0000000000403089

AUTHOR

Linda Troeberg

showing 3 related works from this author

Microvesicles shed by oligodendroglioma cells and rheumatoid synovial fibroblasts contain aggrecanase activity

2012

Membrane microvesicle shedding is an active process and occurs in viable cells with no signs of apoptosis or necrosis. We report here that microvesicles shed by oligodendroglioma cells contain an ‘aggrecanase’ activity, cleaving aggrecan at sites previously identified as targets for adamalysin metalloproteinases with disintegrin and thrombospondin domains (ADAMTSs). Degradation was inhibited by EDTA, the metalloproteinase inhibitor GM6001 and by tissue inhibitor of metalloproteinases (TIMP)-3, but not by TIMP-1 or TIMP-2. This inhibitor profile indicates that the shed microvesicles contain aggrecanolytic ADAMTS(s) or related TIMP-3-sensitive metalloproteinase(s). The oligodendroglioma cells…

OligodendrogliomaMembrane vesicleRA rheumatoid arthritisADAMTSMatrix metalloproteinaseCell Physiological PhenomenaAdamalysin03 medical and health sciences0302 clinical medicineSettore BIO/10 - BiochimicaEndopeptidasesHumansAggrecansADAM adamalysinADAMTS a disintegrin and metalloproteinase with thrombospondin motifsMolecular BiologyMetalloproteinase030304 developmental biologyAggrecanaseTissue Inhibitor of Metalloproteinase-3MEF mouse embryonic fibroblasts0303 health sciencesMetalloproteinaseChemistryBrief ReportMVs microvesiclesADAMTSMicrovesicleCytoplasmic VesiclesDipeptidesFibroblastsMolecular biologyRecombinant ProteinsMicrovesiclesECM extracellular matrixMembrane vesiclesCell biologyEnzyme ActivationMMP matrix metalloproteinaseADAM ProteinsADAMTS4030220 oncology & carcinogenesisProteolysisADAMTS5 ProteinRheumatic FeverTIMP tissue inhibitor of metalloproteinaseAggrecan
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Interleukin 13 (IL-13)-regulated expression of the chondroprotective metalloproteinase ADAM15 is reduced in aging cartilage

2020

Objective The adamalysin metalloproteinase 15 (ADAM15) has been shown to protect against development of osteoarthritis in mice. Here, we have investigated factors that control ADAM15 levels in cartilage. Design Secretomes from wild-type and Adam15−/− chondrocytes were compared by label-free quantitative mass spectrometry. mRNA was isolated from murine knee joints, either with or without surgical induction of osteoarthritis on male C57BL/6 mice, and the expression of Adam15 and other related genes quantified by RT-qPCR. ADAM15 in human normal and osteoarthritic cartilage was investigated similarly and by fluorescent immunohistochemistry. Cultured HTB94 chondrosarcoma cells were treated with …

Senescencemedicine.medical_specialtyADAM15medicine.medical_treatmentOsteoarthritisDiseases of the musculoskeletal systemArticleMetalloproteaseAgeSettore BIO/13 - Biologia ApplicataInternal medicineOsteoarthritismedicineddc:610MetalloproteinaseMetalloproteinaseADAM15ChemistryCartilageAutophagyGeneral Medicinemedicine.diseasemedicine.anatomical_structureEndocrinologyCytokineRC925-935IL-13Interleukin 13OsteoarthritiOsteoarthritis and Cartilage Open
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TIMP-3 facilitates binding of target metalloproteinases to the endocytic receptor LRP-1 and promotes scavenging of MMP-1.

2020

AbstractMatrix metalloproteinases (MMPs) and the related families of disintegrin metalloproteinases (ADAMs) and ADAMs with thrombospondin repeats (ADAMTSs) play a crucial role in extracellular matrix (ECM) turnover and shedding of cell-surface molecules. The proteolytic activity of metalloproteinases is post-translationally regulated by their endogenous inhibitors, known as tissue inhibitors of metalloproteinases (TIMPs). Several MMPs, ADAMTSs and TIMPs have been reported to be endocytosed by the low-density lipoprotein receptor-related protein-1 (LRP-1). Different binding affinities of these proteins for the endocytic receptor correlate with different turnover rates which, together with di…

Cell biologyTIMP-3 LRP-1 MMP-1 extracellular matrix endocytosis metalloproteinases endocytic receptorlcsh:MedicinePlasma protein bindingMatrix metalloproteinaseBiochemistryArticleExtracellular matrixDisintegrinHumanslcsh:ScienceReceptorTissue Inhibitor of Metalloproteinase-3MetalloproteinaseThrombospondinMultidisciplinarybiologyChemistrylcsh:RLigand (biochemistry)EndocytosisMatrix MetalloproteinasesCell biologyKineticsMultiprotein Complexesbiology.proteinlcsh:Qlipids (amino acids peptides and proteins)Matrix Metalloproteinase 1Low Density Lipoprotein Receptor-Related Protein-1Protein BindingScientific reports
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