Search results for "Tissue distribution"

showing 10 items of 240 documents

Synthesis and biopharmaceutical characterisation of new poly(hydroxyethylaspartamide) copolymers as drug carriers.

2001

Abstract Four new poly(hydroxyethylaspartamide)-based copolymers bearing (a) poly(ethylene glycol) 2000, (b) poly(ethylene glycol) 5000, (c) poly(ethylene glycol) 2000 and hexadecylalkyl, (d) poly(ethylene glycol) 5000 and hexadecylalkyle, as pendant groups were synthesised. The copolymers were obtained by partial aminolysis of polysuccinimide with poly(ethylene glycol) and hexadecylalkyl amino derivatives followed by reaction with ethanolamine. Naked polyhydroxyaspartamide was obtained by polysuccinimide reaction with ethanolamine. The nuclear magnetic resonance, infrared, light scattering and elemental analysis allowed for the extensive physico-chemical characterisation of the carriers. T…

chemistry.chemical_classificationBiodistributionDrug CarriersMagnetic Resonance SpectroscopySpectrophotometry InfraredPolymersBiophysicsPolymerBiochemistryPolyethylene Glycolschemistry.chemical_compoundMiceAminolysisEthanolaminechemistryNeoplasmsPolymer chemistryCopolymerAnimalsTissue DistributionDrug carrierPeptidesMolecular BiologyEthylene glycolConjugateBiochimica et biophysica acta
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Biochemical identification and tissue-specific expression patterns of keratins in the zebrafish Danio rerio

1998

We have identified a number of type I and type II keratins in the zebrafish Danio rerio by two-dimensional polyacrylamide gel electrophoresis, complementary keratin blot-binding assay and immunoblotting. These keratins range from 56 kDa to 46 kDa in molecular mass and from pH 6.6 to pH 5.2 in isoelectric point. Type II zebrafish keratins exhibit significantly higher molecular masses (56-52 kDa) compared with the type I keratins (50-48 kDa), but the isoelectric points show no significant difference between the two keratin subclasses (type II: pH 6.0-5.5; type I: pH 6.1-5.2). According to their occurrence in various zebrafish tissues, the identified keratins can be classified into "E" (epider…

chemistry.chemical_classificationanimal structuresHistologyintegumentary systembiologyMolecular massCellular differentiationDanioCell Biologybiology.organism_classificationMolecular biologyPathology and Forensic MedicineIsoelectric pointMicroscopy FluorescenceBiochemistrychemistryGenetic modelKeratinAnimalsKeratinsTissue DistributionPolyacrylamide gel electrophoresisZebrafishCytoskeletonZebrafishCell and Tissue Research
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A plasma protein corona enhances the biocompatibility of Au@Fe3O4 Janus particles

2015

AbstractAu@Fe3O4 Janus particles (JPs) are heteroparticles with discrete domains defined by different materials. Their tunable composition and morphology confer multimodal and versatile capabilities for use as contrast agents and drug carriers in future medicine. Au@Fe3O4 JPs have colloidal properties and surface characteristics leading to interactions with proteins in biological fluids. The resulting protein adsorption layer (“protein corona”) critically affects their interaction with living matter. Although Au@Fe3O4 JPs displayed good biocompatibility in a standardized in vitro situation, an in-depth characterization of the protein corona is of prime importance to unravel underlying mecha…

endocrine systemMaterials scienceBiocompatibilitySurface PropertiesJanus particlesBiophysicsContrast MediaJanus particlesProtein CoronaNanotechnologyBioengineeringMultimodal ImagingNanocapsulesBiomaterialsMiceCoated Materials BiocompatibleNanocapsulesAnimalsHumansTissue DistributionNanotoxicityParticle SizeMagnetite NanoparticlesEndothelial CellsBlood ProteinsAdhesionMagnetic Resonance ImagingNanomedicineProtein coronaNanotoxicologyMechanics of MaterialsIn vivo imagingBiophysicsCeramics and CompositesAdsorptionGoldParticle sizeTomography X-Ray ComputedProtein adsorptionBiomaterials
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Neuropeptide Y (NPY)-like immunoreactivity in the guinea pig pineal organ.

1986

Relatively little is known about mammalian pineal neuropeptides. In the present study neuropeptide Y-like immunoreactivity (NPY-LI) was examined in the guinea pig pineal gland. NPY-LI was restricted to few intrapineal nerve fibers of faint fluorescence intensity. They showed no preferential localization with regard to the different pineal portions. As catecholaminergic fibers are abundant in the guinea pig pineal gland, the scarcity of NPY-LI fibers indicates that in the pineal colocalization of noradrenaline and NPY-LI is not a regular feature, in contrast to other organs. The possibility exists that in the pineal NPY-LI fibers are not of peripheral sympathetic but of central origin.

endocrine systemmedicine.medical_specialtyGuinea PigsNeuropeptideFluorescent Antibody TechniqueNerve Tissue ProteinsBiologyPineal GlandTrypsin like enzymeGuinea pigPineal glandNerve FibersInternal medicinemental disordersmedicineAnimalsNeuropeptide YTissue DistributionCatecholaminergicGeneral NeuroscienceColocalizationNeuropeptide Y receptorhumanitiesEndocrinologymedicine.anatomical_structurenervous systemPineal organhormones hormone substitutes and hormone antagonistsNeuroscience letters
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Evaluation of a novel monoclonal antibody against tumor-associated MUC1 for diagnosis and prognosis of breast cancer

2019

There is still a great unmet medical need concerning diagnosis and treatment of breast cancer which could be addressed by utilizing specific molecular targets. Tumor-associated MUC1 is expressed on over 90 % of all breast cancer entities and differs strongly from its physiological form on epithelial cells, therefore presenting a unique target for breast cancer diagnosis and antibody-mediated immune therapy. Utilizing an anti-tumor vaccine based on a synthetically prepared glycopeptide, we generated a monoclonal antibody (mAb) GGSK-1/30, selectively recognizing human tumor-associated MUC1. This antibody targets exclusively tumor-associated MUC1 in the absence of any binding to MUC1 on health…

medicine.drug_classEstrogen receptorMUC1Breast NeoplasmsMice TransgenicDeferoxamineMonoclonal antibody89Zr03 medical and health sciences0302 clinical medicineBreast cancerIn vivoCell Line TumorBiomarkers TumormedicineAnimalsHumansTissue Distributionskin and connective tissue diseasesMUC1Triple-negative breast cancermAbRadioisotopesMice Inbred BALB Cbiologybusiness.industryMucin-1breast cancer diagnosisAntibodies MonoclonalCancerGeneral MedicinePrognosismedicine.diseaseImmunohistochemistryMice Inbred C57BLPositron-Emission Tomographybiology.proteinCancer researchFemale030211 gastroenterology & hepatologyZirconiumAntibodybusinessResearch PaperInternational Journal of Medical Sciences
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The L-glutamate transporters GLAST (EAAT1) and GLT-1 (EAAT2): expression and regulation in rat lactating mammary gland.

1999

The Na(+)-dependent L-glutamate transporters GLAST (EAAT1) and GLT-1 (EAAT2), were expressed in rat lactating mammary gland, but EAAC1 (EAAT3) was not. GLT-1 expression in rat lactating mammary gland was constant in all the physiological situations studied; however, the GLAST expression is under tight regulation. Fasting for 24 h decreased the GLAST expression which returned to control values after refeeding. Weaning for 24 h produced a decrease in GLAST expression through a mechanism independent of prolactin deficiency. Resuckling for 6 h returned the expression of this transporter to control values. There is a correlation between the levels of GLAST (mRNA and protein) and the in vivo upta…

medicine.medical_specialtyAmino Acid Transport System X-AGMammary glandBlotting WesternMammary Glands AnimalIn vivoInternal medicineLactationmedicineWeaningAnimalsLactationTissue DistributionRats WistarMolecular BiologyMessenger RNAChemistryReverse Transcriptase Polymerase Chain ReactionTransporterProlactin deficiencyCell BiologyBlotting NorthernRatsBlotmedicine.anatomical_structureEndocrinologyATP-Binding Cassette TransportersFemaleMolecular membrane biology
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Expression of inhibitory glycine receptors in postnatal rat cerebral cortex.

1993

The developmental expression of inhibitory glycine receptors was analyzed in postnatal rat cerebral cortex using the specific monoclonal antibody, MAb 4a. This antibody defines an epitope common to all known glycine receptor alpha-subunits. At birth, high levels of immunoreactivity were found, which transiently increased during the second postnatal week, but subsequently declined to low adult levels. Biochemical analysis of the MAb 4a antigen from parietal areas indicates that cortical glycine receptors correspond to the neonatal receptor isoform previously identified in spinal cord of newborn animals. Immunocytochemistry showed that, within 2 weeks after birth, MAb 4a-reactive glycine rece…

medicine.medical_specialtyCentral nervous systemImmunocytochemistryBlotting WesternBiologyRats Sprague-Dawleychemistry.chemical_compoundReceptors GlycineInternal medicineCortex (anatomy)medicineAnimalsTissue DistributionReceptorMolecular BiologyGlycine receptorCerebral CortexGeneral NeuroscienceAntibodies MonoclonalNeural InhibitionStrychnineImmunohistochemistryRatsReceptors Neurotransmittermedicine.anatomical_structureEndocrinologychemistryAnimals NewbornCerebral cortexImmunologyGlycineNeurology (clinical)Developmental BiologyBrain research
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Distribution of Met-enkephalyl-Arg-Gly-Leu in rat larynx: partial coexistence with vasoactive intestinal polypeptide, peptide histidine isoleucine an…

1990

Abstract Using light microscopic (LM) enzyme-immunohistochemistry on deparaffinized adjacent sections Met-enkephalyl-Arg-Gly-Leu (ME-RGL) immunoreactivity was found to partially coexist with immunoreactive neuropeptide Y (NPY), vasoactive intestinal polypeptide (VIP) and peptide histidine isoleucine (PHI) in intrinsic laryngeal neurons of the rat. Further ME-RGL-immunoreactive (ir) fibres were found around glands in the subepithelium, in connective tissue of striated muscle and in the perichondrium, as well as around arterial and venous blood vessels. They frequently contacted mast cells and macrophages. The presence of ME-RGL indicates pro-enkephalin-related origin of this novel laryngeal …

medicine.medical_specialtyEnkephalin MethionineVasoactive intestinal peptideConnective tissueNeuropeptideCalcitonin gene-related peptideBiologyNerve FibersPeptide PHIInternal medicinemedicineAnimalsNeuropeptide YTissue DistributionGeneral NeuroscienceNeuropeptidesLaryngeal NervesPeptide PHINeuropeptide Y receptorRatsmedicine.anatomical_structureEndocrinologyCalcitoninPeripheral nervous systemGangliaLarynxVasoactive Intestinal PeptideNeuroscience letters
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Cloning of two melanocortin (MC) receptors in spiny dogfish

2004

We report the cloning and characterization of two melanocortin receptors (MCRs) from the spiny dogfish (Squalus acanthias) (Sac). Phylogenetic analysis shows that these shark receptors are orthologues of the MC3R and MC5R subtypes, sharing 65% and 70% overall amino acid identity with the human counterparts, respectively. The SacMC3R was expressed and pharmacologically characterized in HEK293 cells. The radioligand binding results show that this receptor has high affinity for adrenocorticotropic hormone (ACTH)-derived peptides while it has comparable affinity for alpha- and beta-melanocyte stimulating hormone (MSH), and slightly lower affinity for gamma-MSH when compared with the human ortho…

medicine.medical_specialtyGreen Fluorescent ProteinsMolecular Sequence DataCHO CellsAdrenocorticotropic hormoneBiologyPolymerase Chain ReactionBiochemistryCell LineRadioligand Assaygamma-MSHAdrenocorticotropic HormoneCricetinaeInternal medicineCyclic AMPEscherichia colimedicineAnimalsHumansPotencyBacteriophagesTissue DistributionAmino Acid SequenceMelanocyte-Stimulating HormonesCloning MolecularReceptorPhylogenyGene Librarychemistry.chemical_classificationSpiny dogfishDose-Response Relationship DrugSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionChinese hamster ovary cellHEK 293 cellsSequence Analysis DNAbiology.organism_classificationMolecular biologyIntronsAmino acidBlotting SouthernKineticsEndocrinologychemistryDogfishReceptor Melanocortin Type 4MelanocortinPeptidesReceptor Melanocortin Type 3European Journal of Biochemistry
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Pharmacological characterization and autoradiographic localization of histamine H2 receptors in human brain identified with [125I]iodoaminopotentidin…

1992

125I-Aminopotentidine (125I-APT), a reversible probe of high specific radioactivity and high affinity and selectivity for the H2 receptor, was used to characterize and localize this histamine receptor subtype in human brain samples obtained at autopsy. On membranes of human caudate nucleus, specific 125I-APT binding at equilibrium revealed a single component, with a dissociation constant of 0.3 nM and maximal capacity of about 100 fmol/mg of protein. At 0.2 nM, 125I-APT specific binding, as defined with tiotidine, an H2-receptor antagonist chemically unrelated to iodoaminopotentidine, represented 40-50% of the total. Specific 125I-APT binding was inhibited by a series of typical H2-receptor…

medicine.medical_specialtyHistamine H1 receptorHippocampal formationBiologyBiochemistryGuanidinesIodine RadioisotopesCellular and Molecular Neurosciencechemistry.chemical_compoundHistamine receptorHistamine H2 receptorInternal medicinemedicineHumansReceptors Histamine H2Tissue DistributionReceptorHistaminergicBrainHuman brainEndocrinologymedicine.anatomical_structurechemistryHistamine H2 AntagonistsAutoradiographyHistamineJournal of neurochemistry
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