ArticleJournal of animal science2026
The role of the y(+)L-type amino acid transporter 2 in promoting zinc absorption as zinc proteinate with moderate chelation strength in broiler primary duodenal epithelial cells.
Article in Journal of animal science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 2 papers.
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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.
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Who cites it
2 citing papers in PubMed.
- In-depth examination of the zinc-mitigation of the molecular effects of heat stress-induced intestinal damage in broilers.Poultry science · 2026Article
- Vitamin D receptor silencing impairs the 1,25-dihydroxyvitamin DPoultry science · 2026Article
Corrections and comments
- Erratum issued
Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
No study is currently available regarding the roles of the amino acid transporters in promoting mineral absorption in animals. To study whether the y(+)L-type amino acid transporter 2 (y+LAT2) participates in enhancing Zn absorption as Zn proteinate with moderate chelation strength (Zn-Prot M) in broilers, three experiments were carried out to investigate the effects of y+LAT2 silencing and overexpression on zinc (Zn) absorption as Zn-Prot M and related gene expressions in broiler primary duodenal epithelial cells (BPDECs) contrasted with Zn sulfate (ZnSO4). In experiment 1, three pairs of siRNAs (si-494, si-834, and si-1153) targeting y+LAT2 were synthesized and transfected within the cells to identify the optimal siRNA for silencing y+LAT2 mRNA expression, and the data were analyzed by one-way ANOVA. In experiment 2, cells were incubated for 2 h in either a DMEM/F12 complete medium without Zn supplementation (Control) or the same medium enriched with 400 μmol Zn/liter as ZnSO4 or Zn-Prot M, with or without the only one effective siRNA targeting y+LAT2, and the data were analyzed by two-way ANOVA. In experiment 3, with or without the recombinant adenovirus plasmid encoding y+LAT2, cells were also treated for 2 h with the same media as in experiment 2, and the data were analyzed by two-way ANOVA. The results demonstrated that in experiment 1, the si-494 was the only one effective (P < 0.0001) siRNA for inhibiting y+LAT2 mRNA expression. In experiment 2, y+LAT2 silencing reduced its own mRNA and protein abundances (P < 0.0001) by 46% and 14% and Zn absorption from Zn-Prot M by 34% (P < 0.05), with no effect (P > 0.05) on Zn absorption from ZnSO4. In experiment 3, y+LAT2 overexpression elevated its own mRNA and protein expressions by 949% and 18% (P < 0.0001) and Zn absorption from Zn-Prot M by 73% (P < 0.05), but didn't affect (P > 0.05) Zn absorption from ZnSO4. Additionally, Zn-Prot M upregulated (P < 0.05) the y+LAT2 protein expression compared to the Control and ZnSO4 by 12 to 17%, with no impact (P > 0.07) on the y+LAT2 mRNA expression, regardless of y+LAT2 silencing or overexpression. In conclusion, the y+LAT2 took part in promoting Zn absorption as Zn-Prot M in BPDECs.
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