chemical_compoundBlood Coagulation Disorders InheritedInternal medicineVitamin K deficiencymedicineHumansGenetics(clinical)Pharmacology (medical)VITAMIN K DEPENDENT CLOTTING FACTORS RARE INHERITED BLEEDING DISORDERSCongenital Bleeding DisorderGenetics (clinical)Medicine(all)Clotting factorbiologybusiness.industrylcsh:RVitamin K2WarfarinInfant NewbornGeneral MedicineBlood Proteinsmedicine.diseaseBlood Coagulation FactorsRecombinant ProteinschemistryCarbon-Carbon LigasesImmunologybiology.proteinVitamin K Deficiencybusinessmedicine.drugProtein C
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Cloning and Targeted Deletion of the Mouse Fetuin Gene

1998

We proposed that the alpha2-Heremans Schmid glycoprotein/fetuin family of serum proteins inhibits unwanted mineralization. To test this hypothesis in animals, we cloned the mouse fetuin gene and generated mice lacking fetuin. The gene consists of seven exons and six introns. The cystatin-like domains D1 and D2 of mouse fetuin are encoded by three exons each, whereas a single terminal exon encodes the carboxyl-terminal domain D3. The promoter structure is well conserved between rat and mouse fetuin genes within the regions shown to bind transcription factors in the rat system. Expression studies demonstrated that mice homozygous for the gene deletion lacked fetuin protein and that mice heter…

alpha-2-HS-GlycoproteinMolecular Sequence DataBiologyBiochemistryMiceEctopic calcificationExonCalcification PhysiologicApatitesmedicineAnimalsCloning MolecularPromoter Regions GeneticMolecular BiologyGeneMice Knockoutchemistry.chemical_classificationBase SequenceIntronBlood ProteinsSequence Analysis DNACell Biologymedicine.diseaseNull alleleMolecular biologyFetuinRatschemistryFemalealpha-FetoproteinsGlycoproteinalpha-2-HS-glycoproteinGene DeletionJournal of Biological Chemistry
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Rat tyrosine kinase inhibitor shows sequence similarity to human α2-HS glycoprotein and bovine fetuin

1991

Human alpha 2-HS glycoprotein and bovine fetuin, abundant proteins of fetal plasma, are structural members of the fetuin family within the cystatin superfamily. They are characterized by the presence of two N-terminally located cystatin-like units and a unique C-terminal sequence segment not present in the other members of the cystatin superfamily. Search for related sequences revealed that the natural inhibitor of the insulin receptor tyrosine kinase [Auberger, Falquerho, Contreres, Pages, Le Cam, Rossi & Le Cam (1989) Cell (Cambridge, Mass.) 58, 631-640] shows sequence similarity to the mammalian fetuins. The sequence identity between rat tyrosine kinase inhibitor, human alpha 2-HS gl…

alpha-2-HS-Glycoproteinmedicine.drug_classMolecular Sequence DataBiochemistryTyrosine-kinase inhibitorReceptor tyrosine kinaseHomology (biology)Protein structureSequence Homology Nucleic AcidmedicineAnimalsHumansAmino Acid SequenceMolecular Biologychemistry.chemical_classificationbiologyBlood ProteinsCell BiologyProtein-Tyrosine KinasesMolecular biologyFetuinRatschemistryBiochemistrybiology.proteinCattlealpha-FetoproteinsGlycoproteinSequence Alignmentalpha-2-HS-glycoproteinResearch ArticleCysteineBiochemical Journal
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The Complement System: Activation and Control

1985

One of the hallmarks of immunology has been analysis and characterization of the C system in biological fluids. It is composed of 11 proteins of the “classical” pathway:1 C1q, C1r, C1s, C4, C2, C3, C5, C6, C7, C8, and C9. There are three proteins of the “alternative” pathway (IUIS-WHO Nomenclature Committee 1981) B, D, and P. Finally, there are four control proteins: C1 inhibitor (Cl¯ INH) and C4b binding protein (C4b-bp) for the classical pathway, I (C3b inactivator or C3b INA) and H (β1 or C3b INA accelerator) for the alternative pathway, and anaphylatoxin inactivator. Due to the dramatic advances in protein chemistry, these 19 distinct serum proteins have been highly purified and charact…

biologyC4b-binding proteinChemistrychemical and pharmacologic phenomenaBlood proteinsComplement systemC1-inhibitorClassical complement pathwayBiochemistryImmunologybiology.proteinAlternative complement pathwayLysine carboxypeptidaseComplement membrane attack complex
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Interactions between proteins and poly(ethylene-glycol) investigated using molecular dynamics simulations

2017

Poly(ethylene-glycol) (PEG) is a polymer used to coat therapeutic preparations, like drugs or drug nanocarriers, and improve their efficacy. This effect is probably due to a reduction of the interactions of the coated species with the host organism. Nevertheless, experiments show that PEGylated materials do interact with the surrounding biological milieu, and in particular with blood proteins. Here, we use atomistic molecular dynamics simulations to characterize the interactions between the polymer and several blood proteins. In these simulations, the proteins are immersed in a mixture of PEG and water molecules. We observe how PEG distributes around the protein surface and measure PEG-prot…

chemistry.chemical_classificationHistoryPoly ethylene glycoltechnology industry and agriculturemacromolecular substances02 engineering and technologyPolymer010402 general chemistry021001 nanoscience & nanotechnology01 natural sciencesBlood proteins0104 chemical sciencesComputer Science ApplicationsEducationMolecular dynamicschemistryHost organismPEG ratioBiophysicsMoleculeNanocarriers0210 nano-technologyJournal of Physics: Conference Series
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Interactions Between Blood Proteins and Nanoparticles Investigated Using Molecular Dynamics Simulations

2019

In the development of new therapeutic agents based on nanoparticles it is of fundamental importance understanding how these substances interact with the underlying biological milieu. Our research is focussed on simulating in silico these interactions using accurate atomistic models, and gather from these information general pictures and simplified models of the underlying phenomena. Here we report results about the interactions of blood proteins with promising hydrophilic polymers used for the coating of therapeutic nanoparticles, about the salt dependent behavior of one of these polymers (poly-(ethylene glycol)) and about the interactions of blood proteins with silica, one of the most used…

chemistry.chemical_classificationIn silicoNanoparticleSalt (chemistry)Polymerengineering.materialBlood proteinschemistry.chemical_compoundMolecular dynamicschemistryCoatingChemical engineeringengineeringEthylene glycol
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Blood Proteins and Their Interactions with Nanoparticles Investigated Using Molecular Dynamics Simulations

2018

Blood proteins play a fundamental role in determining the response of the organism to the injection of drugs or, more in general, of therapeutic preparations in the blood stream. Some of these proteins are responsible for mediating immune response and coagulation. Nanoparticles, which are being intensely investigated as possible drug nanocarriers, heavily interact with blood proteins and their ultimate fate is determined by these interactions. Here we report the results of molecular dynamics simulations of several blood proteins aimed to determining their possible behavior at the nanoparticle surface. On one hand we investigated the behavior of fibrinogen, a glycoprotein, which polymerizes …

chemistry.chemical_classificationbiologyNanoparticleFibrinogenBlood proteinsFibrinMolecular dynamicschemistrybiology.proteinmedicineBiophysicsCoagulation (water treatment)NanocarriersGlycoproteinmedicine.drug
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