0000000000530859

AUTHOR

Benno Jungblut

showing 2 related works from this author

EGFL7 ligates αvβ3 integrin to enhance vessel formation

2013

Angiogenesis, defined as blood vessel formation from a preexisting vasculature, is governed by multiple signal cascades including integrin receptors, in particular integrin αVβ3. Here we identify the endothelial cell (EC)-secreted factor epidermal growth factor-like protein 7 (EGFL7) as a novel specific ligand of integrin αVβ3, thus providing mechanistic insight into its proangiogenic actions in vitro and in vivo. Specifically, EGFL7 attaches to the extracellular matrix and by its interaction with integrin αVβ3 increases the motility of EC, which allows EC to move on a sticky underground during vessel remodeling. We provide evidence that the deregulation of EGFL7 in zebrafish embryos leads …

EGF Family of ProteinsEmbryo NonmammalianAngiogenesisAmino Acid MotifsImmunologyIntegrinGene ExpressionMice NudeEndothelial Growth FactorsBiochemistryCollagen receptorMiceCell MovementCell AdhesionHuman Umbilical Vein Endothelial CellsmedicineAnimalsHumansImmunoprecipitationPhosphorylationZebrafishbiologyReverse Transcriptase Polymerase Chain ReactionChemistryCalcium-Binding ProteinsInfarction Middle Cerebral ArteryVenous plexusCell BiologyHematologyIntegrin alphaVbeta3ImmunohistochemistryExtracellular MatrixCell biologyEndothelial stem cellHEK293 Cellsmedicine.anatomical_structureIntegrin alpha MImmunologybiology.proteinBlood VesselsRNA InterferenceIntegrin beta 6Protein BindingBlood vesselBlood
researchProduct

Ubiquitin-independent function of optineurin in autophagic clearance of protein aggregates.

2013

Summary Aggregation of misfolded proteins and the associated loss of neurons are considered a hallmark of numerous neurodegenerative diseases. Optineurin is present in protein inclusions observed in various neurodegenerative diseases including amyotrophic lateral sclerosis (ALS), Huntington's disease, Alzheimer's disease, Parkinson's disease, Creutzfeld-Jacob disease and Pick's disease. Optineurin deletion mutations have also been described in ALS patients. However, the role of optineurin in mechanisms of protein aggregation remains unclear. In this report, we demonstrate that optineurin recognizes various protein aggregates via its C-terminal coiled-coil domain in a ubiquitin-independent m…

HuntingtinSOD1AggrephagyCell Cycle ProteinsMice TransgenicProtein aggregationBiologyArticle03 medical and health sciencesMice0302 clinical medicineTANK-binding kinase 1UbiquitinTranscription Factor TFIIIAAutophagyAnimalsHumansPhosphorylationZebrafishZebrafish030304 developmental biologyOptineurin0303 health sciencesUbiquitinamyotrophic lateral sclerosis; Huntington disease; Huntingtin; optineurin; phosphorylation; SOD1; TBK1; ubiquitinMembrane Transport ProteinsNeurodegenerative DiseasesCell Biologybiology.organism_classification3. Good healthMice Inbred C57BLDisease Models AnimalCancer researchbiology.protein030217 neurology & neurosurgeryHeLa CellsProtein BindingJournal of cell science
researchProduct