Search results for "llop"

showing 10 items of 640 documents

Association study of MMP8 gene in osteoarthritis.

2016

Objectives: Osteoarthritis (OA) is a joint disease common in the elderly. There is a prior functional evidence for different matrix metalloproteinases (MMPs), such as MMP8 and MMP9, having a role in the breakdown of cartilage extracellular matrix in OA. Thus, we analyzed whether the common genetic variants of MMP8 and MMP9 contribute to the risk of OA. Materials and methods: In total, 13 common tagging single-nucleotide polymorphisms (SNPs) were studied in a discovery knee OA cohort of 185 cases and 895 controls. For validation, two knee OA replication cohorts and two hand OA replication cohorts were studied (altogether 1369 OA cases, 4445 controls in the five cohorts). The chi(2) test for …

0301 basic medicineOncologyMaleLinkage disequilibriumLINKAGE DISEQUILIBRIUMMATRIX METALLOPROTEINASESOsteoarthritisSUSCEPTIBILITYBioinformaticsMMP8BiochemistryOrthopedics and Sports MedicineIN-VIVOta3141Middle AgedOsteoarthritis Knee3142 Public health care science environmental and occupational healthmedicine.anatomical_structureMatrix Metalloproteinase 8CohortFemaleEXPRESSIONAdultmedicine.medical_specialtySingle-nucleotide polymorphismKNEE OSTEOARTHRITISta3111Polymorphism Single NucleotideAssociationANKLE JOINTS03 medical and health sciencesRheumatologyInternal medicinemedicineSNPHumansgeneMolecular BiologyGeneAgedbusiness.industryCartilageta1184Cell BiologyARTICULAR-CARTILAGEmedicine.diseaseosteoarthritis030104 developmental biologyWIDE STATISTICAL SIGNIFICANCENEUTROPHIL COLLAGENASE3111 BiomedicinebusinessConnective tissue research
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A targeted proteomics investigation of the obesity paradox in venous thromboembolism

2021

Abstract The obesity paradox, the controversial finding that obesity promotes disease development but protects against sequelae in patients, has been observed in venous thromboembolism (VTE). The aim of this investigation was to identify a body mass–related proteomic signature in VTE patients and to evaluate whether this signature mediates the obesity paradox in VTE patients. Data from the Genotyping and Molecular Phenotyping in Venous ThromboEmbolism Project, a prospective cohort study of 693 VTE patients, were analyzed. A combined end point of recurrent VTE or all-cause death was used. Relative quantification of 444 proteins was performed using high-throughput targeted proteomics technolo…

0301 basic medicineOncologyProteomicsmedicine.medical_specialtyDisease030204 cardiovascular system & hematologyThrombosis and Hemostasis03 medical and health sciences0302 clinical medicineRisk FactorsInternal medicinemedicineHumansLectins C-Typecardiovascular diseasesObesityProspective StudiesReceptors ImmunologicProspective cohort studyGenotypingMembrane Glycoproteinsbusiness.industryLeptinHazard ratioHematologyVenous Thromboembolismmedicine.diseaseObesityConfidence interval030104 developmental biologyMatrix Metalloproteinase 2businessObesity paradox
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New Insights into the Occurrence of Matrix Metalloproteases -2 and -9 in a Cohort of Breast Cancer Patients and Proteomic Correlations

2018

Matrix metalloproteases (MMPS) are a family of well-known enzymes which operate prevalently in the extracellular domain, where they fulfil the function of remodeling the extracellular matrix. Within the about 26 family members, encoded by 24 genes in humans, MMP-2 and MMP-9, have been regarded as the primary responsibility for the basement membrane and pericellular ECM rearrangement. In cases of infiltrating carcinomas, which arise from the epithelial tissues of a gland or of an internal organ, a marked alteration of the expression and the activity levels of both MMPs is known to occur. Present investigation represents the continuation and upgrading of our previous studies, now focusing on …

0301 basic medicineOncologymedicine.medical_specialtyMatrix metalloproteinaseBiologyProteomicsArticleExtracellular matrix03 medical and health sciences0302 clinical medicinebreast cancerproteomicsBreast cancermatrix metalloproteasesInternal medicineExtracellularmedicineMatrix metalloproteasesSettore BIO/06 - Anatomia Comparata E CitologiaGenelcsh:QH301-705.5oncology_oncogenicsBasement membranebusiness.industryGeneral Medicinemedicine.diseasematrix metalloprotease030104 developmental biologymedicine.anatomical_structurelcsh:Biology (General)030220 oncology & carcinogenesisCohortCancer researchbusinessFunction (biology)
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Propeptide glycosylation and galectin‐3 binding decrease proteolytic activation of human proMMP‐9/progelatinase B

2019

Matrix metalloproteinases (MMPs) are secreted as proenzymes, containing propeptides that interact with the catalytic zinc, thereby controlling MMP activation. The MMP‐9 propeptide is unique in the MMP family because of its post‐translational modification with an N‐linked oligosaccharide. ProMMP‐9 activation by MMP‐3 occurs stepwise by cleavage of the propeptide in an aminoterminal (pro‐AT) and carboxyterminal (pro‐CT) peptide. We chemically synthesized aglycosyl pro‐AT and pro‐CT and purified recombinant glycosylated pro‐ATS f−9. First, we report new cleavage sites in the MMP‐9 propeptide by MMP‐3 and neutrophil elastase. Additionally, we demonstrated with the use of western blot analysis a…

0301 basic medicinePNGase FN-linked glycosylationGlycosylationGlycosylationmatrix metalloproteinase‐9Galectin 3GalectinsProteolysisgalectin‐3Biochemistry03 medical and health scienceschemistry.chemical_compoundCongenital Disorders of Glycosylation0302 clinical medicineN-linked glycosylationmatrix metalloproteinase-9galectin-3medicineHumansZymographyAmino Acid SequenceProtein precursorMolecular BiologyN‐linked glycosylationEnzyme Precursorspropeptidemedicine.diagnostic_testbiologyBlood ProteinsOriginal ArticlesCell BiologyTrypsinEnzyme Activation030104 developmental biologyMatrix Metalloproteinase 9chemistryBiochemistryGelatinasesCase-Control Studiesproteolytic activation030220 oncology & carcinogenesisNeutrophil elastaseProteolysisbiology.proteinMatrix Metalloproteinase 3Original ArticleLeukocyte Elastasemedicine.drug
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Prognostic value of matrix metalloproteinase-9 expression in oral squamous cell carcinoma and its association with angiogenesis

2016

Background: Breakdown of extracellular matrix (ECM) is one of the important hallmarks of cancer progression which facilitates the invasion of tumoral cells to the surrounding tissue. Matrix metalloproteinases (MMPs) can degrade various components of the ECM and basement membrane. The aim of this study was to determine the role of matrix metalloproteinases-9 protein in the biologic behavior of oral squamous cell carcinoma (OSCC) and its relation with tumor angiogenesis. Material and Methods: In this study 42 OSCC and 15 normal epithelium were reviewed by immunohistochemical staining for matrix metalloproteinases-9 and CD105. Results: Matrix metalloproteinases-9 expression was detected in 32 …

0301 basic medicinePathologymedicine.medical_specialtyAngiogenesisOdontologíaMatrix metalloproteinaseMMP9Extracellular matrix03 medical and health sciences0302 clinical medicinemedicineGeneral DentistryBasement membraneOral Medicine and Pathologybusiness.industryResearchCancerEndoglin:CIENCIAS MÉDICAS [UNESCO]medicine.diseaseCiencias de la salud030104 developmental biologymedicine.anatomical_structureTumor progression030220 oncology & carcinogenesisUNESCO::CIENCIAS MÉDICASbusinessJournal of Clinical and Experimental Dentistry
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Copper transporter COPT5 participates in the crosstalk between vacuolar copper and iron pools mobilisation

2019

Copper (Cu) deficiency affects iron (Fe) homeostasis in several plant processes, including the increased Fe requirements due to cuproprotein substitutions for the corresponding Fe counterpart. Loss-of-function mutants from Arabidopsis thaliana high affinity copper transporter COPT5 and Fe transporters NATURAL RESISTANCE-ASSOCIATED MACROPHAGE PROTEIN 3/4 (NRAMP3 and NRAMP4) were used to study the interaction between metals internal pools. A physiological characterisation showed that the copt5 mutant is sensitive to Fe deficiency, and that nramp3nramp4 mutant growth was severely affected under limiting Cu. By a transcriptomic analysis, we observed that NRAMP4 expression was highly induced in …

0301 basic medicinePhysiologyIron[SDV]Life Sciences [q-bio]MutantArabidopsislcsh:Medicinechemistry.chemical_elementChromosomal translocationVacuolePlant RootsArticleMetal03 medical and health sciences0302 clinical medicineCopper Transport ProteinsGene Expression Regulation PlantMetalloproteinHomeostasis[SDV.BV]Life Sciences [q-bio]/Vegetal BiologySLC31 Proteinslcsh:ScienceComputingMilieux_MISCELLANEOUSchemistry.chemical_classificationMultidisciplinaryArabidopsis Proteinslcsh:RBiological TransportTransporterPlants Genetically ModifiedCopperCrosstalk (biology)030104 developmental biologychemistryMetalsvisual_artVacuolesvisual_art.visual_art_mediumBiophysicslcsh:QPlant sciences[SDV.AEN]Life Sciences [q-bio]/Food and NutritionCopper030217 neurology & neurosurgeryScientific Reports
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Temperature increases, hypoxia, and changes in food availability affect immunological biomarkers in the marine mussel Mytilus galloprovincialis

2017

Temperature increases, hypoxia, and changes in food availability are predicted to occur in the future. There is growing concern for the health status of wild and farmed organisms, since environmental stressors alter organism functions, and elicit coordinated physiological responses for homeostasis. Mussels are good bioindicators of environmental conditions. Their ability to maintain unaltered immunosurveillance under adverse environmental conditions may enhance their survival capability. Few studies are currently concerned with the relationships and feedback among multiple stressors. Here, food concentration, temperature, and oxygenation treatments were evaluated for their effects on immune…

0301 basic medicinePhysiologyMytilus galloprovincialiBiologyBiochemistryToxicology03 medical and health scienceschemistry.chemical_compoundEndocrinologyDigestive System Physiological PhenomenaHemolymphAnimalsFood scienceLysosomal membraneHypoxiaEcology Evolution Behavior and SystematicsImmunobiologyMytilusMonophenol MonooxygenaseEsterasesTemperatureHypoxia (environmental)MusselBiomarkerbiology.organism_classificationAlkaline PhosphataseAnoxic watersMytilus030104 developmental biologychemistryFoodEnzymeChlorophyllAlkaline phosphataseAnimal Science and ZoologyEnvironmental multiple stressorLysosomesBioindicatorHomeostasisBiomarkers
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Mammalian plasma fetuin-B is a selective inhibitor of ovastacin and meprin metalloproteinases

2019

AbstractVertebrate fetuins are multi-domain plasma-proteins of the cystatin-superfamily. Human fetuin-A is also known as AHSG, α2-Heremans-Schmid-glycoprotein. Gene-knockout in mice identified fetuin-A as essential for calcified-matrix-metabolism and bone-mineralization. Fetuin-B deficient mice, on the other hand, are female infertile due to zona pellucida ‘hardening’ caused by the metalloproteinase ovastacin in unfertilized oocytes. In wildtype mice fetuin-B inhibits the activity of ovastacin thus maintaining oocytes fertilizable. Here we asked, if fetuins affect further proteases as might be expected from their evolutionary relation to single-domain-cystatins, known as proteinase-inhibito…

0301 basic medicineProteasesGlycosylationalpha-2-HS-Glycoproteinmedicine.medical_treatmentProteolysislcsh:MedicineAstacoideaMatrix metalloproteinaseArticle03 medical and health sciencesMicePlasma0302 clinical medicinemedicineAnimalsHumansFibrinolysinZona pellucidalcsh:ScienceMammalsMetalloproteinaseMultidisciplinaryProteasemedicine.diagnostic_testChemistrylcsh:RWild typeMetalloendopeptidasesFetuinFetuin-BRecombinant ProteinsCell biology030104 developmental biologymedicine.anatomical_structureMatrix Metalloproteinase 9FertilizationProteolysisMetalloproteasesCattlelcsh:Q030217 neurology & neurosurgery
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The C-terminal region of human plasma fetuin-B is dispensable for the raised-elephant-trunk mechanism of inhibition of astacin metallopeptidases

2019

© The Author(s) 2019.

0301 basic medicineProteasesProtein Conformationlcsh:MedicineAstacoideaCrystallography X-RayCleavage (embryo)Protein Structure SecondaryArticleMice03 medical and health sciencesScissile bondHydrolaseAnimalsHumansAmino Acid Sequencelcsh:ScienceProtein secondary structureX-ray crystallographyBinding SitesMultidisciplinary030102 biochemistry & molecular biologyChemistrylcsh:RMetalloendopeptidasesProteasesFetuinFetuin-BCell biologyZincFertility030104 developmental biologyProteolysisMetalloproteaseslcsh:QAstacinLinkerScientific Reports
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Allopurinol partially prevents disuse muscle atrophy in mice and humans

2018

AbstractDisuse muscle wasting will likely affect everyone in his or her lifetime in response to pathologies such as joint immobilization, inactivity or bed rest. There are no good therapies to treat it. We previously found that allopurinol, a drug widely used to treat gout, protects muscle damage after exhaustive exercise and results in functional gains in old individuals. Thus, we decided to test its effect in the prevention of soleus muscle atrophy after two weeks of hindlimb unloading in mice, and lower leg immobilization following ankle sprain in humans (EudraCT: 2011-003541-17). Our results show that allopurinol partially protects against muscle atrophy in both mice and humans. The pro…

0301 basic medicineProteasome Endopeptidase Complexmedicine.medical_specialtyScience[SDV]Life Sciences [q-bio]Allopurinolmedicine.medical_treatmentAllopurinolHindlimbBed restArticleMice03 medical and health sciences0302 clinical medicineAtrophyPhysical Conditioning AnimalInternal medicineAnimalsHumansMedicineAnkle InjuriesMuscle SkeletalWastingSoleus muscleMultidisciplinaryUbiquitinbusiness.industryQRmedicine.diseaseMuscular Disorders AtrophicMuscle atrophy3. Good healthGoutMuscular Atrophy030104 developmental biologyEndocrinologyHindlimb SuspensionMedicinemedicine.symptombusiness030217 neurology & neurosurgerymedicine.drugScientific Reports
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