0000000000191440

AUTHOR

Nahuel A. Ramella

showing 2 related works from this author

Human apolipoprotein A-I natural variants: molecular mechanisms underlying amyloidogenic propensity

2012

Human apolipoprotein A-I (apoA-I)-derived amyloidosis can present with either wild-type (Wt) protein deposits in atherosclerotic plaques or as a hereditary form in which apoA-I variants deposit causing multiple organ failure. More than 15 single amino acid replacement amyloidogenic apoA-I variants have been described, but the molecular mechanisms involved in amyloid-associated pathology remain largely unknown. Here, we have investigated by fluorescence and biochemical approaches the stabilities and propensities to aggregate of two disease-associated apoA-I variants, apoA-IGly26Arg, associated with polyneuropathy and kidney dysfunction, and apoA-ILys107-0, implicated in amyloidosis in severe…

ProteomicsProtein Foldinglcsh:MedicineProtein aggregationpolymyxinsBiochemistryProtein Structure SecondaryMiceProtein structureneutrophilsMolecular Cell Biologypolycyclic compoundslcsh:ScienceCellular Stress ResponsesMultidisciplinaryProtein StabilityAmyloidosisCiencias QuímicasfluorescenseCell biologymacrophagesBiochemistryToxicityMedicineProtein foldinglipids (amino acids peptides and proteins)medicine.symptomPolyneuropathyResearch ArticleProtein StructureMedicinaLipoproteinsImmunologyBiophysicsInflammationAmyloidogenic ProteinsBiologyProtein ChemistryMicrobiologyCell Lineprotein aggregationmacrophage activationmedicineAnimalsHumansoligomersProtein InteractionsBiologyInflammationamyloidosisApolipoprotein A-IMacrophageslcsh:RImmunityProteinsnutritional and metabolic diseasesmedicine.diseaseApolipoproteinsAmino Acid SubstitutionCell cultureinflammationCiencias Médicaslcsh:QClinical ImmunologyMutant ProteinspolyneuropathyProtein Multimerization
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Human apolipoprotein A-I Gly26Arg stimulation of inflammatory responses via NF-kB activation: Potential roles in amyloidosis?

2018

The cascade of molecular events leading to Human apolipoprotein A–I (apoA–I) amyloidosis is not completely understood, not even the pathways that determine clinical manifestations associated to systemic protein deposition in organs such as liver, kidney and heart. About twenty natural variants of apoA–I were described as inducing amyloidosis, but the mechanisms driving their aggregation and deposition are still unclear. We previously identified that the mutant Gly26Arg but not Lys107-0 induced the release of cytokines and reactive oxygen species from cultured RAW 264.7 murine macrophages, suggesting that part of the pathogenic pathway could elicit of an inflammatory signal. In this work we …

0301 basic medicineLipopolysaccharideMACROPHAGES ACTIVATIONMutantStimulationInflammationOxidative phosphorylationPathology and Forensic MedicineCiencias Biológicas03 medical and health scienceschemistry.chemical_compoundINFLAMMATIONPhysiology (medical)APOLIPOPROTEIN A-I VARIANTSmedicineNUCLEAR FACTOR-ΚBchemistry.chemical_classificationReactive oxygen speciesAmyloidosisNF-κBBioquímica y Biología Molecularmedicine.diseaseCell biology030104 developmental biologychemistryAMYLOIDOSISlipids (amino acids peptides and proteins)medicine.symptomCIENCIAS NATURALES Y EXACTASPathophysiology
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