Search results for "collage"

showing 10 items of 638 documents

Type V collagen-induced upregulation of capn2 (large subunit of m-calpain) gene expression and DNA fragmentation in 8701-BC breast cancer cells

2011

Abstract Type V collagen is known to be over-deposited in the stroma of ductal infiltrating carcinomas of the breast. When used as a substrate, type V collagen restrains growth and invasion, and affects gene expression of 8701-BC ductal infiltrating carcinomas cells. Here we supplement existing data by demonstrating type V collagen dependent upregulation of capn2 gene expression in 8701-BC cells through differential display-PCR and Western blot assays. Furthermore, we suggest that our data obtained by centrifugal sedimentation and electrophoresis strongly suggest a correlation between calpain overproduction and DNA fragmentation, since the incubation with calpain inhibitor partly reverts th…

centrifugal sedimentationProtein subunitClinical BiochemistryBreast NeoplasmsDNA FragmentationPolymerase Chain ReactionBiochemistryGene Expression Regulation EnzymologicStromaWestern blotDownregulation and upregulationCell Line TumorGene expressionmedicineHumansSettore BIO/06 - Anatomia Comparata E CitologiaOverproductionMolecular Biologybiologymedicine.diagnostic_testCalpainChemistryGene Expression ProfilingCalpainDNA NeoplasmMolecular biologyUp-Regulationcalpain inhibitordifferential display-PCRgene expressionbiology.proteinDNA fragmentationFemalevoltage gradient gel electrophoresisCollagen Type VBiological Chemistry
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Sponge aggregation factor: identification of the specific collagen-binding site by means of a monoclonal antibody.

1988

The aggregation factor (AF) from the sponge Geodia cydonium is known to be a complex proteinaceous particle, composed of a series of different (glyco)proteins (Mr lower than 150,000) around a 90S sunburst-like core structure. One of the low-Mr proteins is the 47-KD cell binding fragment. We describe a new monoclonal antibody (mAb), III1E6, raised against purified AF particles, which recognizes in tissue slices structures present both on the plasma membrane and in a network-like manner in the extracellular space. By applying immunoelectron microscopical, immunoblotting, and immunoaffinity chromatographical techniques, the mAb III1E6 was shown to recognize the core structure of the AF partic…

chemistry.chemical_classificationBinding SitesHistologyCell adhesion moleculeImmunoelectron microscopyAntibodies MonoclonalProteinsCell CommunicationAdhesionBiologyMolecular biologyPoriferachemistryCell–cell interactionCell surface receptorBiophysicsAnimalsCollagenAnatomyBinding siteCell adhesionGlycoproteinCell Adhesion MoleculesCell AggregationJournal of Histochemistry & Cytochemistry
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The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a lig…

1984

The structure and function of the 2-oxoglutarate binding site of prolyl 4-hydroxylase was studied by assaying the inhibitory potential of 24 selected aliphatic or aromatic compounds. All except one of them inhibited the enzyme competitively with respect to 2-oxoglutarate and noncompetitively with respect to Fe2+, the Ki values ranging from 0.8 microM to over 15 mM. The Ki values for the two most effective inhibitors, pyridine 2,5-dicarboxylate and 2,4-dicarboxylate, were about 0.8 microM and 2 microM, these compounds being the most potent inhibitors of prolyl 4-hydroxylase with respect to 2-oxoglutarate known so far. Only one of the compounds tested, 2-oxoadipinate, was able to support hydr…

chemistry.chemical_classificationCoordination sphereBinding SitesDecarboxylationStereochemistryIronProcollagen-Proline DioxygenaseChick EmbryoLigand (biochemistry)LigandsBiochemistryBinding CompetitiveDecarboxylationHydroxylationchemistry.chemical_compoundEnzymechemistryOxidoreductaseMoietyAnimalsKetoglutaric AcidsFerrous CompoundsBinding siteProtein BindingEuropean journal of biochemistry
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Hypusinated eIF5A is required for the translation of collagen.

2021

ABSTRACT Translation of mRNAs that encode peptide sequences with consecutive prolines (polyproline) requires the conserved and essential elongation factor eIF5A to facilitate the formation of peptide bonds. It has been shown that, upon eIF5A depletion, yeast ribosomes stall in polyproline motifs, but also in tripeptide sequences that combine proline with glycine and charged amino acids. Mammalian collagens are enriched in putative eIF5A-dependent Pro-Gly-containing tripeptides. Here, we show that depletion of active eIF5A in mouse fibroblasts reduced collagen type I α1 chain (Col1a1) content, which concentrated around the nuclei. Moreover, it provoked the upregulation of endoplasmic reticul…

chemistry.chemical_classificationEndoplasmic reticulumRNA-Binding ProteinsTranslation (biology)Cell BiologyTripeptideSaccharomyces cerevisiaeBiologyCell biologyAmino acidElongation factorCollagen type I alpha 1MicechemistryPeptide Initiation FactorsUnfolded protein responseAnimalsCollagenRibosomesPolyproline helixJournal of cell science
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Collagen overglycosylation: a biochemical feature that may contribute to bone quality.

2005

Skeletal ability to resist mechanical stress is determined by bone amount and quality, which relies on macro- and micro-architecture, turnover, bone matrix, and mineralisation; the role of collagen has not been clearly elucidated. Numerous post-translational steps are involved in collagen type I biosynthesis, including residue hydroxylation and glycosylation catalysed by enzymes that work until the protein folds forming the triple helix; therefore, folding rate regulates these processes. Overglycosylated hydroxylysines are poor substrates for epsilon-amino group deamination which initiates cross-link formation. Three clinical conditions associated with fractures may relate collagen overglyc…

chemistry.chemical_classificationGlycosylationGlycosylationOsteoporosisBiophysicsDeaminationCell BiologyOsteogenesis Imperfectamedicine.diseaseBiochemistryBone and BonesHydroxylationPostmenopausechemistry.chemical_compoundEnzymeBiosynthesischemistryBiochemistryDiabetes Mellitus Type 2Osteogenesis imperfectamedicineHumansCollagenMolecular BiologyTriple helixBiochemical and biophysical research communications
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072 Collagen gene expression and tenascin pattern in normal, osteoarthritic, and rheumatoid connective tissues

1992

The extracellular matrix consists of four major components, namely collagens, elastin, proteoglyeans and glycoproteins. Collagens are important members of the ECM, forming a family of at least t 3 different structurally related proteins. Tenascin, synonymous with cytoactin, hexabrachion and J1, is a new member of matrix glycoproteins with a molecular mass of 1200 kD. It exhibits a "hexabrachion" structure with an ellipsoid central globule from which six arms of 75 nm in length diverge in a T-junction arrangement [1]. Rheumatoid arthritis (RA) belongs to the group of connective tissue diseases. In contrast to abundant data about ECM-changes in systemic sclerodermia [2] the matrix alterations…

chemistry.chemical_classificationbiologyChemistryTenascinConnective tissueMatrix (biology)BiochemistryMolecular biologyAnalytical ChemistryExtracellular matrixCollagen type I alpha 1medicine.anatomical_structureGene expressionbiology.proteinmedicineGlycoproteinElastinFresenius' Journal of Analytical Chemistry
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Identification of Type I and IX Collagens in the Ascidian Ciona intestinalis

2001

Immunohistochemical methods showed that a type I collagen is a component of the tunic of Ciona intestinalis, involved in the encapsulation process. Since the fibril-forming collagen types are characterized by triple helical domain with a highly preserved Gly-Xaa-Yaa repeated sequence, a probe coding the fibril-forming type I collagen of the echinoderm Paracentrotus lividus was used to identify ascidian cDNA clones. Northern blot hybridization established that P. lividus probe cross-hybridizes with a 6 Kb C. intestinalis mRNA isolated from the pharynx. Using the echinodermal type I collagen cDNA as a probe several positive clones were identified. Analysis of sequence and the deduced amino ac…

chemistry.chemical_classificationbiologychemistryComplementary DNACiona intestinalisNorthern blotbiology.organism_classificationRepeated sequenceMolecular biologyHomology (biology)Paracentrotus lividusType I collagenAmino acid
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Changes in collagen cross-linking of articular cartilage are revealed by spectral reflectance imaging

2012

Excessive cross-linking of collagen during aging may contribute to degeneration of articular cartilage. Traditionally, the amount of cross-links is derived by using destructive high-performance liquid chromatography (HPLC). However, a sensitive, non-destructive method could help to evaluate tissue integrity, including cross-links. We increased collagen cross-linking in bovine articular cartilage by controlled threose incubation. During the incubation, optical spectral reflectance images of the samples were captured and related to HPLC results using regression analysis. Significant correlations with reflectance and cross-links were observed. When further developed the optical method may enab…

chemistry.chemical_compoundCollagen cross linkingThreoseChemistryIn vivoArticular cartilageReflectivityOptical reflectionBiomedical engineering2012 25th IEEE International Symposium on Computer-Based Medical Systems (CBMS)
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In-vitro Proteoglykansynthese in redifferenzierten Chondrozyten

1989

Human chondrocytes growing in monolayer cultures de-differentiate and produce type I collagen. They re-differentiate and resume their in-vivo characteristics (including the production of type II collagen) when cultured in an agarose-gel. To characterize the modulated cells in more detail, biochemical studies were performed in chondrocytes suspended in agarose for 1 to 3 weeks.

chemistry.chemical_compoundchemistryMonolayerType II collagenAgaroseMolecular biologyIn vitroType I collagen
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Inserto di collagene biodegradabile vs mitomicina-C nella trabeculectomia: risultati a medio termine di uno studio prospettico di fase II.

2010

chirurgia del glaucomaSettore MED/30 - Malattie Apparato Visivotrabeculectomiacollagene biodegradabile
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