0000000000042647

AUTHOR

Friedrich Koch-nolte

0000-0003-1730-6674

showing 2 related works from this author

CD38-Specific Biparatopic Heavy Chain Antibodies Display Potent Complement-Dependent Cytotoxicity Against Multiple Myeloma Cells

2018

CD38 is overexpressed by multiple myeloma cells and has emerged as a target for therapeutic antibodies. Nanobodies are soluble single domain antibody fragments derived from the VHH variable domain of heavy chain antibodies naturally occurring in camelids. We previously identified distinct llama nanobodies that recognize three non-overlapping epitopes of the extracellular domain of CD38. Here, we fused these VHH domains to the hinge, CH2, and CH3 domains of human IgG1, yielding highly soluble chimeric llama/human heavy chain antibodies (hcAbs). We analyzed the capacity of these hcAbs to mediate complement-dependent cytotoxicity (CDC) to CD38-expressing human multiple myeloma and Burkitt lymp…

0301 basic medicinelcsh:Immunologic diseases. AllergyRecombinant Fusion ProteinsImmunologyAntineoplastic AgentsEpitope03 medical and health sciencesbiparatopic antibodiesAntigens Neoplasmhemic and lymphatic diseasesCell Line TumorAntibodies BispecificImmunology and AllergyAnimalsHumansCytotoxicitycomplement-dependent cytotoxicityOriginal ResearchHeavy-chain antibodybiologyheavy chain antibodyantibody engineeringChemistryAntibody-Dependent Cell CytotoxicityDaratumumabAntibodies MonoclonalComplement System ProteinsSingle-Domain AntibodiesADP-ribosyl Cyclase 1Complement-dependent cytotoxicityCell biologymultiple myelomananobody030104 developmental biologySingle-domain antibodyCell culturebiology.proteinEpitopes B-LymphocyteImmunotherapyAntibodylcsh:RC581-607Immunoglobulin Heavy ChainsCamelids New WorldCD38Frontiers in Immunology
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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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