Betina Córsico

ORCID: 0000-0003-2606-5606
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About
Contact & Profiles
Research Areas
  • Peroxisome Proliferator-Activated Receptors
  • Drug Transport and Resistance Mechanisms
  • Lipid Membrane Structure and Behavior
  • Trypanosoma species research and implications
  • Lipid metabolism and biosynthesis
  • Parasites and Host Interactions
  • Helminth infection and control
  • Protein Structure and Dynamics
  • Inflammatory mediators and NSAID effects
  • Parasitic infections in humans and animals
  • Amoebic Infections and Treatments
  • RNA and protein synthesis mechanisms
  • Cholesterol and Lipid Metabolism
  • Diabetes, Cardiovascular Risks, and Lipoproteins
  • Cancer, Lipids, and Metabolism
  • Parasite Biology and Host Interactions
  • Metabolism and Genetic Disorders
  • Peptidase Inhibition and Analysis
  • Immune Response and Inflammation
  • Parasitic Infections and Diagnostics
  • Cancer, Hypoxia, and Metabolism
  • Congenital Anomalies and Fetal Surgery
  • Biotin and Related Studies
  • Influenza Virus Research Studies
  • Receptor Mechanisms and Signaling

Consejo Nacional de Investigaciones Científicas y Técnicas
2011-2023

Universidad Nacional de La Plata
2011-2022

Biochemistry Research Institute of La Plata
2010-2022

Instituto de Biotecnología y Biología Molecular
2012-2019

Centro Científico Tecnológico - La Plata
2009-2013

Rutgers, The State University of New Jersey
1998-2004

Institute of Astronomy and Space Physics
2003

Instituto de Química y Fisicoquímica Biológicas
2003

National Institute of Immunology
1994

Fatty acid binding proteins (FABPs) exhibit a β-barrel topology, comprising 10 antiparallel β-sheets capped by two short α-helical segments. Previous studies suggested that fatty transfer from several FABPs occurs during interaction between the protein and acceptor membrane, helical domain of plays an important role in this process. In study, we employed helix-less variant intestinal FABP (IFABP-HL) examined rate mechanism fluorescent anthroyloxy acids (AOFA) to model membranes comparison...

10.1073/pnas.95.21.12174 article EN other-oa Proceedings of the National Academy of Sciences 1998-10-13

Antigen B (EgAgB) is an abundant lipoprotein released by the larva of cestode Echinococcus granulosus into host tissues. Its protein moiety belongs to cestode-specific family known as hydrophobic ligand binding (HLBP), and encoded five gene subfamilies (EgAgB8/1-EgAgB8/5). The functions EgAgB in parasite biology remain unclear. It may play a role parasite's lipid metabolism since it carries lipids that E. unable synthesise. On other hand, there evidence supporting immuno-modulating...

10.1186/s13071-016-1350-7 article EN cc-by Parasites & Vectors 2016-02-04

Nitro-fatty acids (NO2-FA) are electrophilic lipid mediators derived from unsaturated fatty acid nitration. These species produced endogenously by metabolic and inflammatory reactions mediate anti-oxidative anti-inflammatory responses. NO2-FA have been postulated as partial agonists of the Peroxisome Proliferator-Activated Receptor gamma (PPARγ), which is predominantly expressed in adipocytes myeloid cells. Herein, we explored molecular cellular events associated with PPARγ activation...

10.1016/j.redox.2019.101376 article EN cc-by-nc-nd Redox Biology 2019-11-10

Intestinal fatty acid binding protein (IFABP) and liver FABP (LFABP), homologous proteins expressed at high levels in intestinal absorptive cells, employ markedly different mechanisms for the transfer of acids (FAs) to acceptor membranes. Transfer from IFABP occurs during protein−membrane collisional interactions, while LFABP, by diffusion through aqueous phase. Earlier, we had shown that helical domain is critical determining its FA mechanism. In study presented here, have engineered a pair...

10.1021/bi0357356 article EN Biochemistry 2004-03-01

Intestinal-fatty acid binding protein (IFABP; FABP2) is a 15-kDa intracellular abundantly present in the cytosol of small intestinal (SI) enterocyte. High-fat (HF) feeding IFABP

10.1152/ajpgi.00120.2019 article EN AJP Gastrointestinal and Liver Physiology 2020-01-06

Liver fatty acid-binding protein (LFABP; FABP1) is expressed both in liver and intestinal mucosa. Mice null for LFABP were recently shown to have altered metabolism of not only acids but also monoacylglycerol, the two major products dietary triacylglycerol hydrolysis (Lagakos, W. S., Gajda, A. M., Agellon, L., Binas, B., Choi, V., Mandap, Russnak, T., Zhou, Y. X., Storch, J. (2011) Am. Physiol. Gastrointest. 300, G803–G814). Nevertheless, binding transport monoacylglycerol (MG) by are...

10.1074/jbc.m113.473579 article EN cc-by Journal of Biological Chemistry 2013-05-09

Fatty acid and retinol-binding proteins (FARs) comprise a family of unusual α-helix rich lipid-binding found exclusively in nematodes. They are secreted into host tissues by parasites plants, animals humans. The structure FAR protein from the free-living nematode Caenorhabditis elegans is available, but this [C. FAR-7 (Ce-FAR-7)] subfamily FARs that does not appear to be important at host/parasite interface. We have therefore examined [Necator americanus FAR-1 (Na-FAR-1)] blood-feeding...

10.1042/bj20150068 article EN cc-by Biochemical Journal 2015-08-29

Intestinal fatty acid binding protein (IFABP) is thought to participate in the intracellular transport of acids (FAs). Fatty transfer from IFABP phospholipid membranes proposed occur during protein-membrane collisional interactions. In this study, we analyzed participation electrostatic and hydrophobic interactions mechanism FA membranes. Using a fluorescence resonance energy assay, examined rate anthroyloxy-fatty analogs a) different composition; b) chemically modified IFABPs, which...

10.1194/jlr.m500140-jlr200 article EN cc-by Journal of Lipid Research 2005-05-02

Fatty acid transfer from intestinal fatty acid-binding protein (IFABP) to phospholipid membranes occurs during protein-membrane collisions. Electrostatic interactions involving the alpha-helical "portal" region of have been shown be great importance. In present study, role specific lysine residues in IFABP was directly examined. A series point mutants rat engineered which positive charges this domain were eliminated or reversed. Using a fluorescence resonance energy assay, we analyzed rates...

10.1074/jbc.m511943200 article EN cc-by Journal of Biological Chemistry 2006-03-22

Celiac disease (CD) is an immune‐mediated enteropathy that develops in genetically susceptible individuals following exposure to dietary gluten. Severe changes at the intestinal mucosa observed untreated CD patients are linked level and pattern of expression different genes. Fully differentiated epithelial cells express two isoforms fatty acid binding proteins (FABPs): liver, IFABP LFABP, respectively. These bind transport long chain acids also have other important biological roles signaling...

10.1155/2015/738563 article EN cc-by Mediators of Inflammation 2015-01-01

Previous evidence indicated that discoidal reconstituted high density lipoproteins (rHDL) of apolipoprotein A-I (apoA-I) can interact with lipid membranes (Tricerri, M. A., Córsico, B., Toledo, J. D., Garda, H. and Brenner, R. (1998) Biochim. Biophys. Acta 1391, 67–78). With the aim studying this interaction, photoactivable reagents protein cleavage CNBr hydroxylamine were used. The generic hydrophobic reagent 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine gave information on apoA-I...

10.1074/jbc.m011533200 article EN cc-by Journal of Biological Chemistry 2001-05-01

Background Growth and maintenance of hydatid cysts produced by Echinococcus granulosus have a high requirement for host lipids biosynthetic processes, membrane building possibly cellular developmental signalling. This requires degree lipid trafficking facilitated transporter proteins. Members the fatty acid binding protein (FABP) family been identified in granulosus, one which, EgFABP1 is expressed at tegumental level protoscoleces, but it has also described both cyst fluid secretions...

10.1371/journal.pntd.0001893 article EN cc-by PLoS neglected tropical diseases 2012-11-15

Intestinal fatty acid binding protein (IFABP) appears to interact directly with membranes during transfer [Hsu, K. T., and Storch, J. (1996) Biol. Chem. 271, 13317−13323]. The largely α-helical "portal" domain of IFABP was critical for these protein−membrane interactions. In the present studies, a helixless variant (IFABP-HL) acidic monolayers 1,2-dimyristoylphosphatidic (DMPA) has been monitored by surface pressure measurements, Brewster angle microscopy (BAM), infrared...

10.1021/bi002252i article EN Biochemistry 2001-01-26

Two paralogous groups of fatty acid-binding proteins (FABPs) have been described in vertebrate liver: liver FABP (L-FABP) type, extensively characterized mammals, and basic (Lb-FABP) found fish, amphibians, reptiles, birds. We describe here the toad Lb-FABP complete amino acid sequence, its X-ray structure to 2.5 Å resolution, ligand-binding properties, mechanism transfer phospholipid membranes. Alignment sequence with known L-FABPs Lb-FABPs shows that it is more closely related other...

10.1021/bi034213n article EN Biochemistry 2003-06-17

10.1016/j.bbalip.2010.05.008 article EN Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 2010-06-11
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