0000000000476741

AUTHOR

Eulalia Alonso

showing 4 related works from this author

An antihypertensive lactoferrin hydrolysate inhibits angiotensin I-converting enzyme, modifies expression of hypertension-related genes and enhances …

2015

This study was aimed to explore whether an antihypertensive lactoferrin hydrolysate (LFH) can inhibit angiotensin I-converting enzyme (ACE) activity and modify the expression of genes related to hypertension in human umbilical vein endothelial cells (HUVEC). LFH induced significant inhibition of ACE activity but it did not affect ACE mRNA levels after 24 h of exposure. LFH treatment significantly affected the expression of genes encoding for proteins involved in nitric oxide pathway such as soluble guanylate cyclase 1 α3 subunit (GUCY1A3; 4.42-fold increase) and nitric oxide synthase trafficking (NOSTRIN; 2.45-fold decrease). Furthermore, expression of the PTGS2/COX-2 gene encoding prostagl…

Endothelial cellsMedicine (miscellaneous)PharmacologyLactoferrin hydrolysateTranscriptomic analysisUmbilical veinNitric oxidechemistry.chemical_compoundDownregulation and upregulationTX341-641Nutrition and DieteticsAngiotensin II receptor type 1biologyNutrition. Foods and food supplyLactoferrinGUCY1A3Nitric oxideACE inhibitionNOSTRINMolecular biologyNitric oxide synthasechemistryNitric Oxide Pathwaybiology.proteinFood Science
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N-acetyl-L-glutamate in brain: assay, levels, and regional and subcellular distribution.

1991

N-Acetyl-L-glutamate (NAG), the activator of mitochondrial carbamoyl phosphate synthetase (CPS), is demonstrated by several methods, including a new HPLC assay, in the brain of mammals and of chicken. The brain levels of NAG are 200-300 times lower than the levels of N-acetyl-L-aspartate (NAA), and are similar to the levels of NAG in rat liver. The NAG levels in chicken liver are very low. Although NAG is mitochondrial in the liver, it is cytosolic in brain. Using enzyme activity and immuno assays we did not detect CPS in brain (detection limit, 12.5 micrograms/g brain), excluding that brain NAG is involved in citrullinogenesis. The regional distribution of brain NAG differs from that of NA…

MaleCentral nervous systemurologic and male genital diseasesBiochemistryCellular and Molecular NeuroscienceMiceGlutamatesSpecies SpecificitymedicineAnimalsChromatography High Pressure Liquidchemistry.chemical_classificationN acetyl L glutamateBrain ChemistryAspartic AcidSheepbiologyurogenital systemActivator (genetics)Rats Inbred StrainsGeneral MedicineCarbamoyl phosphate synthetaseEnzyme assayRatsCytosolSubcellular distributionEnzymemedicine.anatomical_structurechemistryBiochemistrybiology.proteinChickensNeurochemical research
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Dietary Arginine Slightly and Variably Affects Tissue Polyamine Levels in Male Swiss Albino Mice

2002

Many key metabolic and physiologic functions involve arginine and arginine-derived metabolites. Requirements for arginine, a "conditionally essential" amino acid for most mammalian species, are met in variable proportions by dietary intake and endogenous synthesis, the latter being sufficient to fulfill arginine needs in adult humans and mice under nonpathologic conditions. However, dietary arginine restriction causes orotic aciduria and abnormal function of the urea cycle. Furthermore, the importance of dietary arginine in the maintenance of homeostasis of arginine-derived metabolites in the body has not yet been analyzed in detail. We therefore examined whether the deprivation or suppleme…

Malechemistry.chemical_classificationmedicine.medical_specialtyNutrition and DieteticsArginineBiogenic PolyaminesMedicine (miscellaneous)SpermineBiologyArgininemedicine.diseaseDietAmino acidSpermidineMicechemistry.chemical_compoundEndocrinologychemistryUrea cycleInternal medicinemedicinePutrescineAnimalsPolyamineOrotic aciduriaThe Journal of Nutrition
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Affinity Cleavage of Carbamoyl-Phosphate Synthetase I Localizes Regions of the Enzyme Interacting with the Molecule of ATP that Phosphorylates Carbam…

1995

Two ATP molecules are used in the reaction catalyzed by carbamoyl-phosphate synthetase I. One molecule (ATPA) phosphorylates HCO3- and the other (ATPB) phosphorylates carbamate. Carbamoyl-phosphate synthetase I is a 160-kDa polypeptide consisting of a 40-kDa N-terminal moiety and a 120-kDa C-terminal moiety, the latter being composed of two similar halves of molecular mass 60 kDa. We showed [Alonso, E., Cervera, J., Garcia-Espana, A., Bendala, E. & Rubio, V. (1992) J. Biol. Chem. 267, 4524-4532] that Fe.ATP bound at the site for ATPB catalyzes the oxidative inactivation of carbamoyl-phosphate synthetase I in a model oxidative system consisting of Fe3+, ascorbate, and O2, and we detected ATP…

chemistry.chemical_classificationbiologyChemistryProtein domainCarbamate kinaseCleavage (embryo)BiochemistryCarbamoyl phosphate synthetase IAmino acidBiochemistrybiology.proteinMoietyNucleotideBinding siteEuropean Journal of Biochemistry
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