Search results for "Procollagen"

showing 8 items of 58 documents

Role of reactive oxygen species in the regulation of HIF-1 by prolyl hydroxylase 2 under mild hypoxia

2012

The function and survival of eukaryotic cells depends on a constant and sufficient oxygen supply. Cells recognize and respond to hypoxia by accumulation of the transcription factor hypoxia-inducible factor 1 (HIF-1), composed of an oxygen-sensitive HIF-1α and a constitutive HIF-1β subunit. Besides physiology, HIF-1 induction is involved in major pathological processes such as cardiovascular disease, inflammation and cancer, which are associated with the formation of reactive oxygen species (ROS). ROS have been reported to affect HIF-1 activity but the role for ROS in regulating HIF-1 has not been definitely settled. In order to shed light on the redox-regulation of HIF-1 by ROS, we studied …

Transcriptional ActivationProcollagen-Proline DioxygenaseMedizinBiologyTransfectionBiochemistryHypoxia-Inducible Factor-Proline DioxygenasesTransactivationCell Line TumormedicineHumansRNA Small InterferingTranscription factorchemistry.chemical_classificationRegulation of gene expressionReactive oxygen speciesGene knockdownGeneral MedicineTransfectionHydrogen PeroxideHypoxia (medical)Cell HypoxiaCell biologyHypoxia-inducible factorschemistryBiochemistryHypoxia-Inducible Factor 1medicine.symptomReactive Oxygen SpeciesOxidation-Reduction
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Effect of dual blockade of renin-angiotensin system on TGF beta 1 and left ventricular structure and function in hypertensive patients

2007

The effects of 24 weeks losartan and ramipril treatment,both alone and in combination, on left ventricular mass (LVM), circulating transforming growth factor b1(TGFb1), procollagen type I (PIP) and III (PIIIP), havebeen evaluated in hypertensive (HT) patients. A total of 57 HT with stage 1 and 2 essential hypertension were included. After 4 weeks run in, a randomized double blind, three arms, double dummy, independent trial was used. All HT patients were randomly allocated to three treatment arms consisting of losartan (50 mg/daily),ramipril (5 mg/ daily) and combined (losartan 50 mg/daily plus ramipril 5 mg/daily) for 24 weeks. TGFb1, PIP and PIIIP, LVM, LVM/h 2.7 and other echocardiograph…

angiotensin II receptor blockertransforming growth factor b1left ventricular geometry and functionprocollagen type I and IIIace-inhibitor
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Procollagen C-proteinase Enhancer Stimulates Procollagen Processing by Binding to the C-propeptide Region Only*

2011

Background: Procollagen C-proteinase enhancer-1 (PCPE-1) is an extracellular glycoprotein that increases activity of certain zinc metalloproteinases involved in tissue development and repair. Results: PCPE-1 binds uniquely to the C-propeptide region of the procollagen molecule. Conclusion: PCPE-1 enhances proteolysis by binding solely to the procollagen C-propeptides. Significance: These data may lead to future applications in the development of antifibrotic therapies.

animal structuresGlycosylationBiologyBiochemistryBone morphogenetic protein 1Protein Structure SecondaryBone Morphogenetic Protein 103 medical and health scienceschemistry.chemical_compoundMetalloprotease0302 clinical medicineHumansBinding siteEnhancerMolecular Biology030304 developmental biologyCell Line TransformedGlycoproteinschemistry.chemical_classification0303 health sciencesMetalloproteinaseExtracellular Matrix ProteinsBinding Sitesintegumentary systemCell BiologyEnzymatic ProcessingFibrosisExtracellular MatrixProcollagen peptidaseCollagen Type IIIchemistryBiochemistry030220 oncology & carcinogenesisembryonic structuresEnzymologyCollagenGlycoproteinProtein Processing Post-TranslationalTriple helixThe Journal of Biological Chemistry
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Influence of oxygen tension on the anti-inflammatory and chondroprotective effects of heme oxygenase-1 in healthy and osteoarthritic human chondrocyt…

2012

s / Osteoarthritis and Cartilage 20 (2012) S54–S296 S136 their isolation. The absence of cross-reaction with the IIA isoform was established by ELISA andWB. In addition, the Saos-2 cell linewas chosen to test a possible labelling of other fibrillar procollagens, mainly type I, V and XI. In fact, this cell line is described to synthesize the (a1)I, (a2)I, (a1)V, (a2)V, (a1)XI and (a2)XI, but no (a3)XI chains. No signal was detected on WB of cellular extracts or conditioned media with anti-pNIIB52, whereas antibodies to the collagen I, V and XI triple-helical parts revealed indeed the presence of proforms of these collagens. Conclusions: Anti-pNIIB52 antibodies allow a very sensitive and spec…

biologyChemistryCartilageBiomedical Engineeringbiology.organism_classificationMolecular biologyOxygen tensionHeme oxygenaseProcollagen peptidasechemistry.chemical_compoundmedicine.anatomical_structureRheumatologyCell culturebiology.proteinmedicineOrthopedics and Sports MedicineAntibodyHemeValenciaOsteoarthritis and Cartilage
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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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Fibrosis markers and CRIM1 increase in chronic heart failure of increasing severity.

2014

AbstractBackground: Fibrosis suppressors/activators in chronic heart failure (CHF) is a topic of investigation.Aim: To quantify serum levels of fibrosis regulators in CHF.Methods: ELISA tests were used to quantify fibrosis regulators, procollagen type-(PIP)I, (PIP)III, collagen-I, III, BMP1,2,3,7, SDF1α, CXCR4, fibulin 1,2,3, BMPER, CRIM1 and BAMBI in 66 CHF (NYHA class I, n = 9; II, n = 34; III n = 23), and in 14 controls.Results: In CHF, TGFβR2, PIPIII, SDF1α and CRIM1 were increased. PIPIII correlated with CRIM1.Conclusions: The BMPs inhibitor CRIM1 is increased and correlates with higher levels of serum PIPIII showing an imbalance in favor of pro-fibrotic mechanisms in CHF.

medicine.medical_specialtyHealth Toxicology and MutagenesisClinical BiochemistryInflammationBiochemistryGastroenterologySeverity of Illness IndexBone morphogenetic protein 1ElectrocardiographyFibrosisInternal medicinemedicineEndothelial dysfunction heart fibrosis inflammationHumanscardiovascular diseasesEndothelial dysfunctionHeart Failurebusiness.industryMembrane ProteinsBone Morphogenetic Protein Receptorsmedicine.diseaseFibulinProcollagen peptidaseHeart failureImmunologyChronic Diseasecardiovascular systemBAMBImedicine.symptombusinesscirculatory and respiratory physiology
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Increased mRNAs for procollagens and key regulating enzymes in rat skeletal muscle following downhill running.

1999

The purpose of the study was to investigate pre-translational regulation of collagen expression after a single bout of exercise. We analysed steady-state messenger ribonucleic acid (mRNA) levels for collagen types I, III and IV, alpha- and beta-subunits of prolyl 4-hydroxylase and lysyl oxidase (enzymes modifying procollagen chains), and enzyme activity of prolyl 4-hydroxylase from rat soleus muscle (MS) and the red parts of quadriceps femoris muscle (MQF) after 12 h and after 1, 2, 4, 7 and 14 days of downhill (-13.5 degrees ) treadmill running at a speed of 17 m.min-1 for 130 min. Histological and biochemical assays revealed exercise-induced muscle damage in MQF but not MS. Steady-state m…

medicine.medical_specialtyPhysiologyClinical BiochemistryPhysical ExertionProcollagen-Proline DioxygenaseLysyl oxidaseBiologyRunningProtein-Lysine 6-OxidaseHydroxyprolinechemistry.chemical_compoundType IV collagenPhysiology (medical)Internal medicineGene expressionmedicineAnimalsExertionRNA MessengerRats WistarMuscle SkeletalGlucuronidaseSoleus muscleSkeletal muscleBlotting NorthernRatsProcollagen peptidaseEndocrinologymedicine.anatomical_structurechemistryFemaleCollagenProcollagenPflugers Archiv : European journal of physiology
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Enhanced prolylhydroxylase activity in the posterior annulus fibrosus of canine intervertebral discs following long-term running exercise

2010

The effect of long-term excercise on the intervertebral disc collagen concentration (hydroxyproline), collagen-synthesizing enzymes (prolyl-4-hydroxylase, PH, and galactosyl-hydroxylysyl glucosyltransferase, GGT) and hydroxypyridinium crosslinks was studied in ten female beagle dogs. The dogs were run on a treadmill for 1 year starting at the age of 15 weeks. The daily running distance was gradually increased to 40km, which distance the dogs ran for the final 15 weeks. Ten untrained dogs from the same breeding colony served as controls. The nucleus pulposus and anterior and posterior halves of the annulus fibrosus of C2-3, T10-12, L4-5 disc segments were analysed. Crosslinks were measured f…

musculoskeletal diseasesTime FactorsProcollagen-Proline DioxygenaseBeagleThoracic VertebraeHydroxyprolinechemistry.chemical_compoundDogsLumbarStress PhysiologicalPhysical Conditioning AnimalmedicineAnimalsOrthopedics and Sports MedicineTreadmillIntervertebral DiscAnnulus (mycology)Lumbar VertebraePhysical conditioningbusiness.industryIntervertebral discAnatomymusculoskeletal systemBiomechanical PhenomenaHydroxyprolinemedicine.anatomical_structurechemistryGlucosyltransferasesModels AnimalCollagen metabolismCervical VertebraePhysical EnduranceFemaleSurgeryCollagenbusinessEuropean Spine Journal
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