Search results for "Metalloproteinase"

showing 10 items of 280 documents

Update on the role of molecular factors and fibroblasts in the pathogenesis of Dupuytren’s disease

2016

The mechanism by which the fibroblast is able to trigger palmar fibromatosis is still not yet fully understood. It would appear certain that the “abnormal” fibroblasts continuously synthesise profibrotic cytokines which are able to determine the activation to myofibroblasts, to stimulate them to the further proliferation and synthesis of other cytokines, to modify the cells’ differentiation and ultrastructural characteristics, as well as the production of matrix and other proteins. Several fibroblast growth factors have been suggested to be responsible of an abnormal cell activation with an aberrantly elevated collagen synthesis and extracellular deposition in Dupuytren’s disease, as TGF-Be…

0301 basic medicinemedicine.medical_specialtySettore MED/19 - Chirurgia PlasticaReviewMatrix metalloproteinaseFibroblast growth factorBiochemistryPathogenesis03 medical and health sciences0302 clinical medicineInternal medicinemedicineExtracellularFibroblastMolecular BiologyCytokines Fibroblast Dupuytren’s disease030222 orthopedicsbiologyCell Biology030104 developmental biologyEndocrinologymedicine.anatomical_structurebiology.proteinCancer researchMyofibroblastPlatelet-derived growth factor receptorPalmar Fibromatosis
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Dipeptidyl Peptidase IV as a Muscle Myokine

2020

Dipeptidyl peptidase IV (DPP-IV) is a unique serine protease that exists in a membrane bound state and in a soluble state in most tissues in the body. DPP-IV has multiple targets including cytokines, neuropeptides, and incretin hormones, and plays an important role in health and disease. Recent work suggests that skeletal muscle releases DPP-IV as a myokine and participates in control of muscle blood flow. However, few of the functions of DPP-IV as a myokine have been investigated to date and there is a poor understanding about what causes DPP-IV to be released from muscle.

0301 basic medicinemedicine.medical_specialtyanimal structuresPhysiologymuscleMini ReviewNeuropeptideIncretin030204 cardiovascular system & hematologyDipeptidyl peptidaselcsh:Physiology03 medical and health sciences0302 clinical medicinePhysiology (medical)Internal medicineMyokinemedicinemetalloproteasesSerine proteaseMetalloproteinasebiologyexerciselcsh:QP1-981ChemistrySkeletal musclewhey proteinpeptidasesecretome030104 developmental biologyEndocrinologymedicine.anatomical_structurebiology.proteinHormoneFrontiers in Physiology
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Roles of NGAL and MMP-9 in the tumor microenvironment and sensitivity to targeted therapy.

2016

Various, diverse molecules contribute to the tumor microenvironment and influence invasion and metastasis. In this review, the roles of neutrophil gelatinase-associated lipocalin (NGAL) and matrix metalloproteinase-9 (MMP-9) in the tumor microenvironment and sensitivity to therapy will be discussed. The lipocalin family of proteins has many important functions. For example when NGAL forms a complex with MMP-9 it increases its stability which is important in cancer metastasis. Small hydrophobic molecules are bound by NGAL which can alter their entry into and efflux from cells. Iron transport and storage are also influenced by NGAL activity. Regulation of iron levels is important for survival…

0301 basic medicinemedicine.medical_treatmentDrug resistance; Iron transport; Lcn2; Lipocalins; MMP-9; NGAL; SiderocalinsAcute-Phase ProteinLipocalinLipocalinMetastasisTargeted therapyAntineoplastic Agent0302 clinical medicineNeoplasmsTumor MicroenvironmentNeoplasm MetastasisNGALProto-Oncogene ProteinMedicine (all)SiderocalinsLipocalinsNeoplasm MetastasiMatrix Metalloproteinase 9030220 oncology & carcinogenesismedicine.symptomSignal transductionMMP-9HumanProtein BindingSignal TransductionSiderocalinAntineoplastic AgentsInflammationBiologyModels Biological03 medical and health sciencesLcn2Lipocalin-2Proto-Oncogene ProteinsmedicineHumansIron transportMolecular BiologyTumor microenvironmentInnate immune systemCell Biologymedicine.disease030104 developmental biologyDrug resistanceCancer cellImmunologyCancer researchNeoplasmAcute-Phase Proteins
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Specialized regulatory T cells control venous blood clot resolution through SPARC.

2020

Abstract The cells and mechanisms involved in blood clot resorption are only partially known. We show that regulatory T cells (Tregs) accumulate in venous blood clots and regulate thrombolysis by controlling the recruitment, differentiation and matrix metalloproteinase (MMP) activity of monocytes. We describe a clot Treg population that forms the matricellular acid– and cysteine-rich protein SPARC (secreted protein acidic and rich in cysteine) and show that SPARC enhances monocyte MMP activity and that SPARC+ Tregs are crucial for blood clot resorption. By comparing different treatment times, we define a therapeutic window of Treg expansion that accelerates clot resorption.

0301 basic medicinemedicine.medical_treatmentImmunologyPopulation030204 cardiovascular system & hematologyMatrix metalloproteinaseBiochemistryT-Lymphocytes RegulatoryMonocytes03 medical and health sciences0302 clinical medicinemedicineAnimalsOsteonectinThrombuseducationVenous Thrombosiseducation.field_of_studyChemistryMonocyteFibrinolysisCell BiologyHematologyVenous bloodThrombolysismedicine.diseaseMatrix MetalloproteinasesResorptionCell biologyMice Inbred C57BL030104 developmental biologymedicine.anatomical_structureCysteineBlood
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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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Genotyping strategy of SMAD-3 rs3825977 gene variant for a differential management of ascending aorta aneurysm in women people: Gender oriented diagn…

2020

Abstract Background and objectives The research of opportune strategies for facilitating the management of complex pathologies, such as ascending aorta aneurysm (AAA), currently represents the principal object of clinicians, clinical pathologists included. Herein, we propose genotyping of gene variants related to TGF-β pathway as useful strategy to improve the complex AAA management, exclusively based on imaging evaluations. Precisely, we investigated four functional SNPs in SMAD and VEGF genes, encoding molecules able to modulate functions and cross-talks of TGF-β pathway. Populations and methods Our study included 92 individuals (70 men (76%) and 22 (24%) women; mean age: 71.4 ± 2.6 years…

0301 basic medicinetransforming growth factorSNPs of SMAD and VEGF genesSMADBioinformaticsAscending aorta aneurysm (AAA)03 medical and health sciences0302 clinical medicineImmune systemmedicine.arteryGenotypeGeneticsmedicineGenotypingGeneGenetics (clinical)aorta aneurysmMetalloproteinaseAortaFemale peoplebusiness.industryGenetic variantsaorta aneurysm; transforming growth factorSettore MED/23030104 developmental biology030220 oncology & carcinogenesisGender medicinebusinessGenotyping strategy
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Effect of a dominant-negative form of ADAM10 in a mouse model of Alzheimer's disease.

2009

The alpha-secretase cleaves in the non-amyloidogenic pathway the amyloid-beta protein precursor (AbetaPP) within the region of the amyloid-beta peptides to prevent their formation and aggregation in the brain. Members of the ADAM family (a disintegrin and metalloprotease) are the main candidates for physiologically relevant alpha-secretases. We recently demonstrated that overexpression of ADAM10 in mice transgenic for human AbetaPP (ADAM10 x APP[V717I]) alleviated functional deficits related to Alzheimer's disease. To further demonstrate that this is due to the specific activity of alpha-secretase, we characterized mice overexpressing an inactive form of ADAM10 (ADAM10[E384A]; ADAM10-dn). T…

ADAM10Morris water navigation taskGlutamic AcidStimulationMice TransgenicADAM10 ProteinAmyloid beta-Protein PrecursorMiceIn vivoAlzheimer DiseaseDisintegrinReaction TimeAnimalsHumansIsoleucineProtein precursorMaze LearningSwimmingMetalloproteinaseAlaninebiologyBehavior AnimalChemistryGeneral NeuroscienceAge FactorsMembrane ProteinsValineGeneral MedicineCell biologyMice Inbred C57BLPsychiatry and Mental healthClinical PsychologyADAM ProteinsDisease Models Animalbiology.proteinSpecific activityGeriatrics and GerontologyAmyloid Precursor Protein SecretasesJournal of Alzheimer's disease : JAD
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MMP-2, MMP-9 and activin A blood levels in patients with breast cancer or prostate cancer metastatic to the bone.

2007

Background: The clinical significance of the circulating levels of activin A and matrix metalloproteinase-2 (MMP-2) and -9 (MMP-9) was investigated in patients with breast cancer (BC) or prostate cancer (PC) with (M1) or without (M0) bone metastasis. Patients and Methods: MMP-2, MMP-9 and activin A blood concentrations were measured by enzyme immunoassays in 79 cancer patients and in 57 healthy blood donors (HS) who served as a control group. The diagnostic accuracy of these molecules to discriminate between M0 and M1 patients was evaluated by the receiver operating characteristic curve (ROC) and compared to that of tumor markers CA15.3 or prostate-specific antigen (PSA). Results: Activin A…

AdultAged 80 and overMaleMucin-1Prostatic NeoplasmsBone NeoplasmsBreast NeoplasmsMiddle AgedActivinsActivin Breast Cancer Bone metastasis proteinasesMatrix Metalloproteinase 9Activins; Adult; Aged; Aged 80 and over; Bone Neoplasms; Breast Neoplasms; Female; Humans; Male; Matrix Metalloproteinase 2; Matrix Metalloproteinase 9; Middle Aged; Mucin-1; Prostatic NeoplasmsHumansMatrix Metalloproteinase 2FemaleAged
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MMP-7 promoter polymorphisms do not influence CD4+ recovery and changes in plasma viral load during antiretroviral therapy for HIV-1 infection.

2005

Summary Matrix metalloproteinase-7 (MMP-7) generates soluble Fas Ligand (FasL), which is involved in the apoptotic loss of CD4+ T cells during HIV infection. We evaluated whether two polymorphisms in MMP-7 promoter could influence CD4+ recover in response to antiretroviral therapy, and found that these polymorphisms are ineffective.

AdultCD4-Positive T-LymphocytesMaleImmunologyHuman immunodeficiency virus (HIV)HIV InfectionsMatrix metalloproteinasemedicine.disease_causeMMP-7; Fas ligand; CD4T cells; HIV infectionFas ligandPlasma viral loadGeneticsHumansMedicineMolecular BiologyGenetics (clinical)Polymorphism Geneticbusiness.industryMetalloendopeptidasesGeneral MedicineMiddle AgedViral LoadAntiretroviral therapySoluble fas ligandCD4 Lymphocyte CountAnti-Retroviral AgentsApoptosisMatrix Metalloproteinase 7ImmunologyHIV-1business
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