Search results for "Carrier Proteins"

showing 7 items of 347 documents

ATG16L1 contribution to Crohnʼs disease risk in Sicily

2011

medicine.medical_specialtyCrohn's diseaseSettore MED/09 - Medicina InternaPolymorphism Geneticbusiness.industryGastroenterologyAutophagy-Related Proteinsmedicine.diseaseGastroenterologyCrohn DiseaseRisk FactorsInternal medicinemedicineHumansImmunology and AllergyCarrier ProteinsbusinessCrohn's disease.genetics.ATG16L1SicilyATG16L1Inflammatory Bowel Diseases
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Identification of a novel mutation of MTP gene in a patient with abetalipoproteinemia.

2011

Abetalipoproteinemia (ABL), or Bassen-Kornzweig syndrome, is a rare autosomal recessive disorder of lipoprotein metabolism, characterized by fat malabsorption, hypocholesterolemia retinitis pigmentosa, progressive neuropathy and acanthocytosis from early infancy. We describe the clinical and molecular characterization of a 6-month-old infant born of consanguineous, apparently healthy parents from Iran. The patient was hospitalized because of failure to thrive, greasy stool and vomiting. The patient's serum lipid profile, the clinical phenotype and the duodenal histology suggested the clinical diagnosis of ABL. The MTP gene analysis by direct sequencing revealed a novel homozygous mutation (…

medicine.medical_specialtyHeterozygoteSettore MED/09 - Medicina InternaDuodenumSpecialties of internal medicineInternal medicineRetinitis pigmentosamedicineHumansgeneticsFamily HealthMTP gene mutations.ABLHepatologymedicine.diagnostic_testApoB-containing lipoproteins.business.industryAbetalipoproteinemiaInfantAbetalipoproteinemia.Heterozygote advantageGeneral Medicinemedicine.diseaseLipidsAbetalipoproteinemiaFat malabsorptionHypocholesterolemiaEndocrinologyPhenotypeRC581-951Failure to thriveFemaleHypocholesterolemia.medicine.symptomLipid profilebusinessCarrier Proteins
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Signaling through BMPR-IA regulates quiescence and long-term activity of neural stem cells in the adult hippocampus.

2010

SummaryNeural stem cells (NSCs) in the adult hippocampus divide infrequently, and the molecules that modulate their quiescence are largely unknown. Here, we show that bone morphogenetic protein (BMP) signaling is active in hippocampal NSCs, downstream of BMPR-IA. BMPs reversibly diminish proliferation of cultured NSCs while maintaining their undifferentiated state. In vivo, acute blockade of BMP signaling in the hippocampus by intracerebral infusion of Noggin first recruits quiescent NSCs into the cycle and increases neurogenesis; subsequently, it leads to decreased stem cell division and depletion of precursors and newborn neurons. Consistently, selective ablation of Bmpr1a in hippocampal …

medicine.medical_specialtyanimal structuresGenetic VectorsHippocampal formationBiologyBone morphogenetic proteinHippocampusModels BiologicalMOLNEUROCell LineMiceNeural Stem CellsInternal medicineGeneticsmedicineAnimalsHumansNogginBone Morphogenetic Protein Receptors Type ICells Culturedreproductive and urinary physiologySmad4 ProteinNeuronsReverse Transcriptase Polymerase Chain ReactionStem CellsCell CycleLentivirusNeurogenesisCentral-nervous-system; Bone morphogenetic protein; Dentate gyrus; Progenitor cells; Neurogenesis; Expression; Receptor; Noggin; Brain; DifferentiationCell BiologyFlow CytometrySTEMCELLRats Inbred F344BMPR1ANeural stem cellRatsCell biologyEndocrinologyStem cell divisionnervous systemembryonic structuresMolecular MedicineStem cellbiological phenomena cell phenomena and immunityCarrier ProteinsSignal Transduction
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Analysis of a soluble lipid-protein complex carrying endogenous 11-cis retinaldehyde from bovine retinal pigment epithelium.

1989

A soluble lipid-protein complex in bovine retinal pigment epithelium is shown to carry endogenous 11-cis retinaldehyde, in the extent of 15% of the total 11-cis retinaldehyde found in this tissue. The complex, analyzed with respect to its chemical composition, exhibits a lipid composition close resembling the lipid composition of the rod outer segment membrane; the SDS-PAGE evidences the presence of a number of protein bands, two of which of 34 and 27 kDa appear glycoproteins. Finally, the lipid-protein complex exhibits a discrete level of a Cathepsin D-like protease activity. From the above, the possibility is discussed that the soluble lipid-protein complex could represent some phagolysos…

medicine.medical_treatmentPhagocytosisLipoproteinsClinical BiochemistryEndogenyBiologyPigmentRetinoidsCytosolmedicineAnimalsPigment Epithelium of EyeMolecular BiologyPhospholipidsTriglycerideschemistry.chemical_classificationCathepsinProteaseRetinal pigment epitheliumCell BiologyGeneral MedicineMolecular Weightmedicine.anatomical_structureCholesterolchemistryBiochemistryvisual_artRetinaldehydevisual_art.visual_art_mediumChromatography GelRetinaldehydeCattleElectrophoresis Polyacrylamide GelGlycoproteinCarrier ProteinsMolecular and cellular biochemistry
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Osteoprotegerin (OPG) and RANKL expression and distribution in developing human craniomandibular joint.

2005

Abstract During embryogenesis the bone tissue of craniomandibular joint (CMJ) is formed through two pathways: intramembranous ossification and endochondral ossification. The development process is under the control of regulatory factors.The osteoprotegerin (OPG) and the receptor activator of nuclear factor (NF)-κB ligand are key regulators of osteoclastogenesis. The aim of this study is the localization of OPG and RANKL mRNA and protein in the foetal CMJ by immunohistochemistry (IHC) and in situ hybridization (ISH). The main results were: OPG and RANKL mRNA and protein were co-localized in the same cell types; OPG and RANKL were specially immunolocated in osteogenic cells; immunolabeling wa…

musculoskeletal diseasesCartilage Articularmedicine.medical_specialtyReceptors Cytoplasmic and NuclearIn situ hybridizationBiologyBone tissueReceptors Tumor Necrosis FactorBone remodelingOsteoprotegerinOsteogenesisInternal medicineBone cellmedicineHumansRNA MessengerEndochondral ossificationIn Situ HybridizationGlycoproteinsMembrane GlycoproteinsReceptor Activator of Nuclear Factor-kappa BTemporomandibular JointRANK LigandOsteoprotegerinCell BiologyGeneral MedicineImmunohistochemistryCell biologyEndocrinologymedicine.anatomical_structureRANKLIntramembranous ossificationbiology.proteinCarrier ProteinsDevelopmental BiologyTissuecell
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Maturation of Epidermal Langerhans Cells In Vitro Is Accompanied by Downregulation of 4F2 (CD98) as Determined by Differential Display

1998

Following short-term culture, Langerhans cells mature morphologically and functionally into potent immunostimulatory cells. As regulation of gene expression accompanies this maturation process, it is likely that differentially expressed genes are involved in the maturation events. Using the recently described method of differential display, we generated cDNA expression patterns starting with mRNA of murine epidermal Langerhans cells isolated either directly (fLC) or following 3 d cultivation (cLC). Five hundred putative differentially expressed cDNA fragments were recovered from the gel. For a part of the fragments differential expression was confirmed by dot blot and Southern hybridization…

skinLangerhans cellDNA ComplementaryDown-RegulationFusion Regulatory Protein-1GrowthDermatologyBiologyBiochemistryMiceDownregulation and upregulationAntigens CDComplementary DNAmedicineAnimalsRNA MessengerCloning Moleculardifferential gene expressionGeneMolecular BiologySouthern blotRegulation of gene expressionJNK2Differential displayMice Inbred BALB Cepidermal cellsGene Expression Regulation DevelopmentalCell BiologyMolecular biologyMice Inbred C57BLmedicine.anatomical_structureGenesCell cultureLangerhans CellsAntigens SurfaceCarrier ProteinsSequence AnalysisJournal of Investigative Dermatology
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Nuclear localization but not PML protein is required for incorporation of the papillomavirus minor capsid protein L2 into virus-like particles.

2004

ABSTRACT Recent reports suggest that nuclear domain(s) 10 (ND10) is the site of papillomavirus morphogenesis. The viral genome replicates in or close to ND10. In addition, the minor capsid protein, L2, accumulates in these subnuclear structures and recruits the major capsid protein, L1. We have now used cell lines deficient for promyelocytic leukemia (PML) protein, the main structural component of ND10, to study the role of this nuclear protein for L2 incorporation into virus-like particles (VLPs). L2 expressed in PML protein knockout (PML −/− ) cells accumulated in nuclear dots, which resemble L2 aggregates forming at ND10 in PML protein-containing cells. These L2 assemblies also attracted…

virusesImmunologyActive Transport Cell NucleusNuclear dotsBiologyPromyelocytic Leukemia ProteinMicrobiologyCell LinePromyelocytic leukemia proteinMiceDeath-associated protein 6Virus-like particleVirologymedicineAnimalsHumansNuclear proteinPapillomaviridaeAdaptor Proteins Signal TransducingCell NucleusTumor Suppressor ProteinsStructure and AssemblyIntracellular Signaling Peptides and ProteinsVirionvirus diseasesNuclear ProteinsOncogene Proteins Viralbiochemical phenomena metabolism and nutritionMolecular biologyCell biologyNeoplasm ProteinsCell nucleusMicroscopy Electronmedicine.anatomical_structureInsect ScienceMutationbiology.proteinCapsid ProteinsNuclear transportCarrier ProteinsCo-Repressor ProteinsNuclear localization sequenceMolecular ChaperonesTranscription FactorsJournal of virology
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