0000000000020651

AUTHOR

Paolo Mignatti

0000-0002-8157-457x

showing 2 related works from this author

Shedding of Membrane Vesicles Mediates Fibroblast Growth Factor-2 Release from Cells

2003

Fibroblast growth factor-2 (FGF-2), a polypeptide with regulatory activity on cell growth and differentiation, lacks a conventional secretory signal sequence, and its mechanism of release from cells remains unclear. We characterized the role of extracellular vesicle shedding in FGF-2 release. Viable cells released membrane vesicles in the presence of serum. However, in serum-free medium vesicle shedding was dramatically down-regulated, and the cells did not release FGF-2 activity into their conditioned medium. Addition of serum to serum-starved cells rapidly induced intracellular FGF-2 clustering under the plasma membrane and into granules that colocalized with patches of the cell membrane …

SerumFGF-2 extracellular vesiclesBiologyFibroblast growth factorBiochemistryCulture Media Serum-FreeSettore MED/13 - EndocrinologiaCell Line; Tumor; Endothelial Cells; Fibroblast Growth Factor 2; Secretory VesiclesCell LineCell membraneSettore BIO/13 - Biologia ApplicataCell Line TumorSettore BIO/10 - BiochimicamedicineHumansProtein IsoformsFibroblastMolecular BiologyTumorSecretory VesiclesVesicleCell MembraneEndothelial CellsCell BiologyExtracellular vesicleSecretory VesicleCell biologyKineticsmedicine.anatomical_structureMicroscopy FluorescenceCell cultureFibroblast Growth Factor 2IntracellularJournal of Biological Chemistry
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Urokinase Plasminogen Activator and Gelatinases Are Associated with Membrane Vesicles Shed by Human HT1080 Fibrosarcoma Cells

1997

Membrane vesicles are shed by tumor cells both in vivo and in vitro. Although their functions are not well understood, it has been proposed that they may play multiple roles in tumor progression. We characterized membrane vesicles from human HT1080 fibrosarcoma cell cultures for the presence of proteinases involved in tumor invasion. By gelatin zymography and Western blotting, these vesicles showed major bands corresponding to the zymogen and active forms of gelatinase B (MMP-9) and gelatinase A (MMP-2) and to the MMP-9. tissue inhibitor of metalloproteinase 1 complex. Both gelatinases appeared to be associated with the vesicle membrane. HT1080 cell vesicles also showed a strong, plasminoge…

GelatinasesMacromolecular SubstancesFibrosarcomaBlotting WesternCellGelatinase ABiologyBiochemistryTumor Cells CulturedmedicineHumansCollagenasesFibrinolysinMolecular BiologyGlycoproteinsUrokinaseEnzyme PrecursorsVesicleMetalloendopeptidasesTissue Inhibitor of MetalloproteinasesCell BiologyTissue inhibitor of metalloproteinaseUrokinase-Type Plasminogen ActivatorMolecular biologyExtracellular MatrixUrokinase receptorBloodmedicine.anatomical_structureMatrix Metalloproteinase 9GelatinasesMatrix Metalloproteinase 2HT1080medicine.drugJournal of Biological Chemistry
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