scholarly journals Uptake of Manganese from the Manganese-Lysine Complex in Primary Chicken Intestinal Epithelial Cells

Animals ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 559
Author(s):  
Shiping Bai ◽  
Keying Zhang ◽  
Xuemei Ding ◽  
Jianping Wang ◽  
Qiufeng Zeng ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Mrna Expression ◽  
Transport System ◽  
Intestinal Epithelial Cells ◽  
Mrna Level ◽  
Intestinal Epithelial ◽  
Divalent Metal Transporter 1 ◽  
Divalent Metal Transporter ◽  
Cationic Amino Acid ◽  
Metal Transporter

Organic manganese (Mn) sources can replace inorganic Mn as dietary Mn supplements in poultry. To compare the uptake of Mn from the Mn-lysine complex (MnLys) and MnSO4, we first established the primary chicken intestinal epithelial cells (IECs) model and used it to determine Mn uptake. The MnLys increased the uptake of Mn compared to MnSO4. The uptake of Mn decreased in the IECs with Fe addition in the medium regardless of the Mn sources. The MnLys decreased the Mn2+ efflux transporter ferroportin 1 (FPN1) mRNA level but did not influence the Mn2+ influx transporter divalent metal transporter 1 (DMT1) mRNA expression when compared to MnSO4. The results above indicated that the increase of Mn accumulation for MnLys at least partly was due to the decrease of Mn efflux by reduced FPN1 expression. The addition of N-ethylmaleimide, an L-lysine transport system y+ inhibitor, decreased the uptake of Mn from MnLys but did not affect the uptake of Mn from MnSO4. The cycloheximide, as an L-lysine transport system b0,+ activator, increased the uptake of Mn from MnLys, whereas they did not influence the uptake of Mn from MnSO4. The MnLys increased the system y+ members cationic amino acid transporter (CAT) 1 and CAT2, and system b0,+ components rBAT and b0,+AT mRNA expression when compared to MnSO4. These results suggested that the uptake of MnLys complex might be transported by CAT1/2 and system b0,+, which was different from the ionized Mn2+ uptake pathway. In conclusion, the uptake of Mn from MnLys complex not only might be uptake through the ionized Mn2+ pathway, but also appeared to be transported through the CAT1/2 and system b0,+ in primary chicken IECs.

scholarly journals Hyperglycemia Does Not Affect Iron Mediated Toxicity of Cultured Endothelial and Renal Tubular Epithelial Cells: Influence of L-Carnosine

2016 ◽  
Vol 2016 ◽  
pp. 1-9 ◽  
Author(s):  
Shiqi Zhang ◽  
Emmanouil Ntasis ◽  
Sarah Kabtni ◽  
Jaap van den Born ◽  
Gerjan Navis ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Umbilical Vein ◽  
Receptor Protein ◽  
Dependent Manner ◽  
Tubular Epithelial Cells ◽  
Intracellular Iron ◽  
Alternative Source ◽  
Divalent Metal Transporter 1 ◽  
Divalent Metal Transporter ◽  
Metal Transporter

Iron has been suggested to affect the clinical course of type 2 diabetes (T2DM) as accompanying increased intracellular iron accumulation may provide an alternative source for reactive oxygen species (ROS). Although carnosine has proven its therapeutic efficacy in rodent models of T2DM, little is known about its efficacy to protect cells from iron toxicity. We sought to assess if high glucose (HG) exposure makes cultured human umbilical vein endothelial cells (HUVECs) and renal proximal tubular epithelial cells (PTECs) more susceptible to metal induced toxicity and if this is ameliorated by L-carnosine. HUVECs and PTECs, cultured under normal glucose (5 mM, NG) or HG (30 mM), were challenged for 24 h with FeCl3. Cell viability was not impaired under HG conditions nor did HG increase susceptibility to FeCl3. HG did not change the expression of divalent metal transporter 1 (DMT1), ferroportin (IREG), and transferrin receptor protein 1 (TFRC). Irrespective of glucose concentrations L-carnosine prevented toxicity in a dose-dependent manner, only if it was present during the FeCl3challenge. Hence our study indicates that iron induced cytotoxicity is not enhanced under HG conditions. L-Carnosine displayed a strong protective effect, most likely by chelation of iron mediated toxicity.

Energetics of sugar transport by isolated intestinal epithelial cells: effects of cytochalasin B

1979 ◽  
Vol 237 (1) ◽  
pp. C56-C63 ◽  
Author(s):  
G. A. Kimmich ◽  
J. Randles
Keyword(s):  
Steady State ◽  
Epithelial Cells ◽  
Transport System ◽  
Cytochalasin B ◽  
Intestinal Epithelial Cells ◽  
Sugar Accumulation ◽  
Facilitated Diffusion ◽  
Intestinal Epithelial ◽  
Passive System ◽  
Concentration Gradients

The capability of isolated intestinal epithelial cells to establish concentration gradients of 3-O-methylglucose (3-OMG) by a Na+-dependent transport system is limited by concomitant function of a Na+-independent, facilitated diffusion transport system. Monosaccharides accumulated by the active system are continuously lost via the passive system, which acts to lower steady-state sugar gradients maintained by the cell. Cytochalasin B is a potent inhibitor of the passive system and allows the cells to establish a sugar gradient that is much higher than normal. When extracellular [3-;OMG] is 1 mM, cytochalasin induces sugar accumulation ratios of 30-;fold (+/- phlorizin) in contrast to control ratios of approximately 10-;fold. When [3-;OMG] is 0.1 mM, cytochalasin (0.1 mM) induces 40-;fold accumulation ratios. When changes in extracellular sugar concentration are considered, steady-state concentration gradients observed are 70-;fold. For a Na:sugar coupling stoichiometry of 1:1, gradients of this magnitude represent the approximate theoretical maximum for a transport system driven exclusively by the transmembrane electrochemical potential for Na+.

scholarly journals Sodium butyrate stimulates NHE8 expression via its role on activating NHE8 basal promoter activity

2015 ◽  
Vol 309 (6) ◽  
pp. G500-G505 ◽  
Author(s):  
Hua Xu ◽  
Anthony McCoy ◽  
Jing Li ◽  
Yang Zhao ◽  
Fayez K. Ghishan
Keyword(s):  
Epithelial Cells ◽  
Mrna Expression ◽  
Promoter Region ◽  
Intestinal Epithelial Cells ◽  
Gene Promoter ◽  
Sodium Absorption ◽  
Intestinal Epithelial ◽  
Mobility Shift ◽  
Bacterial Fermentation ◽  
Butyrate Treatment

Butyrate is a major metabolite in colonic lumen. It is produced from bacterial fermentation of dietary fiber. Butyrate has been shown to stimulate electroneutral sodium absorption through its regulation on sodium/hydrogen exchanger 3 (NHE3). Although NHE8, the newest addition of intestinal NHE family, is involved in sodium absorption in the intestinal tract, whether butyrate modulates NHE8 expression in the intestinal epithelial cells is not known. In the current study, we showed that butyrate treatment strongly induced NHE8 protein and NHE8 mRNA expression in human intestinal epithelial cells. Transfection with the human NHE8 promoter reporter constructs showed that butyrate treatment stimulated reporter gene expression at an amount comparable with its stimulation of NHE8 mRNA expression. Interestingly, a similar result was also observed in human NHE8 promoter transfected cells after trichostatin (TSA) treatment. Gel mobility shift assay identified an enhanced Sp3 protein binding on the human NHE8 basal promoter region upon butyrate stimulation. Furthermore, Sp3 acetylation modification is involved in butyrate-mediated NHE8 activation in Caco-2 cells. Our findings suggest that the mechanism of butyrate action on NHE8 expression involves enhanced Sp3 interaction at the basal promoter region of the human NHE8 gene promoter to activate NHE8 gene transcription. Thus butyrate is involved in intestinal regulation of NHE8 resulting enhanced sodium absorption.

Divalent metal transporter-1 decreases metal-related injury in the lung

2005 ◽  
Vol 289 (3) ◽  
pp. L460-L467 ◽  
Author(s):  
Andrew J. Ghio ◽  
Claude A. Piantadosi ◽  
Xinchao Wang ◽  
Lisa A. Dailey ◽  
Jacqueline D. Stonehuerner ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Metal Transport ◽  
Airway Epithelial Cells ◽  
Divalent Metal ◽  
Primary Role ◽  
Airway Epithelial ◽  
Divalent Metal Transporter 1 ◽  
Divalent Metal Transporter ◽  
Metal Transporter

Exposure to airborne particulates makes the detoxification of metals a continuous challenge for the lungs. Based on the fate of iron in airway epithelial cells, we postulated that divalent metal transporter-1 (DMT1) participates in detoxification of metal associated with air pollution particles. Homozygous Belgrade rats, which are functionally deficient in DMT1, exhibited diminished metal transport from the lower respiratory tract and greater lung injury than control littermates when exposed to oil fly ash. Preexposure of normal rats to iron in vivo increased expression of the isoform of DMT1 protein that lacked an iron-response element (−IRE), accelerated metal transport out of the lung, and decreased injury after particle exposure. In contrast, normal rats preexposed to vanadium showed less expression of the −IRE isoform of DMT1, decreased metal transport, and greater pulmonary injury after particle instillation. Respiratory epithelial cells in culture gave similar results. Also, DMT1 mRNA and protein expression for the −IRE isoform increased or decreased in these cells when exposed to iron or vanadium, respectively. These results thus demonstrate for the first time a primary role for DMT1 in lung metal transport and detoxification.

scholarly journals Active or Autoclaved Akkermansia muciniphila Relieves TNF-α-Induced Inflammation in Intestinal Epithelial Cells Through Distinct Pathways

2021 ◽  
Vol 12 ◽  
Author(s):  
Yuheng Luo ◽  
Cong Lan ◽  
Kunhong Xie ◽  
Hua Li ◽  
Estelle Devillard ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Signaling Pathway ◽  
Intestinal Inflammation ◽  
Intestinal Epithelial Cells ◽  
Mrna Level ◽  
Intestinal Epithelial ◽  
Akkermansia Muciniphila ◽  
Tnf Α ◽  
Key Genes ◽  
Cell Cycle Signaling

Intestinal inflammation is a major threat to the health and growth of young animals such as piglets. As a next-generation probiotics, limited studies have shown that Akkermansia muciniphila could alleviate inflammation of intestinal epithelial cells (IECs). In this study, a TNF-α-induced inflammatory model of IPEC-J2 cells, the intestinal porcine enterocytes, was built to evaluate the effects of active or inactive A. muciniphila on the inflammation of IECs. The viability of IPEC-J2 cells was the highest when treated with active (108 copies/mL) or inactive (109 copies/mL) A. muciniphila for 7.5 h (P < 0.01). Treated with 20 ng/mL of TNF-α and followed by a treatment of A. muciniphila, the mRNA level of proinflammatory cytokines (IL-8, IL-1β, IL-6 and TNF-α) was remarkably reduced (P < 0.05) along with the increased mRNA level of tight junction proteins (ZO-1 and Occludin, P < 0.05). Flow cytometry analysis showed that active or inactive A. muciniphila significantly suppressed the rate of the early and total apoptotic of the inflammatory IPEC-J2 cells (P < 0.05). According to results of transcriptome sequencing, active and inactive A. muciniphila may decline cell apoptosis by down-regulating the expression of key genes in calcium signaling pathway, or up-regulating the expression of key genes in cell cycle signaling pathway. And the bacterium may alleviate the inflammation of IECs by down-regulating the expression of PI3K upstream receptor genes. Our results indicate that A. muciniphila may be a promising NGP targeting intestinal inflammation.

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