0000000000822463

AUTHOR

Florence Ruggiero

0000-0003-2915-5359

showing 2 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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