Search results for "Sterol Esterase"

showing 10 items of 14 documents

Lysosomal acid lipase deficiency: Expanding differential diagnosis.

2016

The differential diagnoses for metabolic liver diseases may be challenging in clinical settings, which represents a critical issue for disorders such as lysosomal acid lipase deficiency (LAL-D). LAL-D is caused by deficient activity of the LAL enzyme, resulting in the accumulation of cholesteryl esters and triglycerides throughout the body, predominately in the liver, spleen, gastrointestinal tract, and blood vessel walls. LAL-D is a progressive, multi-organ disease with early mortality and significant morbidity characterized by a combination of hepatic dysfunction and dyslipidemia. Evidence suggests LAL-D may be substantially underdiagnosed or misdiagnosed, which is critical given that dis…

0301 basic medicineMalemedicine.medical_specialtyPathologyAdolescentEndocrinology Diabetes and MetabolismDiseaseLysosomal acid lipase deficiencyBiochemistryGastroenterologyDiagnosis Differential03 medical and health sciences0302 clinical medicineEndocrinologyInternal medicineGeneticsmedicineLysosomal storage diseaseHumansChildMolecular BiologyTriglyceridesNiemann-Pick DiseasesGaucher Diseasebusiness.industryWolman DiseaseInfantEnzyme replacement therapySterol Esterasemedicine.diseaseClinical trial030104 developmental biologyEarly DiagnosisSebelipase alfaDisease Progression030211 gastroenterology & hepatologyFemaleCholesterol EstersDifferential diagnosisbusinessDyslipidemiaMolecular genetics and metabolism
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Large-scale screening of lipase acid deficiency in at risk population

2021

International audience; BACKGROUND: Lysosomal acid lipase deficiency (LALD, OMIM#278000) is a rare lysosomal disorder with an autosomal recessive inheritance. The main clinical manifestations are related to a progressive accumulation of cholesteryl esters, triglycerides or both within the lysosome in different organs such as the liver, spleen, and cardiovascular system. A wide range of clinical severity is associated with LALD including a severe very rare antenatal/neonatal/infantile phenotype named Wolman disease and a late-onset form named cholesteryl ester storage disease (CESD). METHODS: This study aimed to investigate a cohort of at-risk patients (4174) presenting with clinical or biol…

0301 basic medicinemedicine.medical_specialty[SDV]Life Sciences [q-bio]Clinical BiochemistryAcid lipase deficiencyDBSSpleenDried blood spotLysosomal acid lipase deficiencyBiochemistryGastroenterologyCESDCholesterol ester storage disease03 medical and health sciences0302 clinical medicinePregnancyLysosomeInternal medicinemedicineHumansAllelebusiness.industryBiochemistry (medical)Infant NewbornWolman DiseaseLipaseGeneral MedicineCholesterol ester storage diseaseLALSterol Esterasemedicine.diseasePhenotype3. Good healthDried blood spot[SDV] Life Sciences [q-bio]030104 developmental biologymedicine.anatomical_structureWolman030220 oncology & carcinogenesisCohortScreeningFemaleCholesterol Estersbusiness
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Enzymatic modification of low-density lipoprotein in the arterial wall: a new role for plasmin and matrix metalloproteinases in atherogenesis.

2004

Objective— Functionally interactive proteases of the plasminogen/plasmin and the matrix metalloproteinase (MMP) system degrade and reorganize the extracellular matrix of the vessel wall in atherosclerosis. Here we investigated whether such proteases are able to confer atherogenic properties onto low density lipoprotein by nonoxidative modification. Methods and Results— Similar to the recently described enzymatically-modified low-density lipoprotein (E-LDL), native LDL exposed to plasmin or matrix MMP-2 or MMP-9 and cholesterylester-hydrolase (CEH) showed extensive deesterification, with ratios of free cholesterol to total cholesterol rising to 0.8 compared with 0.2 in native LDL. When the …

AdultLipoprotein modificationProteasesAdolescentPlasminArteriosclerosisBlotting WesternMatrix metalloproteinaseComplement Hemolytic Activity AssayMonocyteschemistry.chemical_compoundmedicineHumansTrypsinFibrinolysinComplement ActivationCells CulturedAgedbiologyMacrophagesAntibodies MonoclonalSodium Dodecyl SulfateLipoprotein(a)Middle AgedSterol EsteraseCell biologyLipoproteins LDLC-Reactive ProteinchemistryBiochemistryMatrix Metalloproteinase 9Low-density lipoproteinbiology.proteinMatrix Metalloproteinase 2lipids (amino acids peptides and proteins)Electrophoresis Polyacrylamide GelCardiology and Cardiovascular MedicinePlasminogen activatormedicine.drugLipoproteinArteriosclerosis, thrombosis, and vascular biology
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A Phase 3 Trial of Sebelipase Alfa in Lysosomal Acid Lipase Deficiency

2015

BackgroundLysosomal acid lipase is an essential lipid-metabolizing enzyme that breaks down endocytosed lipid particles and regulates lipid metabolism. We conducted a phase 3 trial of enzyme-replacement therapy in children and adults with lysosomal acid lipase deficiency, an underappreciated cause of cirrhosis and severe dyslipidemia. MethodsIn this multicenter, randomized, double-blind, placebo-controlled study involving 66 patients, we evaluated the safety and effectiveness of enzyme-replacement therapy with sebelipase alfa (administered intravenously at a dose of 1 mg per kilogram of body weight every other week); the placebo-controlled phase of the study was 20 weeks long and was followe…

AdultMalemedicine.medical_specialtyCirrhosisAdolescentHDLBiopsy[SDV]Life Sciences [q-bio]Lysosomal acid lipase deficiencyGastroenterologyLDLlaw.inventionYoung Adultchemistry.chemical_compoundDouble-Blind MethodRandomized controlled triallawInternal medicinemedicineHumansAdolescent; Adult; Aged; Alanine Transaminase; Biopsy; Child; Child Preschool; Cholesterol HDL; Cholesterol LDL; Double-Blind Method; Dyslipidemias; Female; Humans; Liver; Male; Middle Aged; Sterol Esterase; Wolman Disease; Young AdultChildPreschoolComputingMilieux_MISCELLANEOUSAgedDyslipidemiasbiologyCholesterolbusiness.industryWolman DiseaseAlanine TransaminaseLipid metabolismGeneral MedicineMiddle AgedSterol Esterasemedicine.disease3. Good healthCholesterolEndocrinologyLiverSebelipase alfachemistryAlanine transaminasebiology.proteinFemalebusinessDyslipidemia
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Atherogenic properties of enzymatically degraded LDL: selective induction of MCP-1 and cytotoxic effects on human macrophages.

1998

Abstract —The mechanisms underlying the selective accumulation of macrophages in early atherosclerotic lesions are poorly understood but are likely to be related to specific properties of altered low density lipoprotein (LDL) deposited in the subendothelium. Enzymatic, nonoxidative degradation of LDL converts the lipoprotein to a potentially atherogenic moiety, enzymatically altered LDL (E-LDL), which activates complement and is rapidly taken up by human macrophages via a scavenger receptor–dependent pathway. Immunohistological evidence indicates that E-LDL is present in an extracellular location in the early lesion. We report that E-LDL causes massive release of monocyte chemotactic prote…

ArteriosclerosisHydrolasesGene ExpressionNeuraminidaseBiologyCCL2Polymerase Chain Reactionchemistry.chemical_compoundExtracellularmedicineMacrophageHumansTrypsinInterleukin 8RNA MessengerCells CulturedChemokine CCL2Cell DeathMonocyteMacrophagesRNA-Directed DNA PolymeraseSterol EsteraseMolecular biologyLipoproteins LDLKineticsmedicine.anatomical_structureBiochemistrychemistryApoptosisLow-density lipoproteinlipids (amino acids peptides and proteins)Cardiology and Cardiovascular MedicineLipoproteinArteriosclerosis, thrombosis, and vascular biology
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Hypersusceptibility of neutrophil granulocytes towards lethal action of free fatty acids contained in enzyme-modified atherogenic low density lipopro…

2008

Abstract Objective The bulk of LDL entrapped in the arterial intima is modified by hydrolytic enzymes, leading to extensive cleavage of cholesterylesters and liberation of fatty acids. The latter induce apoptosis in endothelial cells but are far less cytotoxic towards macrophages. We have compared the cytotoxic effects of enzymatically modified LDL (E-LDL) on macrophages and polymorphonuclear granulocytes (PMN). Methods and results E-LDL displayed toxicity towards PMN at far lower concentrations than towards monocyte-derived macrophages. Native or oxidized LDL had no effect. Free fatty acids contained in E-LDL were the cause of the observed toxicity, which could be mimicked by linoleic acid…

Cell Membrane PermeabilityTime FactorsCell SurvivalNeutrophilsLinoleic acidGranulocyteFatty Acids NonesterifiedHemolysisLinoleic Acidchemistry.chemical_compoundAdenosine TriphosphateSuperoxidesmedicineAnimalsHumansPropidium iodideCells CulturedPeroxidaseRespiratory BurstArachidonic AcidCell DeathL-Lactate DehydrogenaseSuperoxideHydrolysisMacrophagesSterol EsteraseAtherosclerosisRespiratory burstLipoproteins LDLOleic acidmedicine.anatomical_structurechemistryBiochemistryLow-density lipoproteinlipids (amino acids peptides and proteins)Arachidonic acidCalciumRabbitsCardiology and Cardiovascular MedicineOleic AcidPeptide HydrolasesAtherosclerosis
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Severe reduction of blood lysosomal acid lipase activity in cryptogenic cirrhosis: A nationwide multicentre cohort study

2017

Background and aims Blood lysosomal acid lipase (LAL) is reduced in non-alcoholic steatohepatitis, which is the major cause of cryptogenic cirrhosis (CC); few data on LAL activity in CC do exist. We investigated LAL activity in a cohort of patients with liver cirrhosis. Methods This is a multicentre cohort study including 274 patients with liver cirrhosis of different aetiology from 19 centres of Internal Medicine, Gastroenterology and Hepatology distributed throughout Italy. Blood LAL activity (nmol/spot/h) was measured with dried blood spot extracts using Lalistat 2. Results Overall, 133 patients had CC, and 141 patients had cirrhosis by other causes (61 viral, 53 alcoholic, 20 alcoholic …

Liver CirrhosisMaleCryptogenic cirrhosis; Liver disease; Lysosomal acid lipase; PathogenesisCirrhosisCryptogenic cirrhosisCryptogenic cirrhosis; Liver disease; Lysosomal acid lipase; Pathogenesis; Cardiology and Cardiovascular MedicineComorbidityPathogenesisLysosonal acid lipase; non-alcoolic fatty liver disease; cirrhosis030204 cardiovascular system & hematologyGastroenterologyLiver disease0302 clinical medicineModel for End-Stage Liver DiseasePathogenesiRisk FactorsPrevalenceProspective cohort studyMultivariate AnalysiSettore MED/12 - GastroenterologiaMiddle AgedItalyCohortLinear Model030211 gastroenterology & hepatologyFemaleCardiology and Cardiovascular MedicineLiver diseaseHumanmedicine.medical_specialtyLiver CirrhosiDown-Regulation03 medical and health sciencesInternal medicineCryptogenic cirrhosis; Liver disease; Lysosomal acid lipase; Pathogenesis; Aged; Biomarkers; Chi-Square Distribution; Comorbidity; Cross-Sectional Studies; Down-Regulation; Dried Blood Spot Testing; Female; Humans; Italy; Linear Models; Liver Cirrhosis; Male; Middle Aged; Multivariate Analysis; Platelet Count; Prevalence; Risk Factors; Sterol EsterasemedicineLysosonal acid lipaseHumansnon-alcoolic fatty liver diseaseAgedCross-Sectional StudieChi-Square Distributionbusiness.industryPlatelet CountcirrhosisRisk FactorBiomarkerCholesterol ester storage diseaseHepatologySterol Esterasemedicine.diseaseCross-Sectional StudiesMultivariate AnalysisLysosomal acid lipaseLinear ModelsDried Blood Spot TestingSteatohepatitisbusinessCryptogenic cirrhosiBiomarkers
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Comparative changes between pancreas and pancreatic juice digestive enzyme contents during nutritional rehabilitation following severe protein malnut…

1993

The relationship between digestive enzyme activities in the pancreas and pancreatic juice was studied in post-weaning rats fed on a low-protein diet (30 g cereal protein/kg) for 1 month and a refeeding balanced diet (235 g mixed protein/kg) for the following 3 months. A control group was fed on the balanced diet for 4 months. At the end of malnutrition and at various times of refeeding, activities of amylase (EC3.2.1.1), trypsin(EC3.4.21.4), chymotrypsin (EC3.4.21.1), lipase (EC3.1.1.3), phospholipase A2 (EC3.1.1.4) and cholesterolesterase (EC3.1.1.13) in pancreas and pancreatic juice were measured. Recovery of body and pancreas weights was obtained after 3 months of refeeding. Pancreas off…

Malemedicine.medical_specialtyTime FactorsProtein–energy malnutritionDiet therapyMedicine (miscellaneous)Protein-Energy MalnutritionPhospholipases APancreatic JuiceInternal medicinemedicineAnimalsChymotrypsinTrypsinAmylaseRats WistarPancreasNutrition and DieteticsChymotrypsinbiologyLipaseSterol Esterasemedicine.diseaseTrypsinRatsPhospholipases A2Endocrinologymedicine.anatomical_structureAmylasesPancreatic juiceDigestive enzymebiology.proteinRNAPancreasmedicine.drugBritish Journal of Nutrition
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Possible protective role for C-reactive protein in atherogenesis: complement activation by modified lipoproteins halts before detrimental terminal se…

2004

Background—Previous work indicated that enzymatically remodeled LDL (E-LDL) might activate complement in atherosclerotic lesions via a C-reactive protein (CRP)–dependent and CRP-independent pathway. We sought to substantiate this contention and determine whether both pathways drive the sequence to completion.Methods and Results—E-LDL was prepared by sequential treatment of LDL with a protease and cholesteryl esterase. Trypsin, proteinase K, cathepsin H, or plasmin was used with similar results. Functional tests were used to assess total complement hemolytic activity, and immunoassays were used to demonstrate C3 cleavage and to quantify C3a, C4a, C5a, and C5b-9. E-LDL preparations activated …

PlasminArteriosclerosisLipoproteinsCathepsin HPhysiology (medical)EndopeptidasesmedicineHumansComplement ActivationbiologyC-reactive proteinC4ADrug SynergismComplement System ProteinsSterol EsteraseProteinase KTrypsinImmunohistochemistryComplement systemLipoproteins LDLC-Reactive ProteinBiochemistrybiology.proteinCardiology and Cardiovascular MedicineLipoproteinmedicine.drugCirculation
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Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis.

2003

Objective—Modification with proteases and cholesterylesterase transforms LDL to a moiety that resembles lipoproteins isolated from atherosclerotic lesions and possesses atherogenic properties. To identify changes in monocyte-derived foam cells laden with enzymatically modified LDL (E-LDL), we compared patterns of the most abundant transcripts in these cells after incubation with LDL or E-LDL.Methods and Results—Serial analyses of gene expression (SAGE) libraries were constructed from human monocytes after treatment with LDL or E-LDL. Several tags were differentially expressed in LDL-treated versus E-LDL–treated cells, whereby marked selective induction by E-LDL of cathepsin H was conspicuou…

ProteasesCathepsin HCoronary Artery DiseaseBiologyCathepsin HCathepsin L1medicineMacrophageHumansFoam cellGene LibraryCathepsinMonocyteGene Expression ProfilingColocalizationSterol EsteraseMolecular biologyCathepsinsLipoproteins LDLCysteine Endopeptidasesmedicine.anatomical_structureCholesterolBiochemistryGene Expression Regulationlipids (amino acids peptides and proteins)Cardiology and Cardiovascular MedicineFoam CellsArteriosclerosis, thrombosis, and vascular biology
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