Search results for "Galactosyltransferases"

showing 5 items of 5 documents

Evaluation of an amino acid residue critical for the specificity and activity of human Gb3/CD77 synthase

2016

Human Gb3/CD77 synthase (α1,4-galactosyltransferase) is the only known glycosyltransferase that changes acceptor specificity because of a point mutation. The enzyme, encoded by A4GALT locus, is responsible for biosynthesis of Gal(α1–4)Gal moiety in Gb3 (CD77, Pk antigen) and P1 glycosphingolipids. We showed before that a single nucleotide substitution c.631C > G in the open reading frame of A4GALT, resulting in replacement of glutamine with glutamic acid at position 211 (substitution p. Q211E), broadens the enzyme acceptor specificity, so it can not only attach galactose to another galactose but also to N-acetylgalactosamine. The latter reaction leads to synthesis of NOR antigens, which are…

0301 basic medicineAcetylgalactosamineMutation MissenseBiochemistryGlycosphingolipidsSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundGb3/CD77 synthaseBiosynthesisCell Line TumorGlycosyltransferaseAspartic acidHumansAsparagineSite-directed mutagenesisMolecular BiologySite-directed mutagenesisbiologyAntigens NuclearGlutamic acidCell BiologyGalactosyltransferasesMolecular biologyEnzyme assayGlutamineP1PK blood group system030104 developmental biologyAmino Acid SubstitutionBiochemistrychemistryGlycopshingolipidsbiology.proteinNOR polyagglutinationOriginal ArticleGlycoconjugate Journal
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Single nucleotide polymorphisms in A4GALT spur extra products of the human Gb3/CD77 synthase and underlie the P1PK blood group system.

2018

Contrary to the mainstream blood group systems, P1PK continues to puzzle and generate controversies over its molecular background. The P1PK system comprises three glycosphingolipid antigens: Pk, P1 and NOR, all synthesised by a glycosyltransferase called Gb3/CD77 synthase. The Pk antigen is present in most individuals, whereas P1 frequency is lesser and varies regionally, thus underlying two common phenotypes: P1, if the P1 antigen is present, and P2, when P1 is absent. Null and NOR phenotypes are extremely rare. To date, several single nucleotide polymorphisms (SNPs) have been proposed to predict the P1/P2 status, but it has not been clear how important they are in general and in relation …

0301 basic medicinePhysiologyCell Membraneslcsh:MedicineArtificial Gene Amplification and ExtensionBiochemistryPolymerase Chain Reactionchemistry.chemical_compoundSpectrum Analysis TechniquesTranscription (biology)GenotypeMedicine and Health Scienceslcsh:ScienceGeneticsMultidisciplinaryGlobosidesHomozygoteGlycosphingolipidFlow CytometryGalactosyltransferasesPhenotypeLipidsBody FluidsElectrophysiologyCholesterolBloodPhenotypeSpectrophotometryBlood Group AntigensCytophotometryAnatomyCellular Structures and OrganellesResearch ArticleGenotypeSingle-nucleotide polymorphismBiologyResearch and Analysis MethodsReal-Time Polymerase Chain ReactionMembrane PotentialPolymorphism Single NucleotideAntibodiesGlycosphingolipids03 medical and health sciencesAntigenGlycosyltransferaseHumansMolecular Biology TechniquesMolecular BiologyBlood typeSphingolipidslcsh:RBiology and Life SciencesCell Biology030104 developmental biologychemistrybiology.proteinlcsh:QBlood GroupsPLoS ONE
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Flow cytometric analysis of concanavalin A binding to isolated Golgi fractions from rat liver.

1993

Flow cytometry (FCM) has been used repeatedly to study lectin binding to whole cells. However, there are very few attempts to analyze glycoconjugates in isolated subcellular organelles. We have applied FCM to quantitate the specific binding of fluorescein-conjugated concanavalin A (FITC-Con A) to isolated cis and trans fractions of rat liver Golgi complex, the cell compartment involved in glycoprotein maturation and sorting. Our results show similar intensities of Con A-specific binding in the two fractions. Using this method we show a decreased FITC-Con A binding to both Golgi fractions in ethanol-treated rats, which is consistent to previous work on alcoholic effects on galactosyltransfer…

Alcohol DrinkingGlycoconjugateGolgi ApparatusCell FractionationFlow cytometrysymbols.namesakeOrganellemedicineConcanavalin AAnimalsRats Wistarchemistry.chemical_classificationGalactosyltransferaseBinding Sitesbiologymedicine.diagnostic_testLectinCell BiologyIntracellular MembranesGolgi apparatusFlow CytometryGalactosyltransferasesRatsDisease Models AnimalBiochemistrychemistryLiverConcanavalin Abiology.proteinsymbolsGlycoproteinFluorescein-5-isothiocyanateExperimental cell research
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The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability.

2008

Abstract Lysyl hydroxylase (LH) isoform 3 is a post-translational enzyme possessing LH, collagen galactosyltransferase (GT) and glucosyltransferase (GGT) activities. We have demonstrated that LH3 is found not only intracellularly, but also on the cell surface and in the extracellular space, suggesting additional functions for LH3. Here we show that the targeted disruption of LH3 by siRNA causes a marked reduction of both glycosyltransferase activities, and the overexpression of LH3 in HT-1080 cells increases hydroxylation of lysyl residues and the subsequent galactosylation and glucosylation of hydroxylysyl residues. These data confirm the multi-functionality of LH3 in cells. Furthermore, t…

DNA ComplementaryGlycosylationCell SurvivalLysyl hydroxylaseCellhydroxylysyl glycosylationFluorescent Antibody Techniquelysyl hydroxylaseMicrotubulesPermeabilityCell LineGlycosyltransferasemedicineExtracellularAnimalsHumanscell growthViability assayRNA Small InterferingCell Shapecell viabilityCell ProliferationbiologyCell DeathCell growthProcollagen-Lysine 2-Oxoglutarate 5-Dioxygenasecollagen biosynthesisGlycosyltransferasesCell BiologyArticlesGalactosyltransferasesMolecular biologyPeptide FragmentsCulture MediaActin Cytoskeletonmedicine.anatomical_structurepost-translational modificationCell culturebiology.proteinMolecular MedicineGlucosyltransferaseExtracellular Spacehydroxylysyl glycosyltransferaseJournal of cellular and molecular medicine
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Stimulation with carbachol alters endomembrane distribution and plasma membrane expression of intracellular proteins in lacrimal acinar cells.

2000

The events that lead to Sjogren's autoimmune processes in the lacrimal gland remain poorly understood. The acinar cell's responses to acute cholinergic stimulation include release of secretory products across the apical plasma membrane (apm) and a number of processes related to traffic between endomembrane compartments and the basal-lateral plasma membranes (blm), such as recruitment of Na, K-ATPase, accelerated recycling, and accelerated transcytosis of secretory IgA. We tested the hypothesis that stimulation-induced acceleration of endomembrane traffic is accompanied by changes in compartmentation and increased blm expression of proteins that are normally sequestered in endomembrane compa…

medicine.medical_specialtyAcid PhosphataseImmunoblottingGolgi ApparatusStimulationBiologyCholinergic AgonistsCathepsin BCathepsin BCellular and Molecular Neurosciencesymbols.namesakeInternal medicinemedicineAcinar cellAnimalsEndomembrane systemCells Culturedrab5 GTP-Binding ProteinsDifferential centrifugationEnzyme PrecursorsCell MembraneHistocompatibility Antigens Class IIMembrane Proteinsalpha-GlucosidasesGolgi apparatusGalactosyltransferasesCathepsinsSensory SystemsStimulation Chemicalbeta-N-AcetylhexosaminidasesCell biologyOphthalmologyEndocrinologySjogren's SyndromeTranscytosisrab GTP-Binding ProteinssymbolsCarbacholElectrophoresis Polyacrylamide GelFemaleRabbitsSodium-Potassium-Exchanging ATPaseIntracellularExperimental eye research
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