Evidence map›Paper›PMID 31705628›Full record

ArticleJournal of cellular and molecular medicine2020

y+LAT1 and y+LAT2 contribution to arginine uptake in different human cell models: Implications in the pathophysiology of Lysinuric Protein Intolerance.

Bianca Maria Rotoli, Amelia Barilli, Rossana Visigalli, Francesca Ferrari, Valeria Dall'Asta

Open access · goldAbstract read
In one paragraph

Article in Journal of cellular and molecular medicine, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. [Enteral nutrition support for lysinuric protein intolerance: a case report and literature review].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2023
    Review
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 1 institution in 1 country.

Bianca Maria RotoliLaboratory of General Pathology, Department of Medicine and Surgery (DiMec), University of Parma, Parma, Italy.
Amelia BarilliLaboratory of General Pathology, Department of Medicine and Surgery (DiMec), University of Parma, Parma, Italy.
Rossana VisigalliLaboratory of General Pathology, Department of Medicine and Surgery (DiMec), University of Parma, Parma, Italy.
Francesca FerrariLaboratory of General Pathology, Department of Medicine and Surgery (DiMec), University of Parma, Parma, Italy.
Valeria Dall'AstaLaboratory of General Pathology, Department of Medicine and Surgery (DiMec), University of Parma, Parma, Italy.ORCID 0000-0001-8540-0916
University of Parma · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

y+LAT1 (encoded by SLC7A7), together with y+LAT2 (encoded by SLC7A6), is the alternative light subunits composing the heterodimeric transport system y+L for cationic and neutral amino acids. SLC7A7 mutations cause lysinuric protein intolerance (LPI), an inherited multisystem disease characterized by low plasma levels of arginine and lysine, protein-rich food intolerance, failure to thrive, hepatosplenomegaly, osteoporosis, lung involvement, kidney failure, haematologic and immunological disorders. The reason for the heterogeneity of LPI symptoms is thus far only poorly understood. Here, we aimed to quantitatively compare the expression of SLC7A7 and SLC7A6 among different human cell types and evaluate y+LAT1 and y+LAT2 contribution to arginine transport. We demonstrate that system y+L-mediated arginine transport is mainly accounted for by y+LAT1 in monocyte-derived macrophages (MDM) and y+LAT2 in fibroblasts. The kinetic analysis of arginine transport indicates that y+LAT1 and y+LAT2 share a comparable affinity for the substrate. Differences have been highlighted in the expression of SLC7A6 and SLC7A7 mRNA among different cell models: while SLC7A6 is almost equally expressed, SLC7A7 is particularly abundant in MDM, intestinal Caco-2 cells and human renal proximal tubular epithelial cells (HRPTEpC). The characterization of arginine uptake demonstrates that system y+L is operative in renal cells and in Caco-2 where, at the basolateral side, it mediates arginine efflux in exchange with leucine plus sodium. These findings explain the defective absorption/reabsorption of arginine in LPI. Moreover, y+LAT1 is the prevailing transporter in MDM sustaining a pivotal role in the pathogenesis of immunological complications associated with the disease.

Indexed as

Amino Acid Metabolism, Inborn ErrorsAmino Acid Transport Systems, BasicAmino Acid Transport System y+LArginineBiological TransportCaco-2 CellsFibroblastsHumansKidney TubulesLysineMacrophagesMutationSodiumAmino Acid Transport Systems, BasicAmino Acid Transport System y+LArginineLysineSLC7A6 protein, humanSLC7A7 protein, humanSodiumlysinuric protein intoleranceSLC7A6SLC7A7system B0,+system y+L

Identifiers

PMID31705628
PMCPMC6933409
OpenAlexW2984380861

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.