Search results for "Tyrosine Kinase"

showing 10 items of 362 documents

Cloning and expression of new receptors belonging to the immunoglobulin superfamily from the marine sponge Geodia cydonium

1999

A cDNA encoding a receptor tyrosine kinase (RTK) was previously cloned and expressed from the marine sponge (Porifera) Geodia cydonium. In addition to the two intracellular regions characteristic for RTKs, two immunoglobulin (Ig)-like domains are found in the extracellular part of the sponge RTK. In the present study it is shown that no further Ig-like domain is present in the upstream region of the cDNA as well as of the gene hitherto known from the sponge RTK. Two different full-length cDNAs have been isolated and characterized in the present study, which possess two Ig-like domains, one transmembrane segment, and only a short intracellular part, without a TK domain. The two deduced polyp…

DNA ComplementaryTranscription GeneticMolecular Sequence DataImmunologyImmunoglobulinsBiologyReceptor tyrosine kinaseComplementary DNAGeneticsAnimalsHumansAmino Acid SequenceNorthern blotReceptors ImmunologicPeptide Chain Initiation TranslationalIntracellular partPolymorphism GeneticBase SequenceReceptor Protein-Tyrosine KinasesBlotting NorthernImmunohistochemistryMolecular biologyPoriferaProtein Structure TertiaryTransplantationOpen reading frameTransmembrane domainbiology.proteinImmunoglobulin superfamilyCell Adhesion MoleculesImmunogenetics
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Molecular cloning of rat G-protein-coupled receptor kinase 6 (GRK6) from brain tissue, and its mRNA expression in different brain regions and periphe…

1997

The rat G-protein-coupled receptor kinase 6 (GRK6) cDNA was cloned from rat brain tissue by a combination of reverse-transcription polymerase chain reactions (RT-PCR), based on homology to the cloned human GRK6, and rapid amplification of cDNA ends (RACE-PCR). We obtained a clone of 2817 bp with an open reading frame of 1731 bp encoding for a protein of 576 amino acids that is 96.7% identical and 97.9% similar to its human counterpart. mRNA was detectable in all brain areas examined. In addition, GRK6 was expressed in skeletal muscle, small intestine, aorta, liver, heart, lung, thymus, stomach, uterus and kidney.

DNA ComplementaryTranscription GeneticMolecular Sequence DataProtein Serine-Threonine KinasesMolecular cloningBiologyPolymerase Chain ReactionOpen Reading FramesCellular and Molecular NeuroscienceRapid amplification of cDNA endsGTP-Binding ProteinsComplementary DNAGene expressionAnimalsHumansAmino Acid SequenceRNA MessengerCloning MolecularProtein kinase AMolecular BiologyG protein-coupled receptor kinaseMessenger RNABase SequenceSequence Homology Amino AcidBrainReceptor Protein-Tyrosine KinasesG-Protein-Coupled Receptor KinasesMolecular biologyRatsOpen reading frameOrgan SpecificityFemaleSequence AlignmentMolecular Brain Research
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Characterization and phylogenetic analysis of a cDNA encoding the Fes/FER related, non-receptor protein-tyrosine kinase in the marine sponge Sycon ra…

1998

Abstract In search of ancient versions of phylogenetically conserved genes/proteins, which are typical for multicellular animals, we have decided to analyse marine sponges (Porifera), the most ancient and most primitive metazoan organisms. We report here the complete nucleotide sequence of Sycon raphanus cDNA coding for a 879 aa long protein (100 kDa), which displays high overall similarity in primary structure and organization of domains with non-receptor tyrosine kinases (TKs) from the Fes/FER family. The encoded protein, which we named Fes/FER_SR, has a highly conserved, 260 aa long tyrosine kinase domain at the C-terminus. Amino-terminal to the catalytic domain is an 85 aa long SH2 doma…

DNA Complementaryanimal structuresMolecular Sequence DataBiologySH2 domainHomology (biology)PhylogeneticsProto-Oncogene ProteinsComplementary DNAGeneticsAnimalsAmino Acid SequenceSycon raphanusPhylogenyGeneticsSequence Homology Amino AcidProtein primary structureNucleic acid sequenceSequence Analysis DNAGeneral MedicineProtein-Tyrosine Kinasesbiology.organism_classificationPoriferaBiochemistryOncogenes; Signal transduction; SH2 domain; Metazoa; Porifera; PhylogenySequence AlignmentTyrosine kinaseGene
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Immunoglobulin-like domain is present in the extracellular part of the receptor tyrosine kinase from the marine sponge Geodia cydonium.

1994

We have isolated and characterized two cDNAs from the marine sponge Geodia cydonium coding for a new member of a receptor tyrosine kinase of class II. The deduced amino acid sequence shows two characteristic domains: (i) the tyrosine kinase domain; and (ii) and immunoglobulin-like domain. The latter part shows high homology to the vertebrate C2 type immunoglobulin domain. This result demonstrates that immunoglobulin domains are not recent achievements of higher animals but exist also in those animals which have diverged from other organisms about 800 million years ago.

DNA ComplementarybiologySequence Homology Amino AcidMolecular Sequence DatamyrImmunoglobulinsReceptor Protein-Tyrosine KinasesImmunoglobulin domainSH2 domainBiological EvolutionReceptor tyrosine kinasePoriferaProtein Structure TertiaryBiochemistryStructural BiologyPhylogeneticsMultigene FamilyROR1biology.proteinAnimalsAmino Acid SequenceMolecular BiologyPeptide sequenceTyrosine kinaseSequence AlignmentJournal of molecular recognition : JMR
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Thiocarbamate-Linked Polysulfonate–Peptide Conjugates As Selective Hepatocyte Growth Factor Receptor Binders

2014

The capacity of many proteins to interact with natural or synthetic polyanions has been exploited for modulating their biological action. However, the polydispersity of these macromolecular polyanions as well as their poor specificity is a severe limitation to their use as drugs. An emerging trend in this field is the synthesis of homogeneous and well-defined polyanion–peptide conjugates, which act as bivalent ligands, with the peptide part bringing the selectivity of the scaffold. Alternately, this strategy can be used for improving the binding of short peptides to polyanion-binding protein targets. This work describes the design and first synthesis of homogeneous polysulfonate–peptide con…

DendrimersBiomedical EngineeringPharmaceutical ScienceBioengineeringPeptidemacromolecular substancesPlasma protein bindingArticleReceptor tyrosine kinaseSubstrate SpecificityStructure-Activity RelationshipThiocarbamatesmedicineHumansStructure–activity relationshipPharmacologychemistry.chemical_classificationDose-Response Relationship DrugMolecular StructurebiologyHepatocyte Growth FactorChemistryOrganic Chemistrytechnology industry and agricultureProto-Oncogene Proteins c-metProtein Structure TertiaryThiocarbamateBiochemistryHepatocyte Growth Factor ReceptorProto-Oncogene Proteins c-metbiology.proteinHepatocyte growth factorSulfonic AcidsPeptidesProtein BindingBiotechnologymedicine.drugBioconjugate Chemistry
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Gefitinib in lung cancer therapy. Clinical results, predictive markers of response and future perspectives.

2009

Over the past few years, epidermal growth factor receptor has emerged as one of the most important targets in tumorgenesis and several drugs targeting signal transduction pathways have been developed. The first among these agents to be approved for the treatment of NSCLC was gefitinib, a potent, selective and reversible inhibitor of HER1/EGFR tyrosine kinase activity. The review summarizes its clinical development and the new therapeutic options, with particular focus on predictive markers of susceptibility to this drug.

DrugOncologyCancer Researchmedicine.medical_specialtyLung Neoplasmsmolecular markersmedia_common.quotation_subjectgefitinibAntineoplastic AgentsGefitinibcancer therapyGefitinibCarcinoma Non-Small-Cell LungInternal medicinetyrosine kinase inhibitorsmedicineAnimalsHumansgefitinib; non-small cell lung cancer (NSCLC); epidermal growth factor receptor (HER1/EGFR); tyrosine kinase inhibitors; target therapy; molecular markers; EGFR mutationsEpidermal growth factor receptorLung cancermedia_commonPharmacologyClinical Trials as Topicbiologybusiness.industrytarget therapymedicine.diseaseEGFR mutationsepidermal growth factor receptor (HER1/EGFR)ErbB Receptorsnon-small cell lung cancer (NSCLC)OncologyQuinazolinesbiology.proteinMolecular MedicineSignal transductionbusinessBiomarkersEgfr tyrosine kinaseSignal Transductionmedicine.drug
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Tributyltin chloride-induced effects on protein tyrosine phosphorylation and on extracellular-signal-regulated kinase (ERK) phosphorilation in Ascidi…

2011

Ascidians represent an intriguing candidate experimental system for studying the effects of environmental stress. We studied TBT effects and probable related pathways were investigated on ascidian embryos by using Western immunoblotting. Among the various signal transduction pathways involved in response to environmental stress, both tyrosine kinase signalling and MAPKs have been played a significant role. To better understand molecular mechanisms after exposure to TBT we studied the two signal transduction pathways above mentioned. Attempting to unravel the molecular effects of TBT-induced on ascidians embryogenesis, TBT treatments carried out in Phallusia mammillata embryos at gastrula st…

ERK (p44/42)Settore BIO/13 - Biologia ApplicataTyrosine kinase signallingAscidian embryos.Tributyltin-induced effectMAPK
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Effects of tributyltin chloride in ascidian embryos: modulation of kinase-mediated signalling pathways

2009

We studied the effects of various TBT concentrations by assaying the activity of ERK 1/2 (p44/42) and phospho-ERK1/2 (phospho-p44/42), proteins with a key role in ascidian development, and tyrosine kinase-dependent pathway. The effects of this xenobiotic and the role of some signalling mechanisms on ascidian embryos were examined by using Western immunoblotting. The tyrosine phosphorylation pattern in the ascidians Ciona intestinalis and Phallusia mammillata development was examined and different levels of protein phosphorylation were found as a response to TBT at μM range. To determine whether another key signalling pathway was activated, the effects of TBT on the phosphorylation state of …

ERK (p44/42)tributyltin-induced effectanimal structureslcsh:Biology (General)tyrosine kinase signallingembryonic structuresascidian embryoslcsh:QH301-705.5MAPK
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The protein tyrosine kinase Tec regulates a CD44highCD62L- Th17 subset.

2010

Abstract The generation of Th17 cells has to be tightly controlled during an immune response. In this study, we report an increase in a CD44highCD62L− Th17 subset in mice deficient for the protein tyrosine kinase Tec. CD44highCD62L− Tec−/− CD4+ T cells produced enhanced IL-17 upon activation, showed increased expression levels of IL-23R and RORγt, and IL-23–mediated expansion of Tec−/− CD4+ T cells led to an increased production of IL-17. Tec−/− mice immunized with heat-killed Streptococcus pneumoniae displayed increased IL-17 expression levels in the lung postinfection with S. pneumoniae, and this correlated with enhanced pneumococcal clearance and reduced lung inflammation compared with T…

Encephalomyelitis Autoimmune ExperimentalTECeducationImmunologyImmunoblottingInflammationEnzyme-Linked Immunosorbent AssayCell SeparationBiologyMiceImmune systemIn vivoRAR-related orphan receptor gammaT-Lymphocyte SubsetsmedicineImmunology and AllergyAnimalsCell LineageL-SelectinMice KnockoutReverse Transcriptase Polymerase Chain ReactionCD44Interleukin-17hemic and immune systemsCell DifferentiationPneumoniaT-Lymphocytes Helper-InducerProtein-Tyrosine KinasesFlow CytometryMolecular biologyHyaluronan ReceptorsCancer researchbiology.proteinCytokinesmedicine.symptomSignal transductiontissuesTyrosine kinaseSignal TransductionJournal of immunology (Baltimore, Md. : 1950)
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E-selectin modulates the malignant properties of T84 colon carcinoma cells.

2002

The extravasation of metastatic cells is regulated by molecular events involving the initial adhesion of tumor cells to the endothelium and subsequently the migration of cells in the host connective tissue. E-selectin on endothelial cells and sialyl Lewis X carbohydrate component on tumor cells are mainly involved in the adhesion of colon carcinoma cells to the endothelium of target organ. Interaction of T84 colon cancer cells to purified E-selectin in vitro caused an increase in the tyrosine phosphorylation of a number of proteins as well as the modulation of cellular properties correlated to the metastatic phenotype. Specifically, E-selectin-stimulated actin reorganization, increased coll…

EndotheliumLactams MacrocyclicBiophysicsOligosaccharidesBiologyBiochemistryCell–cell interactionCancer stem cellCell MovementE-selectinmedicineBenzoquinonesCell AdhesionTumor Cells CulturedHumansEnzyme InhibitorsNeoplasm MetastasisPhosphorylationCell adhesionPhosphotyrosineSialyl Lewis X AntigenMolecular BiologyCells CulturedCarcinomaSoluble cell adhesion moleculesQuinonesCell migrationCell BiologyProtein-Tyrosine KinasesPhosphoproteinsCoculture TechniquesCell biologymedicine.anatomical_structureRifabutinCancer cellColonic NeoplasmsCancer researchbiology.proteinMatrix Metalloproteinase 2Endothelium VascularE-SelectinBiochemical and biophysical research communications
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