Search results for "Moduli"

showing 10 items of 206 documents

β1D Integrin Inhibits Cell Cycle Progression in Normal Myoblasts and Fibroblasts

1998

Integrins are alphabeta heterodimeric transmembrane receptors involved in the regulation of cell growth and differentiation. The beta1 integrin subunit is widely expressed in vivo and is represented by four alternatively spliced cytoplasmic domain isoforms. beta1D is a muscle-specific variant of beta1 integrin and a predominant beta1 isoform in striated muscles. In the present study we showed that expression of the exogenous beta1D integrin in C2C12 myoblasts and NIH 3T3 or REF 52 fibroblasts inhibited cell proliferation. Unlike the case of the common beta1A isoform, adhesion of beta1D-transfected C2C12 myoblasts specifically via the expressed integrin did not activate mitogen-activated pro…

IntegrinsRecombinant Fusion ProteinsMolecular Sequence DataIntegrinSignal transductionTransfectionCell adhesion; Integrins; Signal transduction; Alternative splicing isoforms; Cell proliferation; MyodifferentiationBiochemistryCD49cCell LineCollagen receptorMiceAlternative splicing isoformsCell surface receptorAnimalsAmino Acid SequenceMuscle SkeletalMolecular BiologyCell proliferationMyodifferentiationbiologyCell growthIntegrin beta1Cell CycleCell adhesionCell DifferentiationReceptors Interleukin-2Cell BiologyImmunohistochemistryMolecular biologyCell biologyEnzyme ActivationProto-Oncogene Proteins c-rafAlternative SplicingGenes rasIntegrin alpha MCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinIntegrin beta 6C2C12Journal of Biological Chemistry
researchProduct

CLONING OF RAT-SPECIFIC LONG PCP4/PEP19 ISOFORM (LPI)

2007

We report the identification of a cDNA that encodes a putative protein of 94 amino acids and expected molecular weight of 10.7 kDa, the C-terminal half of which is identical to that of PEP19, a small, brain-specific protein involved in Ca++/calmodulin signaling. The novel rat-specific protein, tentatively named long PEP19 isoform (LPI), is the product of alternative splicing of the rat PCP4 gene encoding PEP19. We found that antibodies raised against the first 13 N-terminal amino acids of LPI, not present in PEP19, recognize a protein enriched in the developing rat brain.

LPI rat brain Ca++/calmodulin signaling
researchProduct

In regard to “A tale of two clones: Caldesmon staining in the differentiation of cutaneous spindle-cell neoplasms”

2018

LeiomyosarcomaPathologymedicine.medical_specialtyHistologyCellDermatologyH caldesmonPathology and Forensic Medicine030207 dermatology & venereal diseases03 medical and health sciences0302 clinical medicineSmooth musclemedicineHumansHistiocytoma Benign FibrousStaining and LabelingbiologyAtypical fibroxanthomaCell Differentiationmedicine.diseaseStainingCaldesmonmedicine.anatomical_structure030220 oncology & carcinogenesisbiology.proteinCalmodulin-Binding ProteinsJournal of Cutaneous Pathology
researchProduct

Neuroprotection elicited by P2Y13 receptors against genotoxic stress by inducing DUSP2 expression and MAPK signaling recovery.

2014

AbstractNucleotides activating P2Y13 receptors display neuroprotective actions against different apoptotic stimuli in cerebellar granule neurons. In the present study, P2Y13 neuroprotection was analyzed in conditions of genotoxic stress. Exposure to cisplatin and UV radiation induced caspase-3-dependent apoptotic cell death, and p38 MAPK signaling de-regulation. Pre-treatment with P2Y13 nucleotide agonist, 2methyl-thio-ADP (2MeSADP), restored granule neuron survival and prevented p38 long-lasting activation induced by cytotoxic treatments. Microarray gene expression analysis in 2MeSADP-stimulated cells revealed over-representation of genes related to protein phosphatase activity. Among them…

MAPK/ERK pathwayAgonistmedicine.drug_classMAP Kinase Signaling SystemUltraviolet Raysp38 mitogen-activated protein kinasesDUSPp38Genotoxic StressCREBNeuroprotectionMAPK protein phosphataseModels Biologicalp38 Mitogen-Activated Protein KinasesNucleotide receptorP2Y13 receptorCa2+/calmodulin-dependent protein kinaseCerebellummedicineAnimalsPhosphorylationRats WistarReceptorMolecular BiologyCell NucleusNeuronsbiologyCell DeathCaspase 3Receptors Purinergic P2Dual Specificity Phosphatase 2Cell BiologyThionucleotidesNeuroprotectionCell biologyRatsAdenosine DiphosphateEnzyme ActivationNeuroprotective AgentsCytoprotectionbiology.proteinCisplatinDNA DamageBiochimica et biophysica acta
researchProduct

Requirement of caveolae microdomains in extracellular signal-regulated kinase and focal adhesion kinase activation induced by endothelin-1 in primary…

1999

Endothelin-1 (ET-1) mitogenic activity in astrocytes is mediated by the activation of the extracellular signal-regulated kinase (ERK) pathway together with the Rho-dependent activation of the focal adhesion kinase (FAK) pathway. To clarify the mechanisms responsible for the coordinate activation of both pathways in the ET-1 signal propagation, the involvement of caveolae microdomains, suggested to play a role in signal transduction, was evaluated. In this study, it is reported that caveolae of primary astrocytes are enriched in endothelin receptor (ETB-R). Furthermore, signaling molecules such as the adaptor proteins Shc and Grb2, and the small G protein Rho, also reside within these microd…

MAPK/ERK pathwayCaveolin 1BiologyBiochemistryCaveolinsFocal adhesionCellular and Molecular Neurosciencechemistry.chemical_compoundCaveolaeCell AdhesionAnimalsFilipinPhosphorylationCells CulturedCytoskeletonMitogen-Activated Protein Kinase 1Endothelin-1Signal transducing adaptor proteinMembrane ProteinsTyrosine phosphorylationProtein-Tyrosine KinasesActinsCell biologyAnti-Bacterial AgentsCell CompartmentationRatsEnzyme ActivationchemistryAstrocytesFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesCaveolin 1Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinTyrosineGRB2Signal transductionExtracellular SpaceCell Adhesion MoleculesSignal TransductionJournal of neurochemistry
researchProduct

Induction of collagenase-3 (MMP-13) expression in human skin fibroblasts by three-dimensional collagen is mediated by p38 mitogen-activated protein k…

1999

Collagenase-3 (matrix metalloproteinase-13, MMP-13) is a recently identified human MMP with an exceptionally wide substrate specificity and restricted tissue-specific expression. Here we show that MMP-13 expression is induced in normal human skin fibroblasts cultured within three-dimensional collagen gel resulting in production and proteolytic activation of MMP-13. Induction of MMP-13 mRNAs by collagen gel was potently inhibited by blocking antibodies against alpha1 and alpha2 integrin subunits and augmented by activating antibody against beta1 integrin subunit, indicating that both alpha1 beta1 and alpha2 beta1 integrins mediate the MMP-13-inducing cellular signal generated by three-dimens…

MAPK/ERK pathwayIntegrinsReceptors CollagenSB 203580IntegrinDown-RegulationBiologyBiochemistryp38 Mitogen-Activated Protein KinasesCollagen receptorIntegrin alpha1beta1chemistry.chemical_compoundTransforming Growth Factor betaMatrix Metalloproteinase 13medicineHumansCollagenasesProtein kinase AMolecular BiologyDNA PrimersSkinBase SequenceKinaseTumor Necrosis Factor-alphaCell BiologyFibroblastsProtein-Tyrosine KinasesMolecular biologyEnzyme ActivationchemistryCalcium-Calmodulin-Dependent Protein KinasesCollagenasebiology.proteinCollagenMitogen-Activated Protein KinasesTyrosine kinasemedicine.drugInterleukin-1The Journal of biological chemistry
researchProduct

p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113.

1996

Abstract It is demonstrated here that p42 MAPKinase (p42 MAPK) phosphorylates the M yristoylated A lanine- R ich C - K inase S ubstrate (MARCKS) at Ser-113. In permeabilised Swiss 3T3 cells activation of protein kinase C (PKC) leads to p42 MAPK activation, but only the protein kinase C sites in MARCKS become phosphorylated and not Ser-113. The mitogen platelet-derived growth factor (PDGF) elicits the same response. These results demonstrate that while Ser-113 is a substrate for p42 MAPK in vitro and can be phosphorylated in vivo as shown by Taniguchi et al. [(1994) J. Biol. Chem. 269, 18299–18302], its phosphorylation is not subject to acute regulation by p42 MAPK in Swiss 3T3 cells.

MAPK/ERK pathwayMARCKSmedicine.medical_treatmentMitogen-activated protein kinase kinaseBiochemistryenvironment and public healthSubstrate SpecificityMiceStructural BiologySerinep42MAPKinasePhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateCells CulturedProtein Kinase CMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorbiologyChemistryIntracellular Signaling Peptides and Proteins3T3 CellsProtein-Tyrosine KinasesCell biologyBiochemistryMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatebiological phenomena cell phenomena and immunityPlatelet-derived growth factor receptorhormones hormone substitutes and hormone antagonistsendocrine systemRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsGeneticsmedicineAnimalsAmino Acid SequenceMARCKSMolecular BiologyProtein kinase CGrowth factorMembrane ProteinsProteinsCell BiologyPeptide FragmentsEnzyme ActivationMolecular Weightenzymes and coenzymes (carbohydrates)Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedMitogensFEBS letters
researchProduct

Dental stem cell signaling pathway activation in response to hydraulic calcium silicate-based endodontic cements: A systematic review of in vitro stu…

2020

Abstract Objective To present a qualitative synthesis of in vitro studies which analyzed human dental stem cell (DSC) molecular signaling pathway activation in response to hydraulic calcium silicate-based cements (HCSCs). Methods A systematic electronic search was performed in Medline, Scopus, Embase, Web of Science and SciELO databases on January 20 and last updated on March 20, 2020. In vitro studies assessing the implication of signaling pathways in activity related marker (gene/protein) expression and mineralization induced by HCSCs in contact with human DSCs were included. Results The search identified 277 preliminary results. After discarding duplicates, and screening of titles, abstr…

MAPK/ERK pathwayMaterials scienceCellDental CementsBiocompatible Materials02 engineering and technologySMADBiological FactorsDental Materials03 medical and health sciences0302 clinical medicineCa2+/calmodulin-dependent protein kinaseMedicine and Health SciencesmedicineHumansdental stem cellsGeneral Materials ScienceGeneral DentistryBiomedical and Dental MaterialsFOS: Clinical medicineSilicatesStem CellsIn vitro toxicologyWnt signaling pathwayEndodontics and Endodontologycalcium silicate-based cementsin vitroOxides030206 dentistryCalcium Compoundsbiomineralization021001 nanoscience & nanotechnologysignaling pathwaysChemicals and DrugsCell biologyDrug Combinationsmedicine.anatomical_structurebioactivityMechanics of MaterialsDentistryStem cellSignal transduction0210 nano-technologySignal TransductionDental Materials
researchProduct

Endogenous THBD (Thrombomodulin) Mediates Angiogenesis in the Ischemic Brain—Brief Report

2020

Objective: THBD (thrombomodulin) is part of the anticoagulant protein C-system that acts at the endothelium and is involved in anti-inflammatory and barrier-stabilizing processes. A recombinant soluble form of THBD was shown to have protective effects in different organs, but how the endogenous THBD is regulated during ischemia, particularly in the brain is not known to date. The aim of this study was to investigate the role of THBD, especially in brain endothelial cells, during ischemic stroke. Approach and Results: To induce ischemic brain damage, we occluded the middle cerebral artery of mice. We found an increased endothelial expression of Thbd in the peri-infarct area, whereas in the …

Male0301 basic medicineEndotheliumAngiogenesismedicine.drug_classThrombomodulinNeovascularization PhysiologicInflammationEndogeny030204 cardiovascular system & hematologyThrombomodulinlaw.invention03 medical and health sciences0302 clinical medicinelawAnimalsMedicineStrokeCells CulturedMice Knockoutbusiness.industryAnticoagulantBrainEndothelial CellsInfarction Middle Cerebral Arterymedicine.disease3. Good healthMice Inbred C57BLDisease Models Animal030104 developmental biologymedicine.anatomical_structureRecombinant DNACancer researchmedicine.symptomCardiology and Cardiovascular MedicinebusinessSignal TransductionArteriosclerosis, Thrombosis, and Vascular Biology
researchProduct

Plasticity-Related Gene 1 Affects Mouse Barrel Cortex Function via Strengthening of Glutamatergic Thalamocortical Transmission

2016

Plasticity-related gene-1 (PRG-1) is a brain-specific protein that modulates glutamatergic synaptic transmission. Here we investigated the functional role of PRG-1 in adolescent and adult mouse barrel cortex both in vitro and in vivo. Compared with wild-type (WT) animals, PRG-1-deficient (KO) mice showed specific behavioral deficits in tests assessing sensorimotor integration and whisker-based sensory discrimination as shown in the beam balance/walking test and sandpaper tactile discrimination test, respectively. At P25-31, spontaneous network activity in the barrel cortex in vivo was higher in KO mice compared with WT littermates, but not at P16-19. At P16-19, sensory evoked cortical respo…

Male0301 basic medicinePatch-Clamp TechniquesCognitive NeuroscienceThalamusGlutamic AcidNerve Tissue ProteinsStimulationSensory systemWalkingNeurotransmissionBiologySomatosensory systempatch-clamp recordingsSynaptic TransmissionTissue Culture Techniques03 medical and health sciencesCellular and Molecular NeuroscienceGlutamatergic0302 clinical medicineThalamusNeural PathwaysNeuroplasticityAnimalsPostural BalanceMice KnockoutNeuronsNeuronal Plasticitybehaviorin vitroArticlesSomatosensory CortexBarrel cortexnetwork activityin vivo030104 developmental biologyTouch PerceptionVibrissaeCalmodulin-Binding ProteinsFemaleNeuroscience030217 neurology & neurosurgeryCerebral Cortex
researchProduct