Search results for "Prealbumin"

showing 8 items of 8 documents

Therapy of ATTR Cardiac Amyloidosis: Current Indications

2023

Transthyretin cardiac amyloidosis is a restrictive cardiomyopathy caused by extracellular deposition in the heart of amyloid fibrils derived from plasma transthyretin (ATTR), either in its hereditary (ATTRh) or acquired (ATTRwt) forms. Cardiac amyloidosis has a very poor prognosis if therapy is not started promptly. Therefore, it is very important to recognize cardiac amyloidosis early in order to immediately start a treatment capable of modifying the prognosis. Treatment of cardiac amyloidosis is not easy, often requiring a multidisciplinary team. New RNA-interfering drugs (such as patisiran) have been devised and are effective in the treatment of ATTRh amyloidosis. Tafamidis (a stabilizer…

Amyloid Neuropathies FamilialAmyloidHumansPrealbuminTransthyretin cardiac amyloidosisGeneral MedicineCardiomyopathiesCardiology and Cardiovascular MedicineCurrent Problems in Cardiology
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Treatment with essential amino acids in patients on chronic hemodialysis: a double blind cross-over study.

1978

Patients on chronic hemodialysis may suffer from a latent protein deficiency, and therapy with essential amino acids has been recommended. In a double blind cross-over study, 13 hemodialysis patients received orally 15.7 g of essential amino acids daily over a 3-month period. Patients were on a liberal diet, containing 1 g of protein per kilogram of body weight per day. Hemodialysis was adequate. Therapy resulted in an increase in urea, uric acid, C3 c complement factor and a fall in C4. Lysine levels increased and phenylalanine fell. Malnutrition could not account for the observed metabolic changes, which are more likely due to uremic metabolic disturbances. A liberal diet of 1 g of protei…

AdultMalemedicine.medical_specialtymedicine.medical_treatmentMedicine (miscellaneous)PhenylalanineComplement factor Ichemistry.chemical_compoundGlomerulonephritisRenal DialysisInternal medicineProtein DeficiencyMedicineHumansPrealbuminchemistry.chemical_classificationClinical Trials as TopicNutrition and DieteticsPyelonephritisbusiness.industryTransferrinComplement C3Middle Agedmedicine.diseaseCrossover studyAmino acidRetinol-Binding ProteinsMalnutritionEndocrinologychemistryBiochemistryUreaUric acidFemaleHemodialysisAmino Acids EssentialbusinessThe American journal of clinical nutrition
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Familial Amyloid Polyneuropathy

2013

Familial amyloid polyneuropathy (FAP; also known as familiar amyloidosis and hereditary amyloidosis) is an autosomal dominant inherited disease due to mutations of the transthyretin (TTR) gene coding for the corresponding protein, consisting of 127 amino acids. The gene is located on chromosome 18q. More than 100 different mutations are known. Other mutant precursor proteins produced in the liver, such as apolipoprotein I and II, lysozyme and fibrinogen Aα, may be of etiological importance as well. Amyloidogenic mutations of the TTR gene lead to decreased stability of the corresponding protein and subsequently to extracellular deposition of amyloid in several tissues (peripheral and autonom…

Amyloid Neuropathies Familialmedicine.medical_specialtyAmyloidbiologyApolipoprotein Bbusiness.industrymedicine.medical_treatmentAmyloidosisGastroenterologyGeneral MedicineDiseaseLiver transplantationmedicine.diseaseGastroenterologyLiver TransplantationTransthyretinAmyloid NeuropathyInternal medicinePrevalencebiology.proteinmedicineHumansPrealbuminbusinessPolyneuropathyDigestive Diseases
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Follow-up in transthyretin familial amyloid polyneuropathy: Useful investigations

2020

Patients with transthyretin amyloid polyneuropathy (TTR-FAP) and asymptomatic mutation-carriers have to be regularly followed-up in order to identify disease progression and the time point for starting or modifying therapy. In this case series we describe the potential suitability of different variables as progression markers. We retrospectively analyzed the follow-up charts of 10 TTR-FAP patients. Clinical examination included the Neuropathy Impairment Score of Lower Limb (NIS-LL), temperature perception thresholds, nerve conduction and autonomic function tests. The NIS-LL had the greatest value for a sensitive and correct follow-up for all TTR-FAP stages. All other examinations provided u…

congenital hereditary and neonatal diseases and abnormalitiesendocrine systemmedicine.medical_specialtyNeural ConductionPhysical examinationAsymptomatic03 medical and health sciences0302 clinical medicineClinical investigationInternal medicinemedicineHumansPrealbumin030212 general & internal medicineRetrospective StudiesAmyloid Neuropathies Familialbiologymedicine.diagnostic_testbusiness.industryAmyloidosisDisease progressionnutritional and metabolic diseasesmedicine.diseasedigestive system diseasesTransthyretinNeurologybiology.proteinAmyloid polyneuropathyNeurology (clinical)medicine.symptombusinessPolyneuropathy030217 neurology & neurosurgeryFollow-Up StudiesJournal of the Neurological Sciences
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Maternal Inheritance of a Recessive RBP4 Defect in Canine Congenital Eye Disease

2018

SUMMARY Maternally skewed transmission of traits has been associated with genomic imprinting and oocyte-derived mRNA. We report canine congenital eye malformations, caused by an amino acid deletion (K12del) near the N terminus of retinol-binding protein (RBP4). The disease is only expressed when both dam and offspring are deletion homozygotes. RBP carries vitamin A (retinol) from hepatic stores to peripheral tissues, including the placenta and developing eye, where it is required to synthesize retinoic acid. Gestational vitamin A deficiency is a known risk factor for ocular birth defects. The K12del mutation disrupts RBP folding in vivo, decreasing its secretion from hepatocytes to serum. T…

0301 basic medicineMaleNon-Mendelian inheritanceProtein Foldingcongenital eye defectEye Diseasesgenetic structuresNATIVE DISULFIDE BONDSMedical PhysiologyRetinoic acidReproductive health and childbirth413 Veterinary scienceMicrophthalmiavitamin Achemistry.chemical_compoundPlasmaA-vitamiini2.1 Biological and endogenous factorsMicrophthalmosPrealbuminCRYSTAL-STRUCTUREAetiologyBase Pairinglcsh:QH301-705.5Sequence DeletionPediatricwhole genome sequencingVITAMIN-A-DEFICIENCYANOPHTHALMIAPenetrancePedigreemedicine.anatomical_structurePhenotypeFemalemedicine.medical_specialtyGenotypeENDOPLASMIC-RETICULUMGenes RecessiveMETABOLISMBiologyGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesDogscanine geneticsInternal medicinePlacentaRETINOL-BINDING-PROTEINGeneticsmedicineAnimalsHumansRecessiveMALFORMATIONSBIOCHEMICAL BASISAmino Acid SequenceAlleleEye Disease and Disorders of VisionNutritiongenome-wide association study030102 biochemistry & molecular biologywestern blottingMUTATIONSta1184RBP4maternal inheritancemedicine.diseaseRetinol-Binding ProteinsRetinol binding proteinnuclear magnetic resonance030104 developmental biologyEndocrinologychemistryGeneslcsh:Biology (General)microphthalmiaGenetic LociHela Cells1182 Biochemistry cell and molecular biologyCongenital Structural Anomalies3111 BiomedicineBiochemistry and Cell BiologyDigestive DiseasesGenomic imprintingRetinol-Binding Proteins PlasmaHeLa Cells
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Polymeric monolithic microcartridges with gold nanoparticles for the analysis of protein biomarkers by on-line solid-phase extraction capillary elect…

2020

In this study, polymeric monoliths with gold nanoparticles (AuNP@monolith) were investigated as microcartridges for the analysis of protein biomarkers by on-line solid-phase extraction capillary electrophoresis-mass spectrometry (SPE-CE-MS). “Plug-and-play” microcartridges (7 mm) were prepared from a glycidyl methacrylate (GMA)-based monolithic capillary column (5 cm x 250 µm i.d.), which was modified with ammonia and subsequently functionalized with gold nanoparticles (AuNPs). The performance of these novel microcartridges was evaluated with human transthyretin (TTR), which is a protein related to different types of familial amyloidotic polyneuropathies (FAP). Protein retention depended on…

MASS SPECTROMETRYPolymersMetal NanoparticlesOr010402 general chemistryMass spectrometry01 natural sciencesBiochemistryCapillary electrophoresis–mass spectrometryMass SpectrometryAnalytical Chemistry//purl.org/becyt/ford/1 [https]Capillary electrophoresisCAPILLARY ELECTROPHORESISLimit of DetectionElectroforesi capil·lar//purl.org/becyt/ford/1.4 [https]HumansPrealbuminSolid phase extractionChromatographyNanopartículesChemistryElutionSolid Phase Extraction010401 analytical chemistryOrganic ChemistryON-LINE SOLID-PHASE EXTRACTIONElectrophoresis CapillaryReproducibility of ResultsGeneral MedicineMONOLITHIC MICROCARTRIDGETRANSTHYRETIN0104 chemical sciencesEspectrometria de massesIsoelectric pointColloidal goldGOLD NANOPARTICLESEpoxy CompoundsMethacrylatesNanoparticlesGoldIon trapBiomarkers
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A European family with histidine 58 transthyretin mutation in familial amyloid polyneuropathy

1997

1. IntroductionMore than 50 mutations of the transthyretin (TTR) [1]molecule resulting in different clinical forms of amyloidosisincluding familial amyloid polyneuropathy (FAP) havebeen reported to date. Within this FAP spectrum severaltransthyretin mutations are more frequent, others are rare.One mutation, the codon 58 histidine for leucine has pre-viously been recorded only in American subjects (Mary-land/German type), originally reported in a large kinship[2,3] and in another family from Ohio [4]. In the originaldescription of the Maryland/German type of amyloidosis[2], it was stated that the early immigrants in this pedigreewere from the Rhine river area, "nearly all of them from thelef…

MalePathologymedicine.medical_specialtyAtaxiaAmyloid Neuropathiesmedicine.disease_causeAtrophyLeucineGermanymedicineHumansPoint MutationPrealbuminHistidineCodonGenetics (clinical)Genes DominantMutationDysesthesiabiologybusiness.industryPoint mutationAmyloidosisMiddle Agedmedicine.diseaseUnited StatesTransthyretinNeurologyPediatrics Perinatology and Child Healthbiology.proteinNeurology (clinical)medicine.symptomRestriction fragment length polymorphismbusinessNeuromuscular Disorders
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Monitoring effectiveness and safety of Tafamidis in transthyretin amyloidosis in Italy: a longitudinal multicenter study in a non-endemic area

2016

Tafamidis is a transthyretin (TTR) stabilizer able to prevent TTR tetramer dissociation. There have been a few encouraging studies on Tafamidis efficacy in early-onset inherited transthyretin amyloidosis (ATTR) due to Val30Met mutation. However, less is known about its efficacy in later disease stages and in non-Val30Met mutations. We performed a multi-center observational study on symptomatic ATTR patients prescribed to receive Tafamidis. We followed up patients according to a standardized protocol including general medical, cardiological and neurological assessments at baseline and every 6 months up to 3 years. Sixty-one (42 males) patients were recruited. Only 28 % of enrolled subjects h…

MaleTafamidisAmyloid polyneuropathyNeurologyCardiomyopathyDisease030204 cardiovascular system & hematologySeverity of Illness IndexTransthyretinchemistry.chemical_compound0302 clinical medicinePrealbuminTafamidiLongitudinal StudiesStage (cooking)Aged 80 and overBenzoxazolesbiologyAmyloidosisMiddle Agedamyloid polyneuropathy; tafamidis; transthyretinPrognosisTafamidisSettore MED/26 - NEUROLOGIATreatment OutcomeItalyNeurologyDisease ProgressionFemaleAmyloid polyneuropathy; Tafamidis; Transthyretin; Neurology (clinical); NeurologyAdultmedicine.medical_specialty03 medical and health sciencesInternal medicineSeverity of illnessmedicineHumansAgedAmyloid Neuropathies Familialbusiness.industrynutritional and metabolic diseasesmedicine.diseaseSurgeryTransthyretinchemistryMutationbiology.proteinNeurology (clinical)business030217 neurology & neurosurgeryFollow-Up StudiesJournal of Neurology
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