0000000000822460

AUTHOR

Cécile Bijakowski

showing 3 related works from this author

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
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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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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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