Search results for "Procollagen"

showing 10 items of 58 documents

Long-Term Structural and Functional Myocardial Adaptations in Healthy Living Kidney Donors: A Pilot Study

2015

Background and Aims Compensatory renal hypertrophy following unilateral nephrectomy (UNX) occurs in the remaining kidney. However, the long-Term cardiac adaptive process to UNX remains poorly defined in humans. Our goal was to characterize myocardial structure and function in living kidney donors (LKDs), approximately 12 years after UNX. Methods and Results Cardiac function and structure in 15 Italian LKDs, at least 5 years after UNX (median time from donation = 8.4 years) was investigated and compared to those of age and sex matched U.S. citizens healthy controls (n = 15). Standard and speckle tracking echocardiography (STE) was performed in both LKDs and controls. Plasma angiotensin II, a…

Malemedicine.medical_specialtylcsh:MedicinePilot Projectschemistry.chemical_compoundInternal medicineNatriuretic Peptide BrainLiving DonorsmedicineHumanslcsh:ScienceAldosteroneKidney transplantationAgedKidneyMultidisciplinaryAldosteronebusiness.industryAngiotensin IIMyocardiumlcsh:RMyocardial adaptations Kidney donorsCompensatory renal hypertrophyHeartMiddle AgedUnilateral nephrectomymedicine.diseaseSettore MED/11 - Malattie Dell'Apparato CardiovascolareKidney TransplantationAngiotensin IIPeptide FragmentsStructure and functionCardiovascular physiologyCross-Sectional Studiesmedicine.anatomical_structureEndocrinologychemistryCardiologylcsh:QFemalebusinessSettore M-EDF/01 - Metodi E Didattiche Delle Attivita' MotorieAtrial Natriuretic FactorProcollagenResearch ArticlePLOS ONE
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Metalloproteases meprin α and meprin β are C- and N-procollagen proteinases important for collagen assembly and tensile strength.

2013

Type I fibrillar collagen is the most abundant protein in the human body, crucial for the formation and strength of bones, skin, and tendon. Proteolytic enzymes are essential for initiation of the assembly of collagen fibrils by cleaving off the propeptides. We report that Mep1a −/− and Mep1b −/− mice revealed lower amounts of mature collagen I compared with WT mice and exhibited significantly reduced collagen deposition in skin, along with markedly decreased tissue tensile strength. While exploring the mechanism of this phenotype, we found that cleavage of full-length human procollagen I heterotrimers by either meprin α or meprin β led to the generation of mature collagen molecules that s…

Materials scienceConnective tissueCHO CellsCollagen Type IMiceCricetulusFibrosisCricetinaeTensile StrengthmedicineAnimalsHumansProtein precursorSkinMice KnockoutMetalloproteinaseMultidisciplinaryProteolytic enzymesMetalloendopeptidasesProcollagen N-EndopeptidaseBiological Sciencesmedicine.diseaseCell biologyProcollagen peptidaseCollagen type I alpha 1medicine.anatomical_structureHEK293 CellsBiochemistryProteolysisProcollagen N-EndopeptidaseProceedings of the National Academy of Sciences of the United States of America
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Association between biomarkers of inflammation and left ventricular hypertrophy in moderate chronic kidney disease.

2007

Aims: Left ventricular hyper- trophy (LVH) is a predictor for cardiovascu- lar mortality, and it is considered to be a surro- gate marker of preclinical cardiovascular dis- ease. This study aimed at evaluating whether fetuin-A plasma levels are decreased in pa- tients with moderate chronic kidney disease (CKD) and their linkage to plasma concentra- tions of hs-C-reactive protein (CRP), cardio- trophyn-1 (CT-1), tumor necrosis factor- (TNF-), propeptide of collagen Type I (PIP) and to LVH. Material and methods: We enrolled 64 moderate CKD and 55 essential hypertensives (EH) with normal renal func- tion as controls. All the patients underwent an echocardiographic examination; plasma sam- ples…

NephrologyAdultMalePhosphopeptidesmedicine.medical_specialtyInflammationEnzyme-Linked Immunosorbent AssayLeft ventricular hypertrophyMuscle hypertrophyinflammation left ventricular hypertrophy chronic kidney diseaseStatistical significanceInternal medicineMedicineHumansMass indexcardiovascular diseasesInflammationAnalysis of Variancebusiness.industryTumor Necrosis Factor-alphaCase-control studyGeneral MedicineMiddle Agedmedicine.diseaseEndocrinologyC-Reactive ProteinNephrologyEchocardiographyCase-Control StudiesCardiologyCytokinesKidney Failure ChronicRegression AnalysisFemaleHypertrophy Left Ventricularalpha-Fetoproteinsmedicine.symptombusinessBiomarkersProcollagenKidney diseaseClinical nephrology
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Identification of a novel recurrent 1q42.2-1qter deletion in high risk MYCN single copy 11q deleted neuroblastomas

2012

Neuroblastoma is an aggressive embryonal tumor that accounts for similar to 15% of childhood cancer deaths. Hitherto, despite the availability of comprehensive genomic data on DNA copy number changes in neuroblastoma, relatively little is known about the genes driving neuroblastoma tumorigenesis. In this study, high resolution array comparative genome hybridization (CGH) was performed on 188 primary neuroblastoma tumors and 33 neuroblastoma cell lines to search for previously undetected recurrent DNA copy number gains and losses. A new recurrent distal chromosome 1q deletion (del(1)(q42.2qter)) was detected in seven cases. Further analysis of available array CGH datasets revealed 13 additio…

Neuroblastoma/geneticsCancer ResearchProcollagen-Proline DioxygenaseMedizinGene Dosagecomparative genomic hybridizationBiologymedicine.disease_causeGene dosageN-Myc Proto-Oncogene ProteinFumarate HydrataseHypoxia-Inducible Factor-Proline DioxygenasesNeuroblastomaProcollagen-Proline Dioxygenase/geneticsCell Line TumorNeuroblastomamedicineHumansFumarate Hydratase/geneticsGeneOncogene ProteinsGeneticsN-Myc Proto-Oncogene ProteinChromosomes Human Pair 11BreakpointNuclear ProteinsChromosomemedicine.diseaseOncogene Proteins/geneticsNuclear Proteins/geneticsOncologyChromosome DeletionCarcinogenesisComparative genomic hybridization
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Genetic disorders of connective tissues

1991

Due to the growing knowledge of structure and function of extracellular matrix proteins, congenital abnormalities of connective tissues are identified or suspected in an increasing number of clinical disorders. In osteogenesis imperfecta and two subtypes of Ehlers-Danlos syndrome, the affected matrix proteins were identified and mutations in the corresponding genes (procollagen type I and type III, respectively) could be demonstrated. Some forms of chondrodysplasia were shown to be associated with mutations in the gene encoding for the cartilage-specific collagen (type II). In part, the clinical phenotype is determined by the tissue-specific distribution of these collagens. However, the cor…

Pathologymedicine.medical_specialtyMutationbusiness.industryOsteoarthritisOsteogenesis ImperfectaMatrix (biology)medicine.disease_causemedicine.diseaseProcollagen Type IPhenotypeExtracellular matrixPhenotypeRheumatologyOsteogenesis imperfectaMutationmedicineHumansCollagenConnective Tissue DiseasesbusinessGeneCurrent Opinion in Rheumatology
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Specific hepatic delivery of procollagen α1(I) small interfering RNA in lipid‐like nanoparticles resolves liver fibrosis

2015

Fibrosis accompanies the wound-healing response to chronic liver injury and is characterized by excessive hepatic collagen accumulation dominated by collagen type I that often progresses to cirrhosis. Here we present ample in-vivo evidence of an up to 90% suppression of procollagen α1(I) expression, a reduction of septa formation and a 40–60% decrease of collagen deposition in mice with progressive and advanced liver fibrosis, that received cationic lipid nanoparticles loaded with small interfering RNA to the procollagen α1(I) gene (LNP-siCol1a1). After intravenous injection up to ninety percent of LNP-siCol1a1 were retained in the liver of fibrotic mice and accumulated in nonparenchymal > …

Pathologymedicine.medical_specialtySmall interfering RNACirrhosisHepatologyRNABiologymedicine.diseaseProcollagen peptidaseFibrosisParenchymamedicineMyofibroblastGeneHepatology
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The interaction of recombinant subdomains of the procollagen C-proteinase with procollagen I provides a quantitative explanation for functional diffe…

2006

The procollagen C-proteinase (PCP) is a zinc peptidase of the astacin family and the metzincin superfamily. The enzyme removes the C-terminal propeptides of fibrillar procollagens and activates other matrix proteins. Besides its catalytic protease domain, the procollagen C-proteinase contains several C-terminal CUB modules (named after complement factors C1r and C1s, the sea urchin UEGF protein, and BMP-1) and EGF-like domains. The two major splice forms of the C-proteinase differ in their overall domain composition. The longer variant, termed mammalian tolloid (mTld, i.e., PCP-2), has the protease- CUB1-CUB2-EGF1-CUB3-EGF2-CUB4-CUB5 composition, whereas the shorter form termed bone morphog…

ProteasesProtein FoldingTolloid-Like Metalloproteinasesmedicine.medical_treatmentRNA SplicingBiologyAntiparallel (biochemistry)BiochemistryBone morphogenetic protein 1law.inventionBone Morphogenetic Protein 1lawmedicineAnimalsProtein precursorDNA PrimersProteaseBase SequenceCircular DichroismMetalloendopeptidasesSurface Plasmon ResonanceRecombinant ProteinsProcollagen peptidaseSpectrometry FluorescenceBiochemistryBone Morphogenetic ProteinsRecombinant DNAMetalloproteasesElectrophoresis Polyacrylamide GelAstacinProcollagenBiochemistry
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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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The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains.

2007

Abstract Procollagen C-proteinase (PCP) removes the C-terminal pro-peptides of procollagens and also processes other matrix proteins. The major splice form of the PCP is termed BMP1 (bone morphogenetic protein 1). Active BMP1 is composed of an astacin-like protease domain, three CUB (complement, sea urchin Uegf, BMP1) domains and one EGF-like domain. Here we compare the recombinant human full-length BMP1 with its isolated proteolytic domain to further unravel the functional influence of the CUB and EGF domains. We show that the protease domain alone cleaves truncated procollagen VII within the short telopeptide region into fragments of similar size as the full-length enzyme does. However, u…

Protein FoldingCollagen Type VIIDNA Complementarymedicine.medical_treatmentClinical BiochemistryAmino Acid MotifsGene ExpressionGlutamic AcidBiochemistryBone morphogenetic protein 1Mass SpectrometryBone Morphogenetic Protein 1Cell LineSubstrate SpecificityProtein structuremedicineEscherichia coliAnimalsHumansCysteineDisulfidesMolecular BiologyInclusion BodiesMetalloproteinaseProteasebiologyChemistryMetalloendopeptidasesRecombinant ProteinsProtein Structure TertiaryFibronectinProcollagen peptidaseDrosophila melanogasterBiochemistryBone Morphogenetic ProteinsMutationbiology.proteinProtein foldingAstacinBiological chemistry
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Recruitment of HIF-1α and HIF-2α to common target genes is differentially regulated in neuroblastoma: HIF-2α promotes an aggressive phenotype

2006

In neuroblastoma specimens, HIF-2alpha but not HIF-1alpha is strongly expressed in well-vascularized areas. In vitro, HIF-2alpha protein was stabilized at 5% O2 (resembling end capillary oxygen conditions) and, in contrast to the low HIF-1alpha activity at this oxygen level, actively transcribed genes like VEGF. Under hypoxia (1% O2), HIF-1alpha was transiently stabilized and primarily mediated acute responses, whereas HIF-2alpha protein gradually accumulated and governed prolonged hypoxic gene activation. Knockdown of HIF-2alpha reduced growth of neuroblastoma tumors in athymic mice. Furthermore, high HIF-2alpha protein levels were correlated with advanced clinical stage and high VEGF expr…

Transcriptional ActivationCancer ResearchProcollagen-Proline DioxygenaseAggressive phenotypeCELLCYCLEBiologyMiceNeuroblastomaNeuroblastomaBasic Helix-Loop-Helix Transcription FactorsTumor Cells CulturedmedicineAnimalsHumansRNA MessengerChildHypoxiaGeneOligonucleotide Array Sequence AnalysisRegulation of gene expressionGene knockdownGene Expression ProfilingCell BiologyCell cycleHypoxia (medical)Hypoxia-Inducible Factor 1 alpha Subunitmedicine.diseaseIn vitroGene Expression Regulation NeoplasticOxygenPhenotypeOncologyImmunologyCancer researchFemalemedicine.symptomNeoplasm TransplantationCancer Cell
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