Journal
FOOD & FUNCTION
Volume 12, Issue 18, Pages 8787-8799Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1fo01075a
Keywords
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Funding
- Sichuan Science and Technology Program [2020YJ0398]
- Specific Research Supporting Program for Discipline Construction in Sichuan Agricultural University [03570126]
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This study demonstrated that tryptophan enhances cell migration in porcine intestine epithelial cells (IPEC-J2) through the CaSR/Rac1/PLC-γ1 signaling pathway.
This study aimed to investigate the effect of tryptophan on cell migration and its underlying mechanism in porcine intestine epithelial cells (IPEC-J2). This study shows that tryptophan can modulate IPEC-J2 cell proliferation, enhance cell migration and the protein concentration of calcium-sensing receptors (CaSR), total ras-related C3 botulinum toxin substrate 1 (total Rac1), Rho family member 1 of GTP-binding protein (GTP-rac1), and phosphorylated phospholipase C gamma 1 (p-PLC-gamma 1). Moreover, Rac1, phospholipase C-gamma 1 (PLC-gamma 1) silencing or CaSR inhibitor (NPS2143) inhibited tryptophan-induced upregulation of cell migration. In contrast, tryptophan enhanced the cell migration area and protein concentration of total Rac1, GTP-rac1, and phosphorylated PLC gamma 1 in cells transfected with wild type CaSR. The overexpression of CaSR increased cell migration, which was reduced by Rac1 or PLC-gamma 1 silencing. Collectively, our results suggested that tryptophan can improve IPEC-J2 cell migration through the CaSR/Rac1/PLC-gamma 1 signaling pathway.
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