Evidence map›Paper›PMID 21539932›Full record

ArticleBiochimica et biophysica acta

Interaction of enterocyte FABPs with phospholipid membranes: clues for specific physiological roles.

Lisandro J Falomir-Lockhart, Gisela R Franchini, María Ximena Guerbi, Judith Storch, Betina Córsico

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.0field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Article
  6. FABP1 knockdown in human enterocytes impairs proliferation and alters lipid metabolism.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Article
  7. Association of IL-1β, IL-1Ra and FABP1 gene polymorphisms with the metabolic features of polycystic ovary syndrome.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2017
    Article
  8. Article
  9. Identification of a two-component fatty acid kinase responsible for host fatty acid incorporation by Staphylococcus aureus.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  10. Article
  11. Article
  12. Article
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 2 countries.

Lisandro J Falomir-LockhartInstituto de Investigaciones Bioquímicas de La Plata, Facultad de Ciencias Médicas, Universidad Nacional de La Plata, La Plata, Argentina.
Gisela R Franchini
María Ximena Guerbi
Judith Storch
Betina Córsico
Biochemistry Research Institute of La Plata · ARConsejo Nacional de Investigaciones Científicas y Técnicas · ARRutgers, The State University of New Jersey · USUniversidad Nacional de La Plata · AR

Funding

Supplement to DK-38389 Lipid Transport in the IntestineR01DK038389 · NIDDK · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI SAMPATH, HARINI, STORCH, JUDITH · 1992 to 2025
$8.6M
FATTY ACID ASSIMILATION IN THE INTESTINER29DK038389 · NIDDK · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI STORCH, JUDITH · 1987 to 1991
–
NIDDK NIH HHS DK38389NIDDK NIH HHS R01 DK038389
6 · The paper itself

Abstract

Intestinal and liver fatty acid binding proteins (IFABP and LFABP, respectively) are cytosolic soluble proteins with the capacity to bind and transport hydrophobic ligands between different sub-cellular compartments. Their functions are still not clear but they are supposed to be involved in lipid trafficking and metabolism, cell growth, and regulation of several other processes, like cell differentiation. Here we investigated the interaction of these proteins with different models of phospholipid membrane vesicles in order to achieve further insight into their specificity within the enterocyte. A combination of biophysical and biochemical techniques allowed us to determine affinities of these proteins to membranes, the way phospholipid composition and vesicle size and curvature modulate such interaction, as well as the effect of protein binding on the integrity of the membrane structure. We demonstrate here that, besides their apparently opposite ligand transfer mechanisms, both LFABP and IFABP are able to interact with phospholipid membranes, but the factors that modulate such interactions are different for each protein, further implying different roles for IFABP and LFABP in the intracellular context. These results contribute to the proposed central role of intestinal FABPs in the lipid traffic within enterocytes as well as in the regulation of more complex cellular processes.

Indexed as

AnimalsBinding, CompetitiveBiophysical PhenomenaCytochromes cEnterocytesFatty Acid-Binding ProteinsHumansIntestinal MucosaIn Vitro TechniquesLiverMembrane LipidsPhospholipidsProtein BindingProtein Interaction Domains and MotifsUnilamellar LiposomesCytochromes cFatty Acid-Binding ProteinsMembrane LipidsPhospholipidsUnilamellar Liposomes

Identifiers

PMID21539932
PMCPMC3143005
OpenAlexW1982946708

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.