Search results for "Bone Morphogenetic Protein"

showing 10 items of 68 documents

In-vitro regulation of odontogenic gene expression in human embryonic tooth cells and SHED cells

2012

The bud-to-cap stage transition during early tooth development is a time when the tooth-inducing potential becomes restricted to the mesenchyme. Several key genes, expressed in the mesenchyme at this stage, are an absolute requirement for the progression of tooth development. These include the transcription factors Msx1 and Pax9. The inductive potential of tooth mesenchyme cells is a key requisite for whole-tooth bioengineering and thus identification of cells that can retain this property following expansion in culture is an important as yet unresolved, goal. We show here that in-vitro culture of embryonic human tooth mesenchyme cells and SHED cells express low levels of PAX9 and MSX1 and …

MesodermCell signalingHistologyMesenchymeSHEDPAX9MSX1tissue engineering cell signallingBone Morphogenetic Protein 4BiologyCell LinePathology and Forensic MedicineMesodermstomatognathic systemmedicineHumansChildMSX1 Transcription FactorRegulation of gene expressionMesenchymal stem cellGene Expression Regulation DevelopmentalCell BiologyEmbryonic stem cellCell biologystomatognathic diseasesmedicine.anatomical_structureBone morphogenetic protein 4Cell cultureImmunologyOdontogenesisPAX9 Transcription FactorToothSignal TransductionCell and Tissue Research
researchProduct

Functional and structural insights into astacin metallopeptidases

2012

The astacins are a family of multi-domain metallopeptidases with manifold functions in metabolism. They are either secreted or membrane-anchored and are regulated by being synthesized as inactive zymogens and also by colocalizing protein inhibitors. The distinct family members consist of N-terminal signal peptides and pro-segments, zincdependent catalytic domains, further downstream extracellular domains, transmembrane anchors, and cytosolic domains. The catalytic domains of four astacins and the zymogen of one of these have been structurally characterized and shown to comprise compact ~200-residue zinc-dependent moieties divided into an N-terminal and a C-terminal sub-domain by an active-s…

MetzincinSignal peptideStereochemistryMolecular Sequence DataClinical BiochemistryTolloidMatrix metalloproteinaseBiologyBiochemistryEvolution Molecular03 medical and health sciencesEnzyme activatorBone morphogenetic proteinsZymogenAnimalsHumansProtease InhibitorsAmino Acid SequenceTyrosineMolecular BiologyPeptide sequence030304 developmental biologyEnzyme Precursors0303 health sciences030302 biochemistry & molecular biologyMetalloendopeptidasesMeprinTransmembrane protein3. Good healthEnzyme ActivationBiochemistryAstacinCatalytic domainsbchm
researchProduct

Sizzled Is Unique among Secreted Frizzled-related Proteins for Its Ability to Specifically Inhibit Bone Morphogenetic Protein-1 (BMP-1)/Tolloid-like …

2012

BMP-1/tolloid-like proteinases (BTPs) are major enzymes involved in extracellular matrix assembly and activation of bioactive molecules, both growth factors and anti-angiogenic molecules. Although the control of BTP activity by several enhancing molecules is well established, the possibility that regulation also occurs through endogenous inhibitors is still debated. Secreted frizzled-related proteins (sFRPs) have been studied as possible candidates, with highly contradictory results, after the demonstration that sizzled, a sFRP found in Xenopus and zebrafish, was a potent inhibitor of Xenopus and zebrafish tolloid-like proteases. In this study, we demonstrate that mammalian sFRP-1, -2, and …

Models MolecularProteasesFrizzledanimal structuresMolecular Sequence DataXenopusXenopus ProteinsBiochemistryBone morphogenetic protein 1Bone Morphogenetic Protein 1MiceXenopus laevismedicineAnimalsHumansProtease InhibitorsAmino Acid SequenceMolecular BiologyZebrafishGlycoproteinsSequence Homology Amino AcidbiologyExtracellular matrix assemblyfungiIntracellular Signaling Peptides and ProteinsTissue Inhibitor of MetalloproteinasesCell BiologySurface Plasmon Resonancebiology.organism_classificationMatrix MetalloproteinasesRecombinant ProteinsExtracellular MatrixWnt ProteinsBiochemistryMechanism of actionembryonic structuresEnzymologySignal transductionmedicine.symptomPeptide HydrolasesSignal TransductionJournal of Biological Chemistry
researchProduct

Meprins, membrane-bound and secreted astacin metalloproteinases

2008

The astacins are a subfamily of the metzincin superfamily of metalloproteinases. The first to be characterized was the crayfish enzyme astacin. To date more than 200 members of this family have been identified in species ranging from bacteria to humans. Astacins are involved in developmental morphogenesis, matrix assembly, tissue differentiation and digestion. Family members include the procollagen C-proteinase (BMP1, bone morphogenetic protein 1), tolloid and mammalian tolloid-like, HMP (Hydra vulgaris metalloproteinase), sea urchin BP10 (blastula protein) and SPAN (Strongylocentrotus purpuratus astacin), the 'hatching' subfamily comprising alveolin, ovastacin, LCE, HCE ('low' and 'high' c…

Models MolecularSubfamilyanimal structuresProtein ConformationClinical BiochemistryMolecular Sequence DataMatrix metalloproteinaseBiochemistryBone morphogenetic protein 1ArticleSubstrate SpecificityExtracellular matrixIntestinal mucosaAnimalsHumansTissue DistributionAmino Acid SequenceIntestinal MucosaMolecular BiologyPhylogenybiologyMetalloendopeptidasesGeneral Medicinebiology.organism_classificationStrongylocentrotus purpuratusMolecular biologyCell biologyProtein Subunitsembryonic structuresMolecular MedicineMATH domainAstacin
researchProduct

The effect of intracavernosal growth differentiation factor-5 therapy in a rat model of cavernosal nerve injury.

2006

OBJECTIVE To determine whether the intracavernosal application of growth differentiation factor-5 (GDF-5) influences nerve regeneration and erectile function after cavernosal nerve injury in a rat model. MATERIALS AND METHODS Thirty-two male Sprague-Dawley rats were randomly divided into four equal groups: eight had a sham operation (uninjured controls), while 24 had bilateral cavernosal nerve crush. The crush-injury groups were treated at the time of injury with an impregnated collagen sponge implanted into the right corpus cavernosum. The sponge contained no GDF-5 (injured controls), 2 µg (low concentration), or 20 µg GDF-5 (high concentration). Erectile function was assessed by cavernosa…

NephrologyMalemedicine.medical_specialtyUrologyRat modelUrologyStimulationRats Sprague-DawleyRandom AllocationErectile DysfunctionGrowth Differentiation Factor 5Internal medicinemedicineAnimalsTrauma Nervous Systembusiness.industryGrowth differentiation factorNerve injurymedicine.diseaseNerve RegenerationRatsErectile dysfunctionEndocrinologyCollagen spongeNerve crushBone Morphogenetic Proteinsmedicine.symptombusinessPenisBJU international
researchProduct

Neuroprotective Potential of GDF11: Myth or Reality?

2019

In the brain, aging is accompanied by cellular and functional deficiencies that promote vulnerability to neurodegenerative disorders. In blood plasma from young and old animals, various factors such as growth differentiation factor 11 (GDF11), whose levels are elevated in young animals, have been identified. The blood concentrations of these factors appear to be inversely correlated with the age-related decline of neurogenesis. The identification of GDF11 as a “rejuvenating factor” opens up perspectives for the treatment of neurodegenerative diseases. As a pro-neurogenic and pro-angiogenic agent, GDF11 may constitute a basis for novel therapeutic strategies.

OpinionNeurogenesisNeovascularization PhysiologicNeuroprotectionCatalysislcsh:ChemistryInorganic ChemistryBlood plasmaAnimalsHumansRejuvenationrejuvenating factorsMedicinePhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopybusiness.industryOrganic ChemistryNeurogenesisBrainGeneral MedicineComputer Science ApplicationsGrowth Differentiation Factorslcsh:Biology (General)lcsh:QD1-999Bone Morphogenetic ProteinsGDF11GDF11neuroprotectionbusinessNeuroscienceBiomarkersInternational Journal of Molecular Sciences
researchProduct

Inorganic Polyphosphates: Biologically Active Biopolymers for Biomedical Applications

2013

Inorganic polyphosphate (polyP) is a widely occurring but only rarely investigated biopolymer which exists in both prokaryotic and eukaryotic organisms. Only in the last few years, this polymer has been identified to cause morphogenetic activity on cells involved in human bone formation. The calcium complex of polyP was found to display a dual effect on bone-forming osteoblasts and bone-resorbing osteoclasts. Exposure of these cells to polyP (Ca2+ complex) elicits the expression of cytokines that promote the mineralization process by osteoblasts and suppress the differentiation of osteoclast precursor cells to the functionally active mature osteoclasts dissolving bone minerals. The effect o…

PolyphosphateRegulatorBiological activityBiologyBone morphogenetic protein 2Proinflammatory cytokineCell biologychemistry.chemical_compoundMediatormedicine.anatomical_structurechemistryOsteoclastPrecursor cellmedicine
researchProduct

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
researchProduct

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
researchProduct

Human germ cell differentiation from fetal- and adult-derived induced pluripotent stem cells

2010

Historically, our understanding of molecular genetic aspects of human germ cell development has been limited, at least in part due to inaccessibility of early stages of human development to experimentation. However, the derivation of pluripotent stem cells may provide the necessary human genetic system to study germ cell development. In this study, we compared the potential of human induced pluripotent stem cells (iPSCs), derived from adult and fetal somatic cells to form primordial and meiotic germ cells, relative to human embryonic stem cells. We found that ∼5% of human iPSCs differentiated to primordial germ cells (PGCs) following induction with bone morphogenetic proteins. Furthermore, …

Recombinant Fusion ProteinsInduced Pluripotent Stem CellsEmbryoid bodyHaploidyBiologyCell LineDEAD-box RNA Helicases03 medical and health sciences0302 clinical medicineGeneticsmedicineHumansInduced pluripotent stem cellMolecular BiologyEmbryonic Stem CellsGenetics (clinical)030304 developmental biology0303 health sciences030219 obstetrics & reproductive medicineSynaptonemal ComplexGene Expression ProfilingGene Expression Regulation DevelopmentalRNA-Binding ProteinsCell DifferentiationArticlesGeneral MedicineEmbryonic stem cellMolecular biologyGerm Cellsmedicine.anatomical_structureBone Morphogenetic ProteinsGerm line developmentStem cellReprogrammingGerm cellAdult stem cellHuman Molecular Genetics
researchProduct