0000000000843928

AUTHOR

Isabell Cornelsen

showing 2 related works from this author

Melittin Modulates Keratinocyte Function through P2 Receptor-dependent ADAM Activation

2012

Melittin, the major component of the bee venom, is an amphipathic, cationic peptide with a wide spectrum of biological properties that is being considered as an anti-inflammatory and anti-cancer agent. It modulates multiple cellular functions but the underlying mechanisms are not clearly understood. Here, we report that melittin activates disintegrin-like metalloproteases (ADAMs) and that downstream events likely contribute to the biological effects evoked by the peptide. Melittin stimulated the proteolysis of ADAM10 and ADAM17 substrates in human neutrophil granulocytes, endothelial cells and murine fibroblasts. In human HaCaT keratinocytes, melittin induced shedding of the adhesion molecu…

KeratinocytesCell SurvivalBlotting WesternADAM17 ProteinP2 receptorBiologyModels Biologicalcomplex mixturesBiochemistryMelittinCell LineADAM10 ProteinMicechemistry.chemical_compoundTransactivationAdenosine TriphosphateAnimalsHumansPhosphorylationExtracellular Signal-Regulated MAP KinasesReceptorMolecular BiologyCells CulturedMice KnockoutDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionPurinergic receptorHEK 293 cellstechnology industry and agricultureMembrane ProteinsCell BiologyFibroblastsCadherinsEmbryo MammalianMelittenCell biologyErbB ReceptorsADAM ProteinsHaCaTHEK293 CellschemistryPhosphorylationlipids (amino acids peptides and proteins)Receptors Purinergic P2X7Amyloid Precursor Protein SecretasesJournal of Biological Chemistry
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Unsaturated Fatty Acids Drive Disintegrin and Metalloproteinase (ADAM)-dependent Cell Adhesion, Proliferation, and Migration by Modulating Membrane F…

2011

The disintegrin-metalloproteinases ADAM10 and ADAM17 mediate the release of several cell signaling molecules and cell adhesion molecules such as vascular endothelial cadherin or L-selectin affecting endothelial permeability and leukocyte transmigration. Dysregulation of ADAM activity may contribute to the pathogenesis of vascular diseases, but the mechanisms underlying the control of ADAM functions are still incompletely understood. Atherosclerosis is characterized by lipid plaque formation and local accumulation of unsaturated free fatty acids (FFA). Here, we show that unsaturated FFA increase ADAM-mediated substrate cleavage. We demonstrate that these alterations are not due to genuine ch…

KeratinocytesMembrane FluidityADAM10Lipid BilayersVascular permeabilityBiologyADAM17 ProteinBiochemistryCapillary PermeabilityADAM10 ProteinCell MovementMembrane fluidityCell AdhesionAnimalsHumansCell adhesionMolecular BiologyCell ProliferationCell adhesion moleculeCell growthFluorescence recovery after photobleachingEndothelial CellsMembrane ProteinsCell BiologyAtherosclerosisADAM ProteinsCell biologyLipoproteins LDLADAM ProteinsHEK293 CellsFatty Acids UnsaturatedCholesterol EstersRabbitsAmyloid Precursor Protein SecretasesGranulocytes
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