Search results for "collagens"

showing 10 items of 19 documents

Impact of single-dose application of TGF-β, copper peptide, stanozolol and ascorbic acid in hydrogel on midline laparatomy wound healing in a diabeti…

2012

Despite numerous advances and improvements in surgical techniques the incidence of incisional hernias after laparotomy remains high. The aim of this study was to investigate possible effects of single application of ascorbic acid, stanozolol, a synthetic anabolic steroid, copper peptide and transforming growth factor-β (TGF-β) on laparotomy wound healing in an incisional wound model in diabetic mice. After diabetes induction with streptozotozin in Balb-c mice, midline laparatomies were carried out. Closure of the linea alba was followed by single-dose application of the agents dissolved in a hydrogel before skin closure. The functional outcome was assessed in terms of maximum tensile streng…

medicine.medical_specialtymedicine.medical_treatmentFibrillar CollagensAscorbic AcidBiologyDiabetes Mellitus ExperimentalCollagen Type IIICicatrixMiceTransforming Growth Factor betaInternal medicineDiabetes mellitusLaparotomyTensile StrengthGeneticsmedicineAnimalsStanozololLaparotomyMice Inbred BALB CWound HealingHydrogelsGeneral MedicineAscorbic acidmedicine.diseaseDisease Models Animalmedicine.anatomical_structureEndocrinologyLinea alba (abdomen)FemaleWound healingPeptidesAnabolic steroidCopperStanozololmedicine.drugInternational journal of molecular medicine
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Integrin-mediated Cell Adhesion to Type I Collagen Fibrils

2004

In the integrin family, the collagen receptors form a structurally and functionally distinct subgroup. Two members of this subgroup, α1β1 and α2β1 integrins, are known to bind to monomeric form of type I collagen. However, in tissues type I collagen monomers are organized into large fibrils immediately after they are released from cells. Here, we studied collagen fibril recognition by integrins. By an immunoelectron microscopy method we showed that integrin α2I domain is able to bind to classical D-banded type I collagen fibrils. However, according to the solid phase binding assay, the collagen fibril formation appeared to reduce integrin α1I and α2I domain avidity to collagen and to lower …

fibrilsIntegrinsintegrinRecombinant Fusion ProteinsImmunoelectron microscopyIntegrinCHO Cellsmacromolecular substancesIn Vitro TechniquesFibrilBiochemistryCollagen Type IIntegrin alpha1beta1Collagen receptorCricetinaeCell AdhesionAnimalsHumansMicroscopy ImmunoelectronCell adhesionMolecular BiologybiologyChemistryFibrillogenesisCell BiologycollagensCell biologyCollagen type I alpha 1Biochemistrybiology.proteinCattleIntegrin alpha2beta1Type I collagenJournal of Biological Chemistry
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Screening archaeological bone for palaeogenetic and palaeoproteomic studies.

2020

Funder: FP7 Ideas: European Research Council; funder-id: http://dx.doi.org/10.13039/100011199; Grant(s): 295729

1100Proteomics1300Social SciencesMarine and Aquatic Sciences01 natural sciencesBiochemistrySpectroscopy Fourier Transform InfraredLimnologyScreening method0303 health sciencesMultidisciplinaryAncient DNAChemistryFossilsQRFOS: Social sciencesNucleic acidsArchaeologyAttenuated total reflectionMedicinePhysical AnthropologyOrganic contentResearch Article1000010506 paleontologyScienceInfrared spectroscopyPaleoenvironmentsBone and Bones03 medical and health sciencesPaleoanthropologyGeneticsAnimalsHumansPaleolimnologyDNA AncientPaleozoology030304 developmental biology0105 earth and related environmental sciencesEcology and Environmental SciencesBiology and Life SciencesProteinsPaleontologyDNAArchaeologyEarth sciencesAncient DNAAnthropologyPaleobiologyPaleogeneticsCollagensPloS one
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Proteolytic Enzymes Clustered in Specialized Plasma-Membrane Domains Drive Endothelial Cells’ Migration

2016

In vitro cultured endothelial cells forming a continuous monolayer establish stable cell-cell contacts and acquire a "resting" phenotype; on the other hand, when growing in sparse conditions these cells acquire a migratory phenotype and invade the empty area of the culture. Culturing cells in different conditions, we compared expression and clustering of proteolytic enzymes in cells having migratory versus stationary behavior. In order to observe resting and migrating cells in the same microscopic field, a continuous cell monolayer was wounded. Increased expression of proteolytic enzymes was evident in cell membranes of migrating cells especially at sprouting sites and in shed membrane vesi…

0301 basic medicinekalininsepraseCell Membranesbeta1 integrinCelllcsh:MedicineurokinaseBiochemistryEpitheliumCell membrane0302 clinical medicineAnimal CellsMedicine and Health Sciencesdipeptidyl peptidase IVlcsh:ScienceMultidisciplinarybiologyVesicleProteolytic enzymesCell migrationProteasesEnzymesCell biologyLaboratory EquipmentCell Motilitymedicine.anatomical_structureBiochemistry030220 oncology & carcinogenesisEngineering and TechnologyBiological Culturesmatrix metalloproteinase 14Cellular Structures and OrganellesCellular TypesAnatomyResearch ArticleEquipmentCell MigrationResearch and Analysis MethodsGelatin MediaCell Linegelatinase B03 medical and health sciencescollagen type 4fibronectinmedicineHumansVesiclescollagen type 1gelatinase Alcsh:RCell MembraneBiology and Life SciencesEndothelial CellsProteinsMembrane ProteinsEpithelial CellsCell BiologyCulture MediaFibronectinBiological Tissue030104 developmental biologyMembrane proteinCell cultureProteolysisMicroscopy Electron ScanningEnzymologybiology.proteinlcsh:QCollagensDevelopmental BiologyPLOS ONE
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The cell adhesion domain of type XVII collagen promotes integrin-mediated cell spreading by a novel mechanism.

2001

Type XVII collagen (BP180) is a keratinocyte transmembrane protein that exists as the full-length protein in hemidesmosomes and as a 120-kDa shed ectodomain in the extracellular matrix. The largest collagenous domain of type XVII collagen, COL15, has been described previously as a cell adhesion domain (Tasanen, K., Eble, J. A., Aumailley, M., Schumann, H., Baetge, J, Tu, H., Bruckner, P., and Bruckner-Tuderman, L. (2000) J. Biol. Chem. 275, 3093-3099). In the present work, the integrin binding of triple helical, human recombinant COL15 was tested. Solid phase binding assays using recombinant integrin alpha(1)I, alpha(2)I, and alpha(10)I domains and cell spreading assays with alpha(1)beta(1)…

KeratinocytesIntegrinsDNA ComplementaryDystoninIntegrinAmino Acid MotifsNerve Tissue ProteinsCHO CellsBiochemistryAutoantigensCollagen receptorCell LineCell MovementCricetinaeCell AdhesionTumor Cells CulturedAnimalsHumansCloning MolecularCell adhesionMolecular BiologyIntegrin bindingbiologyDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionHemidesmosomeCell BiologyNon-Fibrillar CollagensMolecular biologyRecombinant ProteinsProtein Structure TertiaryFibronectinHaCaTCytoskeletal ProteinsEctodomainbiology.proteinCollagenCarrier ProteinsPeptidesProtein BindingThe Journal of biological chemistry
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Mechanical strain causes adaptive change in bronchial fibroblasts enhancing profibrotic and inflammatory responses

2016

Asthma is characterized by periodic episodes of bronchoconstriction and reversible airway obstruction; these symptoms are attributable to a number of factors including increased mass and reactivity of bronchial smooth muscle and extracellular matrix (ECM) in asthmatic airways. Literature has suggested changes in cell responses and signaling can be elicited via modulation of mechanical stress acting upon them, potentially affecting the microenvironment of the cell. In this study, we hypothesized that mechanical strain directly affects the (myo)fibroblast phenotype in asthma. Therefore, we characterized responses of bronchial fibroblasts, from 6 normal and 11 asthmatic non-smoking volunteers,…

MalePulmonologyPulmonary FibrosisAdult; Asthma; Biomechanical Phenomena; Bronchi; Case-Control Studies; Female; Fibroblasts; Humans; Male; Pneumonia; Pulmonary Fibrosis; Stress Mechanical; Medicine (all); Biochemistry Genetics and Molecular Biology (all); Agricultural and Biological Sciences (all)Glycobiologylcsh:MedicinePathology and Laboratory MedicineBiochemistryAnimal CellsMedicine and Health Scienceslcsh:ScienceImmune ResponseMusculoskeletal SystemConnective Tissue CellsSmooth MusclesMusclesMedicine (all)Extracellular MatrixBiomechanical PhenomenaConnective TissueFibroblastProteoglycansFemaleCellular TypesAnatomyCellular Structures and OrganellesCase-Control StudieResearch ArticleHumanAdultPulmonary FibrosiImmunologyBronchiSigns and SymptomsExtraction techniquesDiagnostic MedicineHumansInflammationBiochemistry Genetics and Molecular Biology (all)Settore BIO/16 - Anatomia Umanalcsh:RBiology and Life SciencesProteinsCell BiologyPneumoniaFibroblastsRNA extractionAsthmaResearch and analysis methodsBiological TissueAgricultural and Biological Sciences (all)Case-Control Studieslcsh:QStress MechanicalCollagens
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Genetic abrogation of the fibronectin-α5β1 integrin interaction in articular cartilage aggravates osteoarthritis in mice.

2018

The balance between synthesis and degradation of the cartilage extracellular matrix is severely altered in osteoarthritis, where degradation predominates. One reason for this imbalance is believed to be due to the ligation of the α5β1 integrin, the classic fibronectin (FN) receptor, with soluble FN fragments instead of insoluble FN fibrils, which induces matrix metalloproteinase (MMP) expression. Our objective was to determine whether the lack of α5β1-FN binding influences cartilage morphogenesis in vivo and whether non-ligated α5β1 protects or aggravates the course of osteoarthritis in mice. We engineered mice (Col2a-Cre;Fn1RGE/fl), whose chondrocytes express an α5β1 binding-deficient FN, …

Cartilage ArticularMale0301 basic medicineIntegrinsKnee JointGlycobiologylcsh:MedicineCartilage morphogenesisOsteoarthritisMatrix metalloproteinaseBiochemistryExtracellular matrixMice0302 clinical medicineAnimal CellsMedicine and Health Scienceslcsh:ScienceConnective Tissue CellsStainingMultidisciplinarybiologyChemistryExtracellular MatrixCell biologymedicine.anatomical_structureConnective TissueProteoglycansMatrix Metalloproteinase 3AnatomyCellular Structures and OrganellesCellular TypesResearch ArticleIntegrin alpha5beta1Signal TransductionIntegrinMice TransgenicResearch and Analysis Methods03 medical and health sciencesChondrocytesPhysical Conditioning AnimalMatrix Metalloproteinase 13OsteoarthritisCell AdhesionmedicineAnimalsHumansRegenerationCytoplasmic Staining030203 arthritis & rheumatologyCartilagelcsh:RBiology and Life SciencesProteinsCell Biologymedicine.diseaseFibronectinsFibronectinDisease Models AnimalBiological TissueCartilage030104 developmental biologyProteoglycanSpecimen Preparation and Treatmentbiology.proteinSafranin Staininglcsh:QCollagensArticular CartilagePLoS ONE
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A custom image-based analysis tool for quantifying elastin and collagen micro-architecture in the wall of the human aorta from multi-photon microscopy

2014

The aorta possesses a micro-architecture that imparts and supports a high degree of compliance and mechanical strength. Alteration of the quantity and/or arrangement of the main load-bearing components of this micro-architecture - the elastin and collagen fibers - leads to mechanical, and hence functional, changes associated with aortic disease and aging. Therefore, in the future, the ability to rigorously characterize the wall fiber micro-architecture could provide insight into the complicated mechanisms of aortic wall remodeling in aging and disease. Elastin and collagen fibers can be observed using state-of-the-art multi-photon microscopy. Image-analysis algorithms have been effective at…

AdultMaleAgingMicro-architectureMaterials scienceFibrillar CollagensBiomedical EngineeringBiophysicsConnective tissueMulti-photon microscopyTortuosityArticleWeight-BearingExtracellular matrixQuantificationmedicine.arteryMicroscopymedicineHumansOrthopedics and Sports MedicineFiberAortaAgedAged 80 and overMicroscopyAortabiologyBinary imageFiber orientationRehabilitationMiddle AgedExtracellular MatrixElastinmedicine.anatomical_structureConnective Tissuebiology.proteinFemaleCollagenElastinAlgorithmsSoftwareBiomedical engineeringJournal of Biomechanics
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Biomechanical properties of oesophagus wall under loading

2003

In this investigation, firstly, the biomechanical properties of different parts of oesophagus were determined. Oesophagus stress and strain are the greatest in the cervical part for all age groups. The human oesophagus deforms unevenly, depending on the direction of load in relation to the organ's axis, it exhibits anisotropical behaviour. With the age the values of mechanical parameters of the oesophagus wall reduce, in particular beginning from 45 years of age, but the modulus of elasticity increases. Biomechanical properties of the oesophagus depend on the architecture of its structure. By loading the organ in the circumferential direction, microfibrilae rupture and deformation of the mu…

AdultMaleAgingMaterials scienceFibrillar collagenFibrillar CollagensBiomedical EngineeringBiophysicsYoung's modulusIn Vitro Techniquessymbols.namesakeEsophagusAge groupsPressureotorhinolaryngologic diseasesEsophagitisHumansOrthopedics and Sports MedicineElasticity (economics)AgedAged 80 and overRehabilitationStress–strain curveAnatomyMiddle AgedElasticitydigestive system diseasesLongitudinal directionCase-Control StudiessymbolsFemaleStress MechanicalJournal of Biomechanics
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Lower strength of the human posterior patellar tendon seems unrelated to mature collagen cross-linking and fibril morphology

2009

The human patellar tendon is frequently affected by tendinopathy, but the etiology of the condition is not established, although differential loading of the anterior and posterior tendon may be associated with the condition. We hypothesized that changes in fibril morphology and collagen cross-linking would parallel differences in material strength between the anterior and posterior tendon. Tendon fascicles were obtained from elective ACL surgery patients and tested micromechanically. Transmission electron microscopy was used to assess fibril morphology, and collagen cross-linking was determined by HPLC and calorimetry. Anterior fascicles were markedly stronger (peak stress: 54.3 ± 21.2 vs.…

AdultMaleCollagen cross linkingPhysiologybusiness.industryFibrillar CollagensPatellar ligamentAnatomyFibrilmedicine.diseasePatellar tendonTendonStructure-Activity RelationshipCross-Linking Reagentsmedicine.anatomical_structurePatellar LigamentTensile StrengthPhysiology (medical)HumansMedicineStress MechanicalTendinopathybusinessFibril morphologyJumper's kneeJournal of Applied Physiology
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