Search results for "Cell adhesion molecule"

showing 10 items of 469 documents

Structural basis of the migfilin-filamin interaction and competition with integrin beta tails.

2008

A link between sites of cell adhesion and the cytoskeleton is essential for regulation of cell shape, motility, and signaling. Migfilin is a recently identified adaptor protein that localizes at cell-cell and cell-extracellular matrix adhesion sites, where it is thought to provide a link to the cytoskeleton by interacting with the actin cross-linking protein filamin. Here we have used x-ray crystallography, NMR spectroscopy, and protein-protein interaction studies to investigate the molecular basis of migfilin binding to filamin. We report that the N-terminal portion of migfilin can bind all three human filamins (FLNa, -b, or -c) and that there are multiple migfilin-binding sites in FLNa. H…

Models MolecularIntegrin beta ChainsMagnetic Resonance SpectroscopyFilaminsIntegrinMolecular ConformationPlasma protein bindingmacromolecular substancesBiologyFilaminLigandsBiochemistryMiceContractile ProteinsFLNAAnimalsHumansCytoskeletonCell adhesionMolecular BiologyActinCytoskeletonDose-Response Relationship DrugMicrofilament ProteinsMechanisms of Signal TransductionSignal transducing adaptor proteinCell BiologyCell biologyCytoskeletal Proteinsbiology.proteinNIH 3T3 CellsCell Adhesion MoleculesProtein BindingThe Journal of biological chemistry
researchProduct

"RKKH" peptides from the snake venom metalloproteinase of Bothrops jararaca bind near the metal ion-dependent adhesion site of the human integrin alp…

1999

Integrin alpha(1)beta(1) and alpha(2)beta(1) are the major cellular receptors for collagen, and collagens bind to these integrins at the inserted I-domain in their alpha subunit. We have previously shown that a cyclic peptide derived from the metalloproteinase domain of the snake venom protein jararhagin blocks the collagen-binding function of the alpha(2) I-domain. Here, we have optimized the structure of the peptide and identified the site where the peptide binds to the alpha(2) I-domain. The peptide sequence Arg-Lys-Lys-His is critical for recognition by the I-domain, and five negatively charged residues surrounding the "metal ion-dependent adhesion site" (MIDAS) of the I-domain, when mu…

Models MolecularIntegrinsReceptors CollagenIntegrinMolecular Sequence DataIntegrin alpha2PeptidePeptide bindingBiochemistryAntigens CDCrotalid VenomsAnimalsHumansBothropsComputer SimulationAmino Acid SequenceMolecular BiologyPeptide sequencechemistry.chemical_classificationMetalloproteinaseBinding SitesbiologySequence Homology Amino AcidChemistryActive siteMetalloendopeptidasesCell BiologyCyclic peptidePeptide FragmentsCell biologyBiochemistryJararhaginbiology.proteinMutagenesis Site-DirectedCell Adhesion MoleculesProtein BindingThe Journal of biological chemistry
researchProduct

International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G Protein–Coupled Receptors

2015

The Adhesion family forms a large branch of the pharmacologically important superfamily of G protein-coupled receptors (GPCRs). As Adhesion GPCRs increasingly receive attention from a wide spectrum of biomedical fields, the Adhesion GPCR Consortium, together with the International Union of Basic and Clinical Pharmacology Committee on Receptor Nomenclature and Drug Classification, proposes a unified nomenclature for Adhesion GPCRs. The new names have ADGR as common dominator followed by a letter and a number to denote each subfamily and subtype, respectively. The new names, with old and alternative names within parentheses, are: ADGRA1 (GPR123), ADGRA2 (GPR124), ADGRA3 (GPR125), ADGRB1 (BAI1…

Models MolecularSocieties ScientificSubfamilyComputational biologyBiologyGPR110PharmacologyLigandsGPR113Second Messenger SystemsReceptors G-Protein-CoupledCell MovementTerminology as TopicCell AdhesionCyclic AMPAnimalsHumansProtein IsoformsReceptorNomenclatureG protein-coupled receptorPharmacologyCell MembraneInternational AgenciesAdhesionQPGPR56Pharmacology ClinicalIUPHAR Nomenclature ReportsMolecular MedicineQP517Cell Adhesion MoleculesSignal TransductionPharmacological Reviews
researchProduct

Synthesis, in vitro activity, and three-dimensional quantitative structure-activity relationship of novel hydrazine inhibitors of human vascular adhe…

2010

Vascular adhesion protein-1 (VAP-1) belongs to the semicarbazide-sensitive amine oxidases (SSAOs) that convert amines into aldehydes. SSAOs are distinct from the mammalian monoamine oxidases (MAOs), but their substrate specificities are partly overlapping. VAP-1 has been proposed as a target for anti-inflammatory drug therapy because of its role in leukocyte adhesion to endothelium. Here, we describe the synthesis and in vitro activities of novel series of VAP-1 selective inhibitors. In addition, the molecular dynamics simulations performed for VAP-1 reveal that the movements of Met211, Ser496, and especially Leu469 can enlarge the ligand-binding pocket, allowing larger ligands than those s…

Models MolecularSubstrate SpecificitiesQuantitative structure–activity relationshipMolecular ConformationQuantitative Structure-Activity RelationshipMolecular Dynamics SimulationLigandsMolecular dynamicsCricetulusCricetinaeDrug DiscoveryAnimalsHumansMonoamine OxidaseBinding SitesChemistryStereoisomerismIn vitrorespiratory tract diseasesRatsMonoamine neurotransmitterHydrazinesBiochemistryDocking (molecular)Molecular MedicineAmine gas treatingAmine Oxidase (Copper-Containing)Cell Adhesion MoleculesVASCULAR ADHESION PROTEIN 1Protein BindingJournal of medicinal chemistry
researchProduct

The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended

2012

Filamins are large proteins that cross-link actin filaments and connect to other cellular components. The C-terminal rod 2 region of FLNa (filamin A) mediates dimerization and interacts with several transmembrane receptors and intracellular signalling adaptors. SAXS (small-angle X-ray scattering) experiments were used to make a model of a six immunoglobulin-like domain fragment of the FLNa rod 2 (domains 16–21). This fragment had a surprising three-branched structural arrangement, where each branch was made of a tightly packed two-domain pair. Peptides derived from transmembrane receptors and intracellular signalling proteins induced a more open structure of the six domain fragment. Mutagen…

Models Moleculargenetics [Receptors Dopamine D3]metabolism [Recombinant Proteins]Protein Conformationgenetics [Antigens CD18]chemistry [Recombinant Proteins]Plasma protein bindingCrystallography X-RayLigandsFilaminmetabolism [Antigens CD18]metabolism [Cytoskeletal Proteins]BiochemistryfilaminsContractile ProteinsProtein structuremetabolism [Peptide Fragments]FLNAchemistry [Antigens CD18]genetics [Cell Adhesion Molecules]Small-angle X-ray scatteringMicrofilament Proteinsgenetics [Contractile Proteins]Recombinant Proteinschemistry [Receptors Dopamine D3]FBLIM1 protein humanddc:540Domain (ring theory)DimerizationProtein Bindingchemistry [Contractile Proteins]FilaminsAntigens CD18metabolism [Cell Adhesion Molecules]BiologyScattering Small Anglemetabolism [Receptors Dopamine D3]Humanschemistry [Microfilament Proteins]Protein Interaction Domains and Motifsmetabolism [Mutant Proteins]DRD3 protein humanMolecular Biologymetabolism [Contractile Proteins]Actingenetics [Cytoskeletal Proteins]Cryoelectron MicroscopyMutagenesista1182Receptors Dopamine D3metabolism [Microfilament Proteins]Cell Biologychemistry [Cell Adhesion Molecules]genetics [Peptide Fragments]Peptide FragmentsCytoskeletal ProteinsCrystallographychemistry [Mutant Proteins]chemistry [Peptide Fragments]CD18 AntigensBiophysicschemistry [Cytoskeletal Proteins]Mutant Proteinsgenetics [Microfilament Proteins]Cell Adhesion MoleculesBiochemical Journal
researchProduct

Caspase-mediated apoptosis in sponges: cloning and function of the phylogenetic oldest apoptotic proteases from Metazoa

2003

AbstractSponges (phylum Porifera) represent the phylogenetically oldest metazoan phylum. These animals have complex cell adhesion and powerful immune systems which allow the formation of a distinct body plan. Consequently, an apoptotic machinery has to be predicted that allows sponges to eliminate unwanted cells accumulating during development. With the marine sponge Geodia cydonium, it is shown that allografts of these animals undergo apoptosis as demonstrated by apoptotic DNA fragmentation. Extracts from allografts contain an enzymic activity characteristic for caspases; as substrate to determine the cleavage activity, Ac-DEVD-AMC was applied. cDNAs encoding predicted caspase-3-related pr…

Molecular Sequence DataApoptosisCaspase 3SpongeCoumarinsEndopeptidasesAnimalsInvertebrateAmino Acid SequenceCloning MolecularEnzyme InhibitorsMolecular BiologyPhylogenyCaspasebiologyCaspase 3Cell adhesion moleculeAlternative splicingApoptotic DNA fragmentationPotential proapoptotic molecule DD2Cell BiologyBcl-2 homologous proteinbiology.organism_classificationSuberites domunculaCaspaseCaspase InhibitorsPoriferaCell biologyIsoenzymesSuberites domunculaSpongeApoptosisCaspasesbiology.proteinOligopeptidesSequence AlignmentBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
researchProduct

Novel Hydrazine Molecules as Tools To Understand the Flexibility of Vascular Adhesion Protein-1 Ligand-Binding Site: Toward More Selective Inhibitors

2011

Vascular adhesion protein-1 (VAP-1) belongs to a family of amine oxidases. It plays a role in leukocyte trafficking and in amine compound metabolism. VAP-1 is linked to various diseases, such as Alzheimer's disease, psoriasis, depression, diabetes, and obesity. Accordingly, selective inhibitors of VAP-1 could potentially be used to treat those diseases. In this study, eight novel VAP-1 hydrazine derivatives were synthesized and their VAP-1 and monoamine oxidase (MAO) inhibition ability was determined in vitro. MD simulations of VAP-1 with these new molecules reveal that the VAP-1 ligand-binding pocket is flexible and capable of fitting substantially larger ligands than was previously believ…

Monoamine Oxidase InhibitorsProtein ConformationMonoamine oxidaseCHO CellsMolecular Dynamics SimulationLigandsSubstrate SpecificityStructure-Activity RelationshipCricetulusCricetinaeDrug DiscoveryAnimalsHumansMoietyHydrazine (antidepressant)Monoamine OxidaseBinding SitesChemistryMethylationAdhesionbacterial infections and mycosesIn vitroRatsrespiratory tract diseasesHydrazinesBiochemistryMolecular MedicineAmine gas treatingAmine Oxidase (Copper-Containing)SelectivityCell Adhesion MoleculesJournal of Medicinal Chemistry
researchProduct

Antibodies to proteinase 3 mediate expression of vascular cell adhesion molecule-1 (VCAM-1).

1996

SUMMARY VCAM-1 was first identified as an adhesion molecule induced on human endothelial cells (HEC) by inflammatory cytokines such as IL-1, tumour necrosis factor (TNF), and lipopolysaccharide (LPS). The molecule binds to a variety of leucocytes, including B cells, T cells, basophils, eosinophils and monocytes. Vascular expression of VCAM-1 has been associated with a number of disease states, including rheumatoid arthritis and vasculitis. The detection of antineutrophil cytoplasmic antibodies (ANCA), especially to proteinase 3 (PR3), has become important in the diagnosis of Wegener’s granulomatosis (WG) and related vasculitides. Recently we were able to demonstrate a direct effect of anti-…

MyeloblastinT-LymphocytesImmunologyMolecular Sequence DataVascular Cell Adhesion Molecule-1BiologyAntibodiesProinflammatory cytokinechemistry.chemical_compoundAntigenProteinase 3Cell AdhesionImmunology and AllergyHumanscardiovascular diseasesRNA MessengerVCAM-1Cell adhesionCells CulturedBase SequenceCell adhesion moleculeSerine EndopeptidasesOriginal ArticleschemistryImmunologybiology.proteinTumor necrosis factor alphaEndothelium VascularAntibodyClinical and experimental immunology
researchProduct

Mir-661: A key Factor in Embryo-Maternal dialog With Potential Clinical Application to Predict Implantation Outcome?

2015

Implantation resulting in a full-term pregnancy is, by large, more than a passive process in which the developed conceptus is passively glued to the uterus through adhesive molecules. It is the result of a perfectly orchestrated dialog between a viable embryo and a receptive endometrium, through a mixture of paracrine and juxtacrine processes in which many key proteins and growth factors play fundamental roles (Pellicer et al., 2002.) Since their discovery, microRNAs have become prominent regulatory candidates, providing missing links for a few biological pathways in this process, although their exact role in human normal embryo formation and endometrial preparation for pregnancy remains un…

NectinsPopulationlcsh:MedicineContext (language use)Fertilization in VitroBiologyBioinformaticsEndometriumHistone DeacetylasesRNA TransportGeneral Biochemistry Genetics and Molecular BiologyCell LineTranscriptomeEndometriumParacrine signallingCell AdhesionmedicineHumansConceptusEmbryo ImplantationEukaryotic Initiation Factorseducationlcsh:R5-920education.field_of_studylcsh:REpithelial CellsEmbryoGeneral MedicineRepressor ProteinsMicroRNAsBlastocystmedicine.anatomical_structureArgonaute Proteinsembryonic structuresImmunologyCommentaryFemaleRNA Interferencelcsh:Medicine (General)Cell Adhesion MoleculesEmbryo qualityEBioMedicine
researchProduct

Roles of molecules involved in epithelial/mesenchymal transition during angiogenesis

2007

Formation of vessels requires "epithelial-mesenchymal" transition of endothelial cells, with several modifications at the level of endothelial cell plasma membranes. These processes are associated with redistribution of cell-cell and cell-substrate adhesion molecules, cross talk between external ECM and internal cytoskeleton through focal adhesion molecules and the expression of several proteolytic enzymes, including matrix metalloproteases and serine proteases. These enzymes with their degradative action on ECM components, generate molecules acting as activators and/or inhibitors of angiogenesis. The purpose of this review is to provide an overview of the molecules involved in epithelial-m…

Neovascularization PathologicbiologyAngiogenesisCell adhesion moleculeChemistryIntegrinProteolytic enzymesEpithelial CellsCadherinsModels BiologicalEpitheliumExtracellular MatrixCell biologyMesodermFocal adhesionTumor progressionCell Adhesionbiology.proteinAnimalsHumansEpithelial–mesenchymal transitionEnzyme InhibitorsCell adhesionCell Adhesion MoleculesFrontiers in Bioscience
researchProduct