0000000000281415

AUTHOR

Sandra Gilbert

showing 3 related works from this author

Structural requirements for V2 vasopressin receptor proteolytic cleavage.

1999

The ligand-induced proteolytic cleavage of the V2 vasopressin receptor transiently expressed in COS cells was investigated. After incubation of the cell membranes with a photoreactive ligand possessing full agonistic properties for V2 receptors, approximately 90% of the porcine and bovine V2 vasopressin receptors were cleaved in the upper part of transmembrane helix 2 at a heptapeptide sequence conserved in both vasopressin and oxytocin receptors. The oxytocin receptor was completely resistant to proteolysis after binding the same photoreactive ligand, which is only a partial agonist for this receptor. Chimeric V2/oxytocin receptors obtained by transfer of extracellular domains of the oxyto…

Models MolecularReceptors VasopressinDNA ComplementaryTime FactorsProtein ConformationSwineMolecular Sequence DataBiologyLigandsTransfectionBiochemistryArginine vasopressin receptor 2Enzyme-linked receptorCyclic AMPAnimalsHumansPoint Mutation5-HT5A receptorAmino Acid SequenceCloning MolecularReceptorProtease-activated receptor 2Vasopressin receptorArginine vasopressin receptor 1BDose-Response Relationship DrugSequence Homology Amino AcidProteinsOxytocin receptorProtein Structure TertiaryEnzyme ActivationBiochemistryMicroscopy FluorescenceReceptors OxytocinType C PhospholipasesCOS CellsMutagenesis Site-DirectedCattlehormones hormone substitutes and hormone antagonistsAdenylyl CyclasesProtein BindingEuropean journal of biochemistry
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α-Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

2001

Disintegrin metalloproteases from different organisms form the ADAM (a disintegrin and metalloprotease) family. All members display a common domain organization and possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signaling. Members of the ADAM family are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain. The proteolytic process is referred to as ectodomain shedding, which is activated by phorbol esters and inhibited by hydroxamic acid-based inhibitors. We have shown that the disintegrin metalloprotease ADAM 10 has both constitutive and regulated alpha-secretase activity. Expression of a dominant n…

Cell signalingDisintegrinsMolecular Sequence DataProtein domainBiologyGeneral Biochemistry Genetics and Molecular BiologyADAM10 ProteinAmyloid beta-Protein PrecursorHistory and Philosophy of ScienceEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansProtease InhibitorsAmino Acid SequenceCell adhesionMetalloproteinaseGeneral NeuroscienceHEK 293 cellsMembrane ProteinsMetalloendopeptidasesRecombinant ProteinsTransmembrane proteincarbohydrates (lipids)ADAM ProteinsBiochemistryEctodomainbiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAnnals of the New York Academy of Sciences
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Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulat…

2003

Tumor necrosis factor-alpha converting enzyme (TACE or ADAM17) is a member of the ADAM (a disintegrin and metalloproteinase) family of type I membrane proteins and mediates the ectodomain shedding of various membrane-anchored signaling and adhesion proteins. TACE is synthesized as an inactive zymogen, which is subsequently proteolytically processed to the catalytically active form. We have identified the proprotein-convertases PC7 and furin to be involved in maturation of TACE. This maturation is negatively influenced by the phorbol ester phorbol-12-myristate-13-acetate (PMA), which decreases the cellular amount of the mature form of TACE in PMA-treated HEK293 and SH-SY5Y cells. Furthermore…

DNA ComplementaryTime FactorsADAM10Blotting WesternGenetic VectorsADAM17 ProteinTransfectionBiochemistryCell LineAmyloid beta-Protein PrecursorAlzheimer DiseaseZymogenEndopeptidasesPhorbol EstersCell AdhesionTumor Cells CulturedAnimalsAspartic Acid EndopeptidasesHumansSubtilisinsProtein kinase A signalingFurinProtein Kinase CProtein kinase CFurinMetalloproteinasebiologyChemistryMetalloendopeptidasesCyclic AMP-Dependent Protein KinasesPeptide FragmentsRatsCell biologyADAM ProteinsEctodomainBiochemistrybiology.proteinTetradecanoylphorbol AcetateCattleTumor necrosis factor alphaProprotein ConvertasesAmyloid Precursor Protein SecretasesSignal TransductionEuropean Journal of Biochemistry
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