Search results for "Ectodomain"

showing 10 items of 29 documents

The Intracellular Cleavage Product of the NG2 Proteoglycan Modulates Translation and Cell-Cycle Kinetics via Effects on mTORC1/FMRP Signaling

2018

The NG2 proteoglycan is expressed by oligodendrocyte precursor cells (OPCs) and is abundantly expressed by tumors such as melanoma and glioblastoma. Functions of NG2 include an influence on proliferation, migration and neuromodulation. Similar to other type-1 membrane proteins, NG2 undergoes proteolysis, generating a large ectodomain, a C-terminal fragment (CTF) and an intracellular domain (ICD) via sequential action of α- and γ-secretases which is enhanced by neuronal activity. Functional roles of NG2 have so far been shown for the full-length protein, the released ectodomain and CTF, but not for the ICD. In this study, we characterized the role of the NG2 ICD in OPC and Human Embryonic Ki…

0301 basic medicinePopulationP70-S6 Kinase 1mTORC1γ-secretaselcsh:RC321-57103 medical and health sciencesCellular and Molecular NeuroscienceNG2educationlcsh:Neurosciences. Biological psychiatry. NeuropsychiatryPI3K/AKT/mTOR pathwayOriginal Researcheducation.field_of_studyChemistryICDHEK 293 cellsTranslation (biology)S6K1Cell biologystomatognathic diseases030104 developmental biologyEctodomainnervous systemeEF2mTORPhosphorylationFMRPOPCNeuroscienceFrontiers in Cellular Neuroscience
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Phosphorylation of meprin β controls its cell surface abundance and subsequently diminishes ectodomain shedding

2021

Meprin β is a zinc-dependent metalloprotease exhibiting a unique cleavage specificity with strong preference for acidic amino acids at the cleavage site. Proteomic studies revealed a diverse substrate pool of meprin β including the interleukin-6 receptor (IL-6R) and the amyloid precursor protein (APP). Dysregulation of meprin β is often associated with pathological conditions such as chronic inflammation, fibrosis, or Alzheimer's disease (AD). The extracellular regulation of meprin β including interactors, sheddases, and activators has been intensively investigated while intracellular regulation has been barely addressed in the literature. This study aimed to analyze C-terminal phosphorylat…

0301 basic medicineProtein Kinase C-alphaImmunoprecipitationmedia_common.quotation_subjectBiochemistry03 medical and health sciences0302 clinical medicineProtein Kinase C betaTumor Cells CulturedGeneticsAmyloid precursor proteinHumansPhosphorylationInternalizationMolecular BiologyProtein kinase Cmedia_commonbiologyChemistryCell MembraneMetalloendopeptidasesSheddaseCell biology030104 developmental biologyGene Expression RegulationEctodomainColonic NeoplasmsProteolysisbiology.proteinPhosphorylationExtracellular Space030217 neurology & neurosurgeryIntracellularBiotechnologyThe FASEB Journal
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Quantitative Proteomics Reveals Changes Induced by TIMP-3 on Cell Membrane Composition and Novel Metalloprotease Substrates

2021

Ectodomain shedding is a key mechanism of several biological processes, including cell-communication. Disintegrin and metalloproteinases (ADAMs), together with the membrane-type matrix metalloproteinases, play a pivotal role in shedding transmembrane proteins. Aberrant shedding is associated to several pathological conditions, including arthritis. Tissue inhibitor of metalloproteases 3 (TIMP-3), an endogenous inhibitor of ADAMs and matrix metalloproteases (MMPs), has been proven to be beneficial in such diseases. Thus, strategies to increase TIMP-3 bioavailability in the tissue have been sought for development of therapeutics. Nevertheless, high levels of TIMP-3 may lead to mechanism-based …

0301 basic medicineProteomicsADAM15ProteomeCellMatrix metalloproteinaseMass SpectrometryCell membranelcsh:Chemistryanalysis [Proteome]lcsh:QH301-705.5proteomicSpectroscopybiologyChemistrytissue inhibitor of metalloproteases 3 (TIMP-3)General MedicineTransmembrane proteinComputer Science ApplicationsCell biologymedicine.anatomical_structureEctodomainddc:540TIMP3 protein humanmetalloproteinaseectodomain sheddingmetabolism [Tissue Inhibitor of Metalloproteinase-3]Quantitative proteomicsADAM15 protein humanchemistry [Cell Membrane]Catalysismetabolism [Cell Membrane]ArticlemetalloproteinasesInorganic Chemistry03 medical and health sciencestissue inhibitor of metalloproteases 3 (TIMP-3).medicineDisintegrinHumansPhysical and Theoretical ChemistryMolecular BiologyTissue Inhibitor of Metalloproteinase-3030102 biochemistry & molecular biologyOrganic ChemistryCell MembraneMembrane Proteinsmetabolism [Proteome]ADAM Proteins030104 developmental biologyHEK293 Cellslcsh:Biology (General)lcsh:QD1-999metabolism [ADAM Proteins]biology.proteinmetabolism [Membrane Proteins]International Journal of Molecular Sciences
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Endogenous β-neurexins on axons and within synapses show regulated dynamic behavior

2021

Summary: Neurexins are key organizer molecules that regulate synaptic function and are implicated in autism and schizophrenia. β-neurexins interact with numerous cell adhesion and receptor molecules, but their neuronal localization remains elusive. Using single-molecule tracking and high-resolution microscopy to detect neurexin1β and neurexin3β in primary hippocampal neurons from knockin mice, we demonstrate that endogenous β-neurexins are present in fewer than half of excitatory and inhibitory synapses. Moreover, we observe a large extrasynaptic pool of β-neurexins on axons and show that axonal β-neurexins diffuse with higher surface mobility than those transiently confined within synapses…

0301 basic medicineQH301-705.5Green Fluorescent ProteinsNerve Tissue ProteinsEndogenyHippocampal formationNeurotransmissionGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicineProtein DomainsAnimalsPremovement neuronal activityneurotransmissionBiology (General)synaptic functionCell adhesionelectron microscopyintegumentary systemChemistryCell MembranefungiGlutamate receptorcell adhesionproteaseAxonsCell biologyMice Inbred C57BL030104 developmental biologyEctodomainProteolysisSynapsesExcitatory postsynaptic potentialsingle-particle tracking030217 neurology & neurosurgeryCell Reports
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Usherin defects lead to early-onset retinal dysfunction in zebrafish

2018

Mutations in USH2A are the most frequent cause of Usher syndrome and autosomal recessive nonsyndromic retinitis pigmentosa. To unravel the pathogenic mechanisms underlying USH2A-associated retinal degeneration and to evaluate future therapeutic strategies that could potentially halt the progression of this devastating disorder, an animal model is needed. The available Ush2a knock-out mouse model does not mimic the human phenotype, because it presents with only a mild and late-onset retinal degeneration. Using CRISPR/Cas9-technology, we introduced protein-truncating germline lesions into the zebrafish ush2a gene (ush2a(rmc1): c.2337_2342delinsAC; p.Cys780GlnfsTer32 and ush2a(b1245): c.15520_…

0301 basic medicineRetinal degenerationGenotyping TechniquesUsher syndrome2804 Cellular and Molecular NeuroscienceApoptosis030105 genetics & heredityBiologyArticleRetinaGermlineSensory disorders Donders Center for Medical Neuroscience [Radboudumc 12]Gene Knockout Techniques03 medical and health sciencesCellular and Molecular NeuroscienceUSH2 complex2809 Sensory SystemsAll institutes and research themes of the Radboud University Medical CenterRetinitis pigmentosaElectroretinographymedicineotorhinolaryngologic diseasesJournal ArticleAnimalsMicroscopy ImmunoelectronZebrafishZebrafishExtracellular Matrix ProteinsRetinal DegenerationMembrane ProteinsZebrafish ProteinsRetinal Photoreceptor Cell Outer Segmentmedicine.diseasebiology.organism_classification2731 OphthalmologySensory Systems10124 Institute of Molecular Life SciencesCell biologyDisease Models AnimalOphthalmology030104 developmental biologyGene Expression RegulationEctodomainMutation570 Life sciences; biologyXenotropic and Polytropic Retrovirus ReceptorUsher SyndromesErg
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The soluble form of pan-RTK inhibitor and tumor suppressor LRIG1 mediates downregulation of AXL through direct protein–protein interaction in gliobla…

2019

Abstract Background Targeted approaches for inhibiting epidermal growth factor receptor (EGFR) and other receptor tyrosine kinases (RTKs) in glioblastoma (GBM) have led to therapeutic resistance and little clinical benefit, raising the need for the development of alternative strategies. Endogenous LRIG1 (Leucine-rich Repeats and ImmunoGlobulin-like domains protein 1) is an RTK inhibitory protein required for stem cell maintenance, and we previously demonstrated the soluble ectodomain of LRIG1 (sLRIG1) to potently inhibit GBM growth in vitro and in vivo. Methods Here, we generated a recombinant protein of the ectodomain of LRIG1 (sLRIG1) and determined its activity in various cellular GBM mo…

0301 basic medicinebiologyChemistryEGFRReceptor Protein-Tyrosine KinasesglioblastomaLRIG1AXLProximity ligation assayReceptor tyrosine kinase03 medical and health sciences030104 developmental biology0302 clinical medicineEctodomainDownregulation and upregulation030220 oncology & carcinogenesisBasic and Translational Investigationsbiology.proteinCancer researchreceptor tyrosine kinaseEpidermal growth factor receptorStem cellCell adhesionNeuro-oncology Advances
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Ectodomain shedding of CD99 within highly conserved regions is mediated by the metalloprotease meprin β and promotes transendothelial cell migration.

2016

The adhesion molecule CD99 is essential for the transendothelial migration of leukocytes. In this study, we used biochemical and cellular assays to show that CD99 undergoes ectodomain shedding by the metalloprotease meprin β and subsequent intramembrane proteolysis by γ-secretase. The cleavage site in CD99 was identified by mass spectrometry within an acidic region highly conserved through different vertebrate species. This finding fits perfectly to the unique cleavage specificity of meprin β with a strong preference for aspartate residues and suggests coevolution of protease and substrate. We hypothesized that limited CD99 cleavage by meprin β would alter cellular transendothelial migratio…

0301 basic medicinemedicine.medical_treatmentProteolysis12E7 AntigenCleavage (embryo)Biochemistry03 medical and health sciencesCarcinoma Lewis LungMice0302 clinical medicineGeneticsmedicineAnimalsHumansMolecular BiologyConserved SequenceMetalloproteinaseProteasemedicine.diagnostic_testChemistryTransendothelial and Transepithelial MigrationLewis lung carcinomaMetalloendopeptidasesCell migrationMolecular biologyIn vitroMice Inbred C57BL030104 developmental biologyHEK293 CellsEctodomain030220 oncology & carcinogenesisProteolysisBiotechnologyHeLa CellsFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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The Metalloprotease Meprin β Is an Alternative β-Secretase of APP

2017

The membrane bound metalloprotease meprin β is important for collagen fibril assembly in connective tissue formation and for the detachment of the intestinal mucus layer for proper barrier function. Recent proteomic studies revealed dozens of putative new substrates of meprin β, including the amyloid precursor protein (APP). It was shown that APP is cleaved by meprin β in distinct ways, either at the β-secretase site resulting in increased levels of Aβ peptides, or at the N-terminus releasing 11 kDa, and 20 kDa peptide fragments. The latter event was discussed to be rather neuroprotective, whereas the ectodomain shedding of APP by meprin β reminiscent to BACE-1 is in line with the amyloid h…

0301 basic medicineproteolysisADAM10ProteolysisN-terminal truncated AβReview03 medical and health sciencesCellular and Molecular Neuroscienceshedding0302 clinical medicinemedicineAmyloid precursor proteinMolecular BiologyMetalloproteinasemedicine.diagnostic_testbiologyChemistryCell adhesion moleculemeprin βSheddaseBiochemistry of Alzheimer's disease030104 developmental biologyBiochemistryEctodomainbiology.proteinAPP030217 neurology & neurosurgeryNeuroscienceFrontiers in Molecular Neuroscience
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Extracellular Domains of the Bradykinin B2 Receptor Involved in Ligand Binding and Agonist Sensing Defined by Anti-peptide Antibodies

1996

Many of the physiological functions of bradykinin are mediated via the B2 receptor. Little is known about binding sites for bradykinin on the receptor. Therefore, antisera against peptides derived from the putative extracellular domains of the B2 receptor were raised. The antibodies strongly reacted with their corresponding antigens and cross-reacted both with the denatured and the native B2 receptor. Affinity-purified antibodies to the various extracellular domains were used to probe the contact sites between the receptor and its agonist, bradykinin or its antagonist HOE140. Antibodies to extracellular domain 3 (second loop) efficiently interfered, in a concentration-dependent manner, with…

AgonistReceptor Bradykinin B2medicine.drug_classMolecular Sequence DataFluorescent Antibody TechniqueCHO CellsSpodopteraBradykininTransfectionBiochemistryAntibodiesProtein Structure SecondaryCell LineCricetinaeExtracellularmedicineAnimalsHumansAmino Acid SequenceBradykinin receptorBinding siteReceptorMolecular BiologyChemistryReceptors BradykininCell MembraneCell BiologyMolecular biologyPeptide FragmentsRecombinant ProteinsRatsCell biologyModels StructuralEctodomainCompetitive antagonistIntracellularJournal of Biological Chemistry
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α-Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

2001

Disintegrin metalloproteases from different organisms form the ADAM (a disintegrin and metalloprotease) family. All members display a common domain organization and possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signaling. Members of the ADAM family are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain. The proteolytic process is referred to as ectodomain shedding, which is activated by phorbol esters and inhibited by hydroxamic acid-based inhibitors. We have shown that the disintegrin metalloprotease ADAM 10 has both constitutive and regulated alpha-secretase activity. Expression of a dominant n…

Cell signalingDisintegrinsMolecular Sequence DataProtein domainBiologyGeneral Biochemistry Genetics and Molecular BiologyADAM10 ProteinAmyloid beta-Protein PrecursorHistory and Philosophy of ScienceEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansProtease InhibitorsAmino Acid SequenceCell adhesionMetalloproteinaseGeneral NeuroscienceHEK 293 cellsMembrane ProteinsMetalloendopeptidasesRecombinant ProteinsTransmembrane proteincarbohydrates (lipids)ADAM ProteinsBiochemistryEctodomainbiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAnnals of the New York Academy of Sciences
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