Search results for "Tripeptidyl peptidase I"

showing 4 items of 4 documents

TPP2 mutation associated with sterile brain inflammation mimicking MS

2018

ObjectiveTo ascertain the genetic cause of a consanguineous family from Syria suffering from a sterile brain inflammation mimicking a mild nonprogressive form of MS.MethodsWe used homozygosity mapping and next-generation sequencing to detect the disease-causing gene in the affected siblings. In addition, we performed RNA and protein expression studies, enzymatic activity assays, immunohistochemistry, and targeted sequencing of further MS cases from Austria, Germany, Canada and Jordan.ResultsIn this study, we describe the identification of a homozygous missense mutation (c.82T>G, p.Cys28Gly) in the tripeptidyl peptidase II (TPP2) gene in all 3 affected siblings of the family. Sequencing o…

0301 basic medicine41132medicine.disease_causeMajor histocompatibility complexArticle03 medical and health sciencesExon0302 clinical medicineGene expressionmedicineMissense mutationGeneGenetics (clinical)Medicinsk genetikMutationbiologyTripeptidyl peptidase IIDisease gene identificationMolecular biology3. Good health030104 developmental biologybiology.proteinNeurology (clinical)Medical Genetics030217 neurology & neurosurgeryNeurology Genetics
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Enzyme replacement therapy with recombinant pro-CTSD (cathepsin D) corrects defective proteolysis and autophagy in neuronal ceroid lipofuscinosis

2019

CTSD (cathepsin D) is one of the major lysosomal proteases indispensable for the maintenance of cellular proteostasis by turning over substrates of endocytosis, phagocytosis and autophagy. Consequently, CTSD deficiency leads to a strong impairment of the lysosomal-autophagy machinery. In mice and humans CTSD dysfunction underlies the congenital variant (CLN10) of neuronal ceroid lipofuscinosis (NCL). NCLs are distinct lysosomal storage disorders (LSDs) sharing various hallmarks, namely accumulation of protein aggregates and ceroid lipofuscin leading to neurodegeneration and blindness. The most established and clinically approved approach to treat LSDs is enzyme replacement therapy (ERT) aim…

0301 basic medicineproteolysisCathepsin DCathepsin DCathepsin BstorageCathepsin L03 medical and health sciencesSequestosome 1Neuronal Ceroid-LipofuscinosesAutophagymedicineAnimalsHumansEnzyme Replacement TherapyeducationMolecular BiologyMice Knockouttherapyeducation.field_of_studyTripeptidyl-Peptidase 1030102 biochemistry & molecular biologybiologyAutophagy; cathepsin D; enzyme replacement therapy; lysosome; neuronal ceroid lipofuscinosis; proteolysis; storage; therapyBrainCell BiologyFibroblastsTripeptidyl peptidase Imedicine.diseaseLRP1Cell biologyDisease Models Animal030104 developmental biologylysosomebiology.proteinAllograft inflammatory factor 1Neuronal ceroid lipofuscinosisneuronal ceroid lipofuscinosisLysosomesResearch PaperAutophagy
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Shotgun Proteomics of Isolated Urinary Extracellular Vesicles for Investigating Respiratory Impedance in Healthy Preschoolers

2021

Urine proteomic applications in children suggested their potential in discriminating between healthy subjects from those with respiratory diseases. The aim of the current study was to combine protein fractionation, by urinary extracellular vesicle isolation, and proteomics analysis in order to establish whether different patterns of respiratory impedance in healthy preschoolers can be characterized from a protein fingerprint. Twenty-one 3–5-yr-old healthy children, representative of 66 recruited subjects, were selected: 12 late preterm (LP) and 9 full-term (T) born. Children underwent measurement of respiratory impedance through Forced Oscillation Technique (FOT) and no significant differen…

MaleProteomePharmaceutical SciencePhysiologyUrineUrineProteomicsAminopeptidasesAnalytical Chemistry0302 clinical medicineDrug DiscoveryElectric ImpedanceMedicineRespiratory systemproteomic0303 health sciencesTripeptidyl-Peptidase 1urine fractionationExtracellular vesicleTripeptidyl peptidase IRespiratory Function Testsforced oscillation techniqueChemistry (miscellaneous)Child PreschoolMolecular MedicineFemaleUrinary systemReceptors Cell SurfaceArticlelcsh:QD241-441Extracellular Vesicles03 medical and health sciencesproteomicslcsh:Organic chemistryHumansNerve Growth FactorsPhysical and Theoretical ChemistryDipeptidyl-Peptidases and Tripeptidyl-PeptidasesEye ProteinsShotgun proteomicsAngiopoietin-Like Protein 2Serpins030304 developmental biologypreschooler healthy childrenbusiness.industryOrganic ChemistryCubilinAngiopoietin-like Proteins030228 respiratory systemThy-1 Antigensextracellular vesicleSerine Proteasesbusiness
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Late infantile neuronal ceroid lipofuscinosis: Quantitative description of the clinical course in patients withCLN2 mutations

2002

We examined 26 individuals with clinical and electron microscopic signs of late infantile neuronal ceroid lipofuscinosis (LINCL). In 22 cases, we found both pathogenic alleles. Sixteen patients exclusively carried either one or a combination of the two common mutations R208X and IVS5-1G > C. In the remaining cases, four missense mutations could be detected, of which R127Q, N286S, and T353P represent novel, previously not described alleles. A clinical performance score was developed by rating motor, visual, and verbal functions and the incidence of cerebral seizures in 3-month intervals during the course of the disease. A Total Disability Score was derived by summing up the single scores for…

Pediatricsmedicine.medical_specialtyDNA Mutational AnalysisCerliponase alfaDiseaseNeurological disorderAminopeptidasesSeverity of Illness IndexNeuronal Ceroid-LipofuscinosesSeizuresEndopeptidasesSeverity of illnessmedicineMissense mutationDipeptidyl-Peptidases and Tripeptidyl-PeptidasesVision OcularGenetics (clinical)Tripeptidyl-Peptidase 1business.industryDNAmedicine.diseaseTripeptidyl peptidase INeuronal Ceroid Lipofuscinosis Type 2MutationNeuronal ceroid lipofuscinosisSerine ProteasesbusinessPsychomotor PerformancePeptide HydrolasesAmerican Journal of Medical Genetics
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