Search results for " Collage"

showing 10 items of 161 documents

High Efficiency In Vitro Wound Healing of Dictyophora indusiata Extracts via Anti-Inflammatory and Collagen Stimulating (MMP-2 Inhibition) Mechanisms

2021

Dictyophora indusiata or Phallus indusiatus is widely used as not only traditional medicine, functional foods, but also, skin care agents. Biological activities of the fruiting body from D. indusiata were widely reported, while the studies on the application of immature bamboo mushroom extracts were limited especially in the wound healing effect. Wound healing process composed of 4 stages including hemostasis, inflammation, proliferation, and remodelling. This study divided the egg stage of bamboo mushroom into 3 parts: peel and green mixture (PGW), core (CW), and whole mushroom (WW). Then, aqueous extracts were investigated for their nucleotide sequencing, biological compound contents, and…

Microbiology (medical)bamboo mushroomQH301-705.5Dictyophora indusiatacollagen stimulating activityanti-inflammatory; bamboo mushroom; collagen stimulating activity; <i>Dictyophora indusiata</i>; matrix metalloproteinase-2 activity; wound healingQuímica farmacèuticawound healingPlant ScienceArticlematrix metalloproteinase-2 activityBiology (General)<i>Dictyophora indusiata</i>Ecology Evolution Behavior and Systematicsanti-inflammatoryJournal of Fungi
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alpha 11beta 1 integrin recognizes the GFOGER sequence in interstitial collagens.

2002

The integrins alpha(1)beta(1), alpha(2)beta(1), alpha(10)beta(1), and alpha(11)beta(1) are referred to as a collagen receptor subgroup of the integrin family. Recently, both alpha(1)beta(1) and alpha(2)beta(1) integrins have been shown to recognize triple-helical GFOGER (where single letter amino acid nomenclature is used, O = hydroxyproline) or GFOGER-like motifs found in collagens, despite their distinct binding specificity for various collagen subtypes. In the present study we have investigated the mechanism whereby the latest member in the integrin family, alpha(11)beta(1), recognizes collagens using C2C12 cells transfected with alpha(11) cDNA and the bacterially expressed recombinant a…

Models MolecularIntegrinsDNA ComplementaryReceptors CollagenPhenylalanineIntegrinAmino Acid MotifsPlasma protein bindingBiochemistrylaw.inventionCollagen receptorMiceProtein structurelawCell AdhesionAnimalsHumansMagnesiumMolecular BiologyBinding selectivityCells Culturedchemistry.chemical_classificationbiologyDose-Response Relationship DrugCell BiologyPrecipitin TestsRecombinant ProteinsAmino acidProtein Structure TertiaryKineticschemistryBiochemistrybiology.proteinRecombinant DNACalciumCollagenPeptidesType I collagenProtein BindingThe Journal of biological chemistry
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"RKKH" peptides from the snake venom metalloproteinase of Bothrops jararaca bind near the metal ion-dependent adhesion site of the human integrin alp…

1999

Integrin alpha(1)beta(1) and alpha(2)beta(1) are the major cellular receptors for collagen, and collagens bind to these integrins at the inserted I-domain in their alpha subunit. We have previously shown that a cyclic peptide derived from the metalloproteinase domain of the snake venom protein jararhagin blocks the collagen-binding function of the alpha(2) I-domain. Here, we have optimized the structure of the peptide and identified the site where the peptide binds to the alpha(2) I-domain. The peptide sequence Arg-Lys-Lys-His is critical for recognition by the I-domain, and five negatively charged residues surrounding the "metal ion-dependent adhesion site" (MIDAS) of the I-domain, when mu…

Models MolecularIntegrinsReceptors CollagenIntegrinMolecular Sequence DataIntegrin alpha2PeptidePeptide bindingBiochemistryAntigens CDCrotalid VenomsAnimalsHumansBothropsComputer SimulationAmino Acid SequenceMolecular BiologyPeptide sequencechemistry.chemical_classificationMetalloproteinaseBinding SitesbiologySequence Homology Amino AcidChemistryActive siteMetalloendopeptidasesCell BiologyCyclic peptidePeptide FragmentsCell biologyBiochemistryJararhaginbiology.proteinMutagenesis Site-DirectedCell Adhesion MoleculesProtein BindingThe Journal of biological chemistry
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Evaluation of the healing of precoated vascular dacron prostheses.

1991

Knitted and woven Dacron grafts commercially coated with bovine collagen, gelatin and human albumin were implanted end-to-side between the infrarenal aorta and the bifurcation in 35 growing pigs. Grafts were explanted after 4, 8 and 12 weeks and compared to 6 uncoated knitted prostheses preclotted with blood that served as a control. Uncoated grafts rapidly developed a firmly attached neointima lined with endothelium. Compared with coated grafts the thrombus-free area of uncoated grafts was significantly larger (P less than 0.05). The slow resorption of albumin resulted in a delayed and incomplete neointimal healing and failing graft incorporation. Although the bovine collagen was only mini…

Neointimamedicine.medical_specialtyBovine collagenfood.ingredientEndotheliumSurface PropertiesSwineProsthesis DesignGelatinfoodmedicineAnimalsSerum AlbuminWound Healingbusiness.industryPolyethylene TerephthalatesAlbuminGraft Occlusion VascularCapsuleHyperplasiamedicine.diseaseSurgeryResorptionBlood Vessel ProsthesisProsthesis Failuremedicine.anatomical_structureMicroscopy Electron ScanningGelatinSurgeryFemaleCollagenEndothelium VascularbusinessBiomedical engineeringLangenbecks Archiv fur Chirurgie
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Shell Extracts from the Marine Bivalve Pecten maximus Regulate the Synthesis of Extracellular Matrix in Primary Cultured Human Skin Fibroblasts

2014

International audience; Mollusc shells are composed of more than 95% calcium carbonate and less than 5% of an organic matrix consisting mostly of proteins, glycoproteins and polysaccharides. Previous studies have elucidated the biological activities of the shell matrices from bivalve molluscs on skin, especially on the expression of the extracellular matrix components of fibroblasts. In this work, we have investigated the potential biological activities of shell matrix components extracted from the shell of the scallop Pecten maximus on human fibroblasts in primary culture. Firstly, we demonstrated that shell matrix components had different effects on general cellular activities. Secondly, …

Pathologylcsh:Medicine[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC][CHIM.THER]Chemical Sciences/Medicinal ChemistryBiochemistryExtracellular matrixCell SignalingMolecular Cell Biologylcsh:ScienceSkinConnective Tissue Cellschemistry.chemical_classificationPectenMultidisciplinary[ CHIM.THER ] Chemical Sciences/Medicinal ChemistryExtracellular MatrixCell biologymedicine.anatomical_structureConnective TissueScallopCytochemistryAnatomyCellular Structures and OrganellesType I collagenResearch ArticleBiotechnologySignal Transductionmedicine.medical_specialtyPrimary Cell CultureExtracellular Matrix SignalingBiologyBiomaterialsDermisAnimal ShellsmedicineAnimalsHumansPecten maximus14. Life underwaterTissue Extractslcsh:R[ SDV.BC.BC ] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Biology and Life SciencesCell BiologyFibroblastsbiology.organism_classificationIn vitroBiological TissuechemistryCell culturelcsh:QGlycoprotein
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SPARC oppositely regulates inflammation and fibrosis in bleomycin-induced lung damage.

2011

Fibrosis results from inflammatory tissue damage and impaired regeneration. In the context of bleomycin-induced pulmonary fibrosis, we demonstrated that the matricellular protein termed secreted protein acidic and rich in cysteine (SPARC) distinctly regulates inflammation and collagen deposition, depending on its cellular origin. Reciprocal Sparc(-/-) and wild-type (WT) bone marrow chimeras revealed that SPARC expression in host fibroblasts is required and sufficient to induce collagen fibrosis in a proper inflammatory environment. Accordingly, Sparc(-/-) >WT chimeras showed exacerbated inflammation and fibrosis due to the inability of Sparc(-/-) macrophages to down-regulate tumor necrosis …

Pathologymedicine.medical_specialtyAnimals; Bleomycin; Bone Marrow Cells; Chimera; Collagen; Down-Regulation; Fibroblasts; Leukocytes; Macrophages; Mice; Mice Inbred BALB C; Osteonectin; Pneumonia; Pulmonary Fibrosis; Transforming Growth Factor beta; Tumor Necrosis Factor-alphaPulmonary FibrosisDown-RegulationInflammationBone Marrow CellsBiologyPathology and Forensic MedicineMiceFibrosisTumor necrosis factor productionTransforming Growth Factor betaPulmonary fibrosismedicineLeukocytesAnimalsOsteonectinInbred BALB CChimeraTumor Necrosis Factor-alphaMacrophagesMatricellular proteinRegular ArticleSPARCTransforming growth factor betaPneumoniaFibroblastsBLEOMYCINmedicine.diseaseSPARC; BLEOMYCIN; LUNG DAMAGELUNG DAMAGECancer researchbiology.proteinTumor necrosis factor alphaCollagenmedicine.symptomOsteonectin
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Structure and Function of Matrix Components in the Cruciate Ligaments

1992

In the present study, the matrix components of 100 cruciate ligaments were analyzed by conventional electron microscopy, immunohistology, morphometry, and immunoelectron microscopy. The anterior (ACL) and the posterior (PCL) cruciate ligaments contained collagen types III, IV, and VI. Several structural glycoproteins, like fibronectin, laminin, entactin, tenascin, and undulin were detected using monoclonal antibodies. Whereas laminin and entactin were higher concentrated in the PCL, type VI collagen was more frequently found in the ACL. The ACL had a critical nourishment in its distal and middle thirds. In all ligament parts the PCL revealed a better vascular supply with strong correlation …

Pathologymedicine.medical_specialtyHistologybiologyChemistryImmunoelectron microscopyTenascinmusculoskeletal systemExtracellular matrixFibronectinCruciate ligamentType IV collagenmedicine.anatomical_structureLamininbiology.proteinmedicineLigamentAnatomyhuman activitiesCells Tissues Organs
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Expression of osteopontin messenger RNA and protein in rheumatoid arthritis: Effects of osteopontin on the release of collagenase 1 from articular ch…

2000

Objective Osteopontin (OPN) is an extracellular matrix protein that has been implicated in the interactions between tumor cells and host matrix, including those involved in invasion and spread of tumor cells. Because joint destruction in rheumatoid arthritis (RA) is mediated by the invasive growth of synovial tissue through its attachment to cartilage, we examined the expression of OPN in the synovia of patients with RA and the effect of OPN on the production of collagenase 1 in rheumatoid synovial fibroblasts and articular chondrocytes. Methods The expression of OPN messenger RNA (mRNA) and protein in synovia from 10 RA patients was examined by in situ hybridization and immunohistochemistr…

Pathologymedicine.medical_specialtybiologyCartilageImmunologyMolecular biologyChondrocyteExtracellular matrixmedicine.anatomical_structurestomatognathic systemRheumatologybiology.proteinCollagenasemedicineImmunology and AllergyInterstitial collagenasePharmacology (medical)OsteopontinSynovial membraneFibroblastmedicine.drugArthritis &amp; Rheumatism
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A comparison of spreading and motility behaviour of 8701-BC breast carcinoma cells on type I, I-trimer and type V collagen substrata. Evidence for a …

1991

Ductal infiltrating carcinoma (d.i.c.) of human breast is a highly invasive neoplasm characterized by enhanced deposition of collagen. Paradoxically, enhanced collagen deposition is not correlated with inhibition of the migration of tumour cells into the host tissue. d.i.c. is characterized by the reappearance of ‘embryonic’ type I-trimer collagen and an increase in type V collagen content in the matrix. The effects of these two collagen types were compared with type I collagen as culture substrata on the spreading pattern, cytoskeletal organization and motile behaviour of 8701-BC breast carcinoma cells using rhodamine-phalloidin staining, a DNAase I-competition assay, scanning electron mic…

PhotomicrographyStromal cellVideotape RecordingMotilityBreast NeoplasmsTrimerCell BiologyMatrix (biology)BiologyActinsCulture MediaExtracellular MatrixCell biologyCollagen type I alpha 1Carcinoma Intraductal NoninfiltratingCell MovementCell cultureImmunologyTumor Cells CulturedHumansCollagenNeoplasm MetastasisCytoskeletonType I collagenJournal of Cell Science
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Inhibition of prolyl hydroxylation and procollagen processing in chick-embryo calvaria by a derivative of pyridine-2,4-dicarboxylate. Characterizatio…

1991

The biochemical and morphological consequences of procollagen prolyl 4-hydroxylase inhibition by pyridine-2,4-dicarboxylic acid (2,4-PDCA) and its diethyl ester (diethyl-2,4-PDC) were studied in chick-embryo calvaria, which predominantly synthesize type I collagen. Half-maximal inhibition of tissue hydroxyproline formation required 650 microM-2,4-PDCA, whereas the Ki with respect to chicken prolyl 4-hydroxylase in vitro was 2 microM. In contrast, half-maximal inhibition was caused by 10 microM-diethyl-2,4-PDC in the intact calvaria, although chicken prolyl 4-hydroxylase in vitro was not inhibited even at 1 mM. The collagenous material produced in the presence of diethyl-2,4-PDC showed an al…

Protein DenaturationProtein ConformationPyridinesProcollagen-Proline DioxygenaseCalvariaChick EmbryoEndoplasmic ReticulumModels BiologicalBiochemistryBone and BonesHydroxylationHydroxyprolinechemistry.chemical_compoundmedicineAnimalsMolecular BiologyCells CulturedEndoplasmic reticulumCell BiologyIn vitroKineticsProcollagen peptidasemedicine.anatomical_structurechemistryBiochemistryMicrosomeCollagenProcollagenType I collagenResearch ArticleBiochemical Journal
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