Search results for "Procollagen"

showing 10 items of 58 documents

Strong Cooperativity and Loose Geometry between CUB Domains Are the Basis for Procollagen C-Proteinase Enhancer Activity

2009

Procollagen C-proteinase enhancers (PCPE-1 and -2) specifically activate bone morphogenetic protein-1 (BMP-1) and other members of the tolloid proteinase family during C-terminal processing of fibrillar collagen precursors. PCPEs consist of two CUB domains (CUB1 and CUB2) and one NTR domain separated by one short and one long linker. It was previously shown that PCPEs can strongly interact with procollagen molecules, but the exact mechanism by which they enhance BMP-1 activity remains largely unknown. Here, we used a series of deletion mutants of PCPE-1 and two chimeric constructs with repetitions of the same CUB domain to study the role of each domain and linker. Out of all the forms teste…

CooperativityPlasma protein bindingTransfectionBinding CompetitiveBiochemistryBone morphogenetic protein 1Bone Morphogenetic Protein 1Cell LineHumansAmino Acid SequenceBinding siteEnhancerMolecular BiologyGlycoproteinsExtracellular Matrix ProteinsBinding SitesEnzyme Catalysis and RegulationChemistryCircular DichroismCell BiologyCUB domainKineticsProcollagen peptidaseBiochemistryMutationBiophysicsElectrophoresis Polyacrylamide GelLinkerProcollagenProtein BindingJournal of Biological Chemistry
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The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability.

2008

Abstract Lysyl hydroxylase (LH) isoform 3 is a post-translational enzyme possessing LH, collagen galactosyltransferase (GT) and glucosyltransferase (GGT) activities. We have demonstrated that LH3 is found not only intracellularly, but also on the cell surface and in the extracellular space, suggesting additional functions for LH3. Here we show that the targeted disruption of LH3 by siRNA causes a marked reduction of both glycosyltransferase activities, and the overexpression of LH3 in HT-1080 cells increases hydroxylation of lysyl residues and the subsequent galactosylation and glucosylation of hydroxylysyl residues. These data confirm the multi-functionality of LH3 in cells. Furthermore, t…

DNA ComplementaryGlycosylationCell SurvivalLysyl hydroxylaseCellhydroxylysyl glycosylationFluorescent Antibody Techniquelysyl hydroxylaseMicrotubulesPermeabilityCell LineGlycosyltransferasemedicineExtracellularAnimalsHumanscell growthViability assayRNA Small InterferingCell Shapecell viabilityCell ProliferationbiologyCell DeathCell growthProcollagen-Lysine 2-Oxoglutarate 5-Dioxygenasecollagen biosynthesisGlycosyltransferasesCell BiologyArticlesGalactosyltransferasesMolecular biologyPeptide FragmentsCulture MediaActin Cytoskeletonmedicine.anatomical_structurepost-translational modificationCell culturebiology.proteinMolecular MedicineGlucosyltransferaseExtracellular Spacehydroxylysyl glycosyltransferaseJournal of cellular and molecular medicine
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Interferon-alpha 2a increases serum concentration of hyaluronic acid and type III procollagen aminoterminal propeptide in patients with chronic hepat…

1994

Interferon-alpha (IFN-alpha) has become an important drug for the treatment of chronic viral liver diseases. However, the action of IFN-alpha remains unclear. We investigated whether human recombinant IFN-alpha modulates serum concentrations of hyaluronic acid (HA) and type III procollagen aminoterminal propeptide (P-III-NP) in 56 patients with chronic hepatitis-B under IFN-alpha therapy. IFN-alpha increased the HA serum level in 44 of 46 patients and, after cessation of treatment, HA serum levels returned to the pretherapy levels. The increase of HA serum level was higher in patients with active cirrhosis (aC) than in patients with chronic persistent hepatitis (CPH) and in patients with se…

Drugmedicine.medical_specialtyCirrhosisPhysiologymedia_common.quotation_subjectBiopsyInterferon alpha-2Viruslaw.invention03 medical and health scienceschemistry.chemical_compound0302 clinical medicinelawInternal medicineHyaluronic acidMedicineHumansHyaluronic AcidProtein precursor030304 developmental biologymedia_commonHepatitis Chronic0303 health sciencesbusiness.industryGastroenterologyInterferon-alphaHepatologymedicine.diseaseHepatitis BPeptide FragmentsRecombinant Proteins3. Good healthProcollagen peptidaseEndocrinologychemistry030220 oncology & carcinogenesisImmunologyChronic DiseaseRecombinant DNAbusinessProcollagenFollow-Up StudiesDigestive diseases and sciences
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TGF-beta1 in liver fibrosis: an inducible transgenic mouse model to study liver fibrogenesis.

1999

Transforming growth factor-beta1 (TGF-beta1) is a powerful stimulus for collagen formation in vitro. To determine the in vivo effects of TGF-beta1 on liver fibrogenesis, we generated transgenic mice overexpressing a fusion gene [C-reactive protein (CRP)/TGF-beta1] consisting of the cDNA coding for an activated form of TGF-beta1 under the control of the regulatory elements of the inducible human CRP gene promoter. Two transgenic lines were generated with liver-specific overexpression of mature TGF-beta1. After induction of the acute phase response (15 h) with lipopolysaccharide (100 microgram ip), plasma TGF-beta1 levels reached600 ng/ml in transgenic animals, which is100 times above normal …

Genetically modified mouseLipopolysaccharidesmedicine.medical_specialtyTranscription GeneticPhysiologyTransgeneRecombinant Fusion ProteinsMice TransgenicBiologyRegulatory Sequences Nucleic AcidLiver Cirrhosis ExperimentalMiceDownregulation and upregulationFibrosisIn vivoTransforming Growth Factor betaPhysiology (medical)Internal medicinemedicineAnimalsHumansRNA MessengerPromoter Regions GeneticRegulation of gene expressionHepatologyGastroenterologymedicine.diseaseMolecular biologyImmunohistochemistryEndocrinologymedicine.anatomical_structureC-Reactive ProteinGene Expression RegulationLiverHepatocyteHepatic stellate cellCollagenProcollagen
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Role of the Netrin-like Domain of Procollagen C-Proteinase Enhancer-1 in the Control of Metalloproteinase Activity

2010

The netrin-like (NTR) domain is a feature of several extracellular proteins, most notably the N-terminal domain of tissue inhibitors of metalloproteinases (TIMPs), where it functions as a strong inhibitor of matrix metalloproteinases and some other members of the metzincin superfamily. The presence of a C-terminal NTR domain in procollagen C-proteinase enhancers (PCPEs), proteins that stimulate the activity of astacin-like tolloid proteinases, raises the possibility that this might also have inhibitory activity. Here we show that both long and short forms of the PCPE-1 NTR domain, the latter beginning at the N-terminal cysteine known to be critical for TIMP activity, show no inhibition, at …

Glycobiology and Extracellular MatricesMatrix metalloproteinaseBiochemistryBONE MORPHOGENETIC PROTEIN-1AdamalysinFIBRILLAR PROCOLLAGENSTolloid ProteinaseExtracellular Matrix Proteins0303 health sciencesADAMTSFRIZZLED-RELATED PROTEINS030302 biochemistry & molecular biologyTissue Inhibitor of Metalloproteinases11 Medical And Health SciencesALPHA-CONVERTING-ENZYMEI PROCOLLAGENADAM ProteinsExtracellular MatrixPLASMINOGEN ACTIVATIONBiochemistryCollagen03 Chemical SciencesLife Sciences & BiomedicineProcollagenBiochemistry & Molecular BiologyTERMINAL DOMAINTolloid-Like MetalloproteinasesADAMTSBiologyBone morphogenetic protein 1Cell Line03 medical and health sciencesDisintegrinHumansHUMAN TISSUE INHIBITORMatrix MetalloproteinaseMolecular BiologyGlycoproteins030304 developmental biologyThrombospondinScience & TechnologyHeparinADAMCell Biology06 Biological SciencesMATRIX-METALLOPROTEINASESProtein Structure TertiaryADAM ProteinsProcollagen peptidaseSULFATED GLYCOSAMINOGLYCANSEnzymologybiology.proteinJournal of Biological Chemistry
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Processing of procollagen III by meprins: new players in extracellular matrix assembly?

2010

Meprins α and β, a subgroup of zinc metalloproteinases belonging to the astacin family, are known to cleave components of the extracellular matrix, either during physiological remodeling or in pathological situations. In this study we present a new role for meprins in matrix assembly, namely the proteolytic processing of procollagens. Both meprins α and β release the N- and C-propeptides from procollagen III, with such processing events being critical steps in collagen fibril formation. In addition, both meprins cleave procollagen III at exactly the same site as the procollagen C-proteinases, including bone morphogenetic protein-1 (BMP-1) and other members of the tolloid proteinase family. …

Keratinocytesmacromolecular substancesDermatologyMatrix metalloproteinaseCleavage (embryo)BiochemistryBone Morphogenetic Protein 1Substrate SpecificityExtracellular matrix03 medical and health sciencesDermismedicineHumansEnhancerMolecular BiologyCells Cultured030304 developmental biology0303 health sciencesExtracellular Matrix Proteinsintegumentary systemChemistryExtracellular matrix assembly030302 biochemistry & molecular biologyMetalloendopeptidasesCell BiologyDermisFibroblastsFibrosisProcollagen peptidasemedicine.anatomical_structureCollagen Type IIIHEK293 CellsBiochemistryKeloidAstacinThe Journal of investigative dermatology
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Transforming growth factor beta1 T29C gene polymorphism and hypertension: relationship with cardiovascular and renal damage.

2008

Distribution of T29C TGFb1 gene polymorphism was analysed in 260 hypertensive and 134 normotensive subjects. Circulating TGFb1 and procollagen type III levels, microalbuminuria, left ventricular geometry and function were evaluated in all the hypertensives subgrouped according to T29C TGFb1 gene polymorphism. Circulating TGFb1by ELISA technique, procollagen type III by a specific radioimmunoassay, microalbuminuria by radioimmunoassay, left ventricular geometry and function by echocardiography were determined. All groups were comparable for gender, age and sex. Regarding T29C TGFb1 gene polymorphism, prevalence of TC or CC genotypes was significantly (pv0.05) higher in hypertensives than nor…

Key Words: Circulating TGFb1 hypertension left ventricular hypertrophy microalbuminuria procollagen type III TGFb1 gene polymorphism.
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FACIT collagen (1α-chain) is expressed by hemocytes and epidermis during the inflammatory response of the ascidian Ciona intestinalis

2007

Based on previous cloning and sequencing study, real-time PCR and in situ hybridization assays of the inflamed body wall of LPS-injected Ciona intestinalis showed the enhanced gene expression of a collagen with FACIT structural features (Ci-type IX-Col 1alpha-chain). By using specific antibodies raised against an opportunely chosen Ci-type IX-Col synthetic peptide, the fibroblast property of hemocytes challenged in vitro with LPS (at 4h) was displayed by flow cytometry, while immunocytochemistry identified hemocytes with large granules (morula cells) as collagen-producing cells. Hemocyte lysate supernatant analyzed in immunoblotting contained a 60 kDa band identifiable as 1alpha-chain-Ci-ty…

LipopolysaccharidesHemocytesImmunologyImmunocytochemistryIn situ hybridizationCollagen Type IXFACIT collagenExtracellular matrixParacrine CommunicationEscherichia colimedicineAnimalsCiona intestinalisFibroblastIn Situ HybridizationInflammationbiologyEpidermis (botany)Gene Expression Profilingbiology.organism_classificationImmunohistochemistryMolecular biologyCiona intestinalisExtracellular Matrixmedicine.anatomical_structureEpidermal CellsImmunologyEpidermisWound healingProtein Processing Post-TranslationalProcollagenDevelopmental BiologyDevelopmental & Comparative Immunology
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Prediction of progressive liver fibrosis in hepatitis C infection by serum and tissue levels of transforming growth factor-beta.

2001

Although many patients with chronic viral hepatitis C infection suffer from progressive liver disease, the rate of fibrosis progression is highly variable and some patients do not show any measurable progression. However, our ability to predict which patients progress is very limited. Since transforming growth factor-beta (TGF-beta) is a key mediator of liver fibrogenesis, we assessed the predictive role of TGF-beta for fibrogenesis in chronic hepatitis C. We studied 39 patients with chronic hepatitis C in whom two liver biopsies were taken at least 12 months apart, and who did not receive therapy during this period. TGF-beta was measured by bioassay and by ELISA in serum samples taken at t…

Liver CirrhosisMalePathologymedicine.medical_specialtyCirrhosisAntiviral AgentsSeverity of Illness IndexFibrosisPredictive Value of TestsTransforming Growth Factor betaVirologyBiopsymedicineHumansHepatologymedicine.diagnostic_testbusiness.industryAlanine TransaminaseHepatitis CHepatitis C ChronicMiddle AgedViral Loadmedicine.diseaseInfectious DiseasesLiver biopsyPredictive value of testsChronic DiseaseDisease ProgressionFemalebusinessViral loadProgressive diseaseBiomarkersProcollagenJournal of viral hepatitis
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Identification of Novel pro-α2(IX) Collagen Gene Mutations in Two Families with Distinctive Oligo-Epiphyseal Forms of Multiple Epiphyseal Dysplasia

1999

Multiple epiphyseal dysplasia (MED) is a genetically heterogeneous disorder with marked clinical and radiographic variability. Traditionally, the mild "Ribbing" and severe "Fairbank" types have been used to define a broad phenotypic spectrum. Mutations in the gene encoding cartilage oligomeric-matrix protein have been shown to result in several types of MED, whereas mutations in the gene encoding the alpha2 chain of type IX collagen (COL9A2) have so far been found only in two families with the Fairbank type of MED. Type IX collagen is a heterotrimer of pro-alpha chains derived from three distinct genes-COL9A1, COL9A2, and COL9A3. In this article, we describe two families with distinctive ol…

MaleAdolescentRNA SplicingMutantGene mutationBiologyOsteochondrodysplasiasmedicine.disease_causeMultiple epiphyseal dysplasia03 medical and health sciencesExon0302 clinical medicineOsteoarthritismedicineGeneticsHumansGenetics(clinical)Genetic TestingOsteochondrodysplasiaMultiple epiphyseal dysplasiaGene mutationAlleleChildPolymorphism Single-Stranded ConformationalGenetics (clinical)030304 developmental biologyGenetics0303 health sciencesMutationType IX collagenGenetic heterogeneitymedicine.diseaseOsteochondrodysplasiaPedigreeRadiographyCartilageChild PreschoolMutationFemaleEpiphysesProcollagen030217 neurology & neurosurgeryResearch ArticleThe American Journal of Human Genetics
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