Search results for "Proprotein Convertases"

showing 8 items of 18 documents

Identification of Two Mannoproteins Released from Cell Walls of a Saccharomyces cerevisiae mnn1 mnn9 Double Mutant by Reducing Agents

1999

The cell wall of Saccharomyces cerevisiae represents some 30% of the total weight of the cell and is made up of β-glucans, mannose-containing glycoproteins (mannoproteins), and small amounts of chitin (9, 15). The mannoproteins can be divided into three groups according to the linkages that bind them to the structure of the cell wall: (i) noncovalently bound, (ii) covalently bound to the structural glucan, and (iii) disulfide bound to other proteins that are themselves covalently bound to the structural glucan of the cell wall (8). Our work has focused on the disulfide-bound mannoproteins, probably the least well known of the three groups mentioned above. Previous work (25) showed that trea…

GlycosylationSaccharomyces cerevisiae ProteinsGlycosylationBlotting WesternMolecular Sequence DataSaccharomyces cerevisiaeSaccharomyces cerevisiaeMicrobiologyGene Expression Regulation EnzymologicFungal ProteinsCell wallOpen Reading FramesSurface-Active Agentschemistry.chemical_compoundCell WallGene Expression Regulation FungalEndopeptidasesAspartic Acid EndopeptidasesAmino Acid SequenceSubtilisinsFluorescent Antibody Technique IndirectMolecular BiologyMercaptoethanolGlucanGel electrophoresischemistry.chemical_classificationFungal proteinMembrane GlycoproteinsbiologySodium Dodecyl SulfateBiological Transportbiology.organism_classificationRecombinant ProteinsYeastMolecular Weightcarbohydrates (lipids)Cytoskeletal ProteinsEukaryotic CellsPhenotypechemistryBiochemistryMutagenesisReducing AgentsElectrophoresis Polyacrylamide GelProprotein ConvertasesProtein Tyrosine PhosphatasesGlycoproteinGene DeletionJournal of Bacteriology
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Next-generation-sequencing-based identification of familial hypercholesterolemia-related mutations in subjects with increased LDL–C levels in a latvi…

2015

Background Familial hypercholesterolemia (FH) is one of the commonest monogenic disorders, predominantly inherited as an autosomal dominant trait. When untreated, it results in early coronary heart disease. The vast majority of FH remains undiagnosed in Latvia. The identification and early treatment of affected individuals remain a challenge worldwide. Most cases of FH are caused by mutations in one of four genes, APOB, LDLR, PCSK9, or LDLRAP1. The spectrum of disease-causing variants is very diverse and the variation detection panels usually used in its diagnosis cover only a minority of the disease-causing gene variants. However, DNA-based tests may provide an FH diagnosis for FH patients…

MaleNonsynonymous substitutionApolipoprotein BCoronary Artery DiseaseFamilial hypercholesterolemiaDiseaseCohort StudiesPCSK9Genetics(clinical)Family historyGenetics (clinical)Aged 80 and overGeneticseducation.field_of_studybiologySerine EndopeptidasesHigh-Throughput Nucleotide SequencingAutosomal dominant traitMiddle AgedLDLRAP1Apolipoprotein B-100Femalelipids (amino acids peptides and proteins)Proprotein ConvertasesProprotein Convertase 9APOBResearch ArticleAdultPopulationPolymorphism Single NucleotideLDLHyperlipoproteinemia Type IIYoung AdultGeneticsmedicineHumanseducationAdaptor Proteins Signal TransducingAgedDiagnostic toolsPCSK9Cholesterol LDLmedicine.diseaseLatviaGenetics PopulationLDLRReceptors LDLMutationNext-generation sequencingbiology.proteinBMC Medical Genetics
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The c.43_44insCTG variation in PCSK9 is associated with low plasma LDL-cholesterol in a Caucasian population.

2006

Abstract The genetic etiology of familial hypobetalipoproteinemia (FHBL) is unclear in the majority of cases. Mutations in apolipoprotein B (APOB) are the only confirmed causes of FHBL. Recently, loss-of-function mutations of PCSK9 gene have been shown to be associated with the hypocholesterolemia phenotype. Our primary goal was to confirm that mutations in PCSK9 could be another cause of FHBL. Using the sequencing approach, we found that the c.43_44insCTG variation in PCSK9, a common in-frame insertion in both African American and Caucasian populations, is associated with the hypocholesterolemia phenotype in three FHBL families. Then we tested whether this variation could be associated wit…

MaleSettore MED/09 - Medicina InternaApolipoprotein BDNA Mutational Analysismedicine.disease_causePCSK9Hypobetalipoproteinemiaschemistry.chemical_compoundGene Frequencyapolipoprotein BChildGenetics (clinical)Aged 80 and overMutationeducation.field_of_studybiologySerine EndopeptidasesMiddle AgedPedigreefamilial hypobetalipoproteinemiaPhenotypeChild Preschoollipids (amino acids peptides and proteins)FemaleProprotein ConvertasesProprotein Convertase 9Adultmedicine.medical_specialtyAdolescentPopulationMolecular Sequence DataWhite PeopleLDLlipidInternal medicineGeneticsmedicineHumanseducationAllele frequencyAgedhypocholesterolemiaCholesterolPCSK9Cholesterol HDLCholesterol LDLmedicine.diseaseHypocholesterolemiaEndocrinologychemistryMutationbiology.proteinLipoproteinHuman mutation
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Region specific expression of furin mRNA in the rat brain.

1993

The distribution of furin mRNA was examined in the rat central nervous system. Northern blot analysis reveals the presence of a 4.4 kb band in all brain tissues examined. In situ hybridization analysis of frozen rat brain sections using a radioactively labeled antisense cRNA probe to rat furin demonstrated moderate to low levels of expression in both neuronal and non-neuronal tissue in all areas examined. Interestingly, higher levels of furin were expressed in selective regions which include the ventricles (the choroid plexus and ependymal cells), the islands of Calleja, the hippocampus and the pineal gland. the ubiquitous localization of furin in the brain is consistent with its postulated…

Malemedicine.medical_specialtyanimal structuresvirusesProprotein convertase 2In situ hybridizationRats Sprague-DawleyInternal medicineGene expressionmedicineAnimalsTissue DistributionNorthern blotRNA MessengerSubtilisinsFurinIn Situ HybridizationFurinbiologyHistocytochemistryGeneral NeuroscienceSerine EndopeptidasesBrainCell biologyRatsEndocrinologymedicine.anatomical_structureProprotein Convertase 2embryonic structuresIslands of Callejabiology.proteinChoroid plexusProprotein ConvertasesEpendymaNeuroscience letters
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Additive effect of mutations in LDLR and PCSK9 genes on the phenotype of familial hypercholesterolemia.

2006

Patients homozygous or Compound heterozygous for LDLR mutations or double heterozygous for LDLR and apo B R3500Q mutation have higher LDL-C levels. more extensive xanthomatosis and more severe premature coronary disease (pCAD) than simple heterozygotes for mutations in either these genes or for missense mutations in PCSK9 gene. It is not known whether combined mutations in LDLR and PKCS9 are associated with such a severe phenotype. We sequenced Apo B and PCSK9 genes in two patients with the clinical diagnosis of homozygous FH who were heterozygous for LDLR gene mutations. Proband Z.P. (LDL-C 13.39 mmol/L and pCAD) was heterozygous for an LDLR mutation (p.E228K) inherited from her father (LD…

ProbandLDLR geneAdultMaleSettore MED/09 - Medicina InternaApolipoprotein BFamilial hypercholesterolemia (FH); Autosomal dominant hypercholesterolemia 3 (ADH3); LDLR gene; PCSK9 gene; Premature coronary artery diseasePremature coronary artery diseaseLDLR PCSK9Mutation MissenseFamilial hypercholesterolemiaCompound heterozygositymedicine.disease_causeHyperlipoproteinemia Type IIFamilial hypercholesterolemia (FH) Autosomal dominant hypercholesterolemia 3 (ADH3) LDLR gene PCSK9 gene Premature coronary artery diseaseFamilial hypercholesterolemia (FH)medicineMissense mutationHumansCells CulturedGeneticsMutationbiologybusiness.industrySerine EndopeptidasesHeterozygote advantageMiddle Agedmedicine.diseaseAutosomal dominant hypercholesterolemia 3 (ADH3)PedigreePhenotypeSettore MED/03 - Genetica MedicaAmino Acid SubstitutionReceptors LDLPCSK9 geneLDL receptorbiology.proteinlipids (amino acids peptides and proteins)FemaleProprotein ConvertasesProprotein Convertase 9Cardiology and Cardiovascular MedicinebusinessAtherosclerosis
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Sequence of the M28 dsRNA: Preprotoxin Is Processed to an α/β Heterodimeric Protein Toxin

1995

The killer and immunity phenotypes of K28 killer strains of Saccharomyces cerevisiae are determined by the 1.75-kb M28 dsRNA virus. In the plus strand, M28p, the K28 preprotoxin gene, comprises bases 13-1047 and is followed, after an additional 85 bases, by a 63-bp poly(A) sequence and a 553-base 3'-sequence. This 3'-sequence contains two potential stem-loop structures predicted to bind the L-A encoded cap-pol protein, initiating encapsidation; high-level expression results in curing of M1 dsRNA. Expression of M28p confers the complete K28 killer and immunity phenotype on a cell lacking M28 dsRNA. K28 toxin is a disulfide-bonded heterodimer of alpha (10.5 kDa) and beta (11 kDa) components w…

Signal peptideDNA ComplementaryGlycosylationSaccharomyces cerevisiae ProteinsGlycosylationMolecular Sequence DataMutantCarboxypeptidasesSaccharomyces cerevisiaeBiologymedicine.disease_causeCleavage (embryo)Fungal Proteinschemistry.chemical_compoundGene Expression Regulation FungalVirologyEndopeptidasesmedicineSecretionAmino Acid SequenceSubtilisinsGeneDNA PrimersRNA Double-StrandedBase SequenceToxinSerine EndopeptidasesMembrane ProteinsRNA FungalMycotoxinsMolecular biologyKiller Factors YeastRNA silencingchemistryProprotein ConvertasesProtein Processing Post-TranslationalVirology
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Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases.

2001

SPECIFIC AIMSTo identify the proprotein convertases responsible for maturation of the α-secretase ADAM10, we investigated the influence of PC7 and furin on ADAM10 processing and the resulting effect on amyloid precursor protein cleavage. We also examined the functional role of the ADAM10 prodomain by coexpression of a prodomain-deleted ADAM10 mutant together with its prodomain in trans.PRINCIPAL FINDINGS1. ADAM10 is proteolytically processed by PC7 and furinThe disintegrin metalloproteinase ADAM10 possesses α-secretase activity as well as a potential proprotein convertase recognition sequence (RKKR) after its prodomain. By amino-terminal sequencing of ADAM10 purified from bovine kidney plas…

animal structuresADAM10Blotting WesternKidneyTransfectionBiochemistryCell LineAmyloid beta-Protein PrecursorStructure-Activity RelationshipZymogenEndopeptidasesGeneticsAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansSubtilisinsProtein PrecursorsMolecular BiologyFurinFurinbiologyChemistryProprotein convertaseEmbryo MammalianRecombinant ProteinsEnzyme ActivationBiochemistryAlpha secretaseMutagenesisbiology.proteinCattleAmyloid Precursor Protein SecretasesProprotein ConvertasesAmyloid precursor protein secretaseBiotechnologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Immunohistochemical localization of the pro-peptide processing enzymes PC1/PC3 and PC2 in the human anal canal.

1997

Abstract HORsch, D., R. Day, N. G. Seidah, E. Weihe and M. K.-H. SchAFer. Immunohistochemical localization of the pro-peptide processing enzymes PC1/PC3 and PC2 in the human anal canal. Peptides 18(5) 755–760, 1997.—The distribution of prohormone/pro-peptide convertases PC1/PC3 and PC2 was investigated in the human anal canal by immunohistochemistry. Both prohormone convertases exhibited region-specific distribution patterns and were observed in neural and neuroendocrine cells and in nonneuroendocrine cellular elements. PC1/PC3 immunoreactivity was present in enteric neurons, subsets of nerve fibers, and neuroendocrine cells, and also in epithelial cells like intestinal stem cells, and a su…

endocrine systemPathologymedicine.medical_specialtyPhysiologyProhormoneNeuropeptideRectumAnal CanalBiologyBiochemistryImmunoenzyme TechniquesCellular and Molecular NeuroscienceEndocrinologymedicineChromograninsAspartic Acid EndopeptidasesHumansSubtilisinsAnal Transitional ZoneNeuronsNeuropeptidesAnal canalNeurosecretory SystemsEpitheliumNeoplasm Proteinsmedicine.anatomical_structureProprotein Convertase 2Fluorescent Antibody Technique DirectChromogranin AProprotein ConvertasesStem cellImmunostainingmedicine.drugPeptides
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