scholarly journals Layilin is critical for mediating hyaluronan 35 kDa-induced intestinal epithelial tight junction protein ZO-1 in vitro and in vivo

2018 ◽  
Vol 66 ◽  
pp. 93-109 ◽  
Author(s):  
Yeojung Kim ◽  
Gail A. West ◽  
Greeshma Ray ◽  
Sean P. Kessler ◽  
Aaron C. Petrey ◽  
...  
Keyword(s):  
Tight Junction ◽  
Tight Junction Protein ◽  
Intestinal Epithelial ◽  
Junction Protein ◽  
Epithelial Tight Junction

scholarly journals Hyaluronan 35 kDa treatment protects mice from Citrobacter rodentium infection and induces epithelial tight junction protein ZO-1 in vivo

2017 ◽  
Vol 62 ◽  
pp. 28-39 ◽  
Author(s):  
Yeojung Kim ◽  
Sean P. Kessler ◽  
Dana R. Obery ◽  
Craig R. Homer ◽  
Christine McDonald ◽  
...  
Keyword(s):  
Tight Junction ◽  
Tight Junction Protein ◽  
Citrobacter Rodentium ◽  
Junction Protein ◽  
Epithelial Tight Junction

scholarly journals Occludin regulates macromolecule flux across the intestinal epithelial tight junction barrier

2011 ◽  
Vol 300 (6) ◽  
pp. G1054-G1064 ◽  
Author(s):  
Rana Al-Sadi ◽  
Khaldun Khatib ◽  
Shuhong Guo ◽  
Dongmei Ye ◽  
Moustafa Youssef ◽  
...  
Keyword(s):  
Tight Junction ◽  
Intestinal Permeability ◽  
Transepithelial Resistance ◽  
Intestinal Epithelial ◽  
Knock Down ◽  
Large Channel ◽  
Epithelial Tight Junction ◽  
Mouse Intestine

Defective intestinal epithelial tight junction (TJ) barrier has been shown to be an important pathogenic factor contributing to the development of intestinal inflammation. The expression of occludin is markedly decreased in intestinal permeability disorders, including in Crohn's disease, ulcerative colitis, and celiac disease, suggesting that the decrease in occludin expression may play a role in the increase in intestinal permeability. The purpose of this study was to delineate the involvement of occludin in intestinal epithelial TJ barrier by selective knock down of occludin in in vitro (filter-grown Caco-2 monolayers) and in vivo (recycling perfusion of mouse intestine) intestinal epithelial models. Our results indicated that occludin small-interfering RNA (siRNA) transfection causes an increase in transepithelial flux of various-sized probes, including urea, mannitol, inulin, and dextran, across the Caco-2 monolayers, without affecting the transepithelial resistance. The increase in relative flux rate was progressively greater for larger-sized probes, indicating that occludin depletion has the greatest effect on the flux of large macromolecules. siRNA-induced knock down of occludin in mouse intestine in vivo also caused an increase in intestinal permeability to dextran but did not affect intestinal tissue transepithelial resistance. In conclusion, these results show for the first time that occludin depletion in intestinal epithelial cells in vitro and in vivo leads to a selective or preferential increase in macromolecule flux, suggesting that occludin plays a crucial role in the maintenance of TJ barrier through the large-channel TJ pathway, the pathway responsible for the macromolecule flux.

scholarly journals Spermine Protects Intestinal Barrier Integrity Through Rac1/PLC-γ1 Signalling Pathway in Piglets

2020 ◽  
Author(s):  
Guangmang Liu ◽  
Xiaomei Xu ◽  
Caimei Wu ◽  
Gang Jia ◽  
Hua Zhao ◽  
...  
Keyword(s):  
Tight Junction ◽  
Intestinal Barrier ◽  
Signalling Pathway ◽  
Tight Junction Protein ◽  
Intestinal Integrity ◽  
Tnf Α ◽  
Junction Protein ◽  
Intestinal Barrier Integrity

Abstract Background: Weaning stress can lead to the disruption of tight junctions and increased intestinal permeabilty, which contributes to the initiation and development of many disease, such as Crohn’s disease and ulcerative colitis. Pigs are more ideal models for human studies than other animals. However, no information is found about the relationship of intestinal integrity and spermine supplementation in pigs. The objective of this study is to investigate whether spermine protects intestinal barrier integrity via Rac1/PLC-γ1 signalling pathway in piglets. Methods: In vivo, the piglets were categorised into the control group and the spermine group, which was fed with spermine at 0.4 mmol kg−1 body weight for 7 hours and 3, 6 and 9 days. In vitro, we examined whether spermine protects the intestinal barrier after TNF-α challenge through Ras-related C3 botulinum toxin substrate 1 (Rac1)/Phospho-lipase C-γ1 (PLC-γ1) signalling pathway. Results: In vivo study revealed that the spermine treatment upregulated tight junction protein mRNA levels and Rac1/PLC-γ1 signalling pathway gene expression in the jejunum of piglets. The serum D-lactate content was significantly reduced after spermine treatment (P < 0.05). In vitro study revealed that 0.1 μM spermine significantly increased the levels of tight junction protein expression, Rac1/PLC-γ1 signalling pathway and transepithelial electrical resistance, and decreased paracellular permeability (P < 0.05). Further experiments showed that spermine treatment increased the levels of tight junction protein expression, Rac1/PLC-γ1 signalling pathway and transepithelial electrical resistance, and decreased paracellular permeability compared with the NSC-23766 and U73122 treatment with spermine after TNF-α challenge (P < 0.05). Conclusion: spermine protects intestinal integrity through the Rac1/PLC-γ1 signalling pathway.

scholarly journals Meprin A impairs epithelial barrier function, enhances monocyte migration, and cleaves the tight junction protein occludin

2013 ◽  
Vol 305 (5) ◽  
pp. F714-F726 ◽  
Author(s):  
Jialing Bao ◽  
Renee E. Yura ◽  
Gail L. Matters ◽  
S. Gaylen Bradley ◽  
Pan Shi ◽  
...  
Keyword(s):  
Tight Junction ◽  
Barrier Function ◽  
Fluorescein Isothiocyanate ◽  
Tight Junction Protein ◽  
Sodium Fluorescein ◽  
Monocyte Migration ◽  
Junction Protein ◽  
Epithelial Barriers

Meprin metalloproteases are highly expressed at the luminal interface of the intestine and kidney and in certain leukocytes. Meprins cleave a variety of substrates in vitro, including extracellular matrix proteins, adherens junction proteins, and cytokines, and have been implicated in a number of inflammatory diseases. The linkage between results in vitro and pathogenesis, however, has not been elucidated. The present study aimed to determine whether meprins are determinative factors in disrupting the barrier function of the epithelium. Active meprin A or meprin B applied to Madin-Darby canine kidney (MDCK) cell monolayers increased permeability to fluorescein isothiocyanate-dextran and disrupted immunostaining of the tight junction protein occludin but not claudin-4. Meprin A, but not meprin B, cleaved occludin in MDCK monolayers. Experiments with recombinant occludin demonstrated that meprin A cleaves the protein between Gly100 and Ser101 on the first extracellular loop. In vivo experiments demonstrated that meprin A infused into the mouse bladder increased the epithelium permeability to sodium fluorescein. Furthermore, monocytes from meprin knockout mice on a C57BL/6 background were less able to migrate through an MDCK monolayer than monocytes from their wild-type counterparts. These results demonstrate the capability of meprin A to disrupt epithelial barriers and implicate occludin as one of the important targets of meprin A that may modulate inflammation.

Changes in tight junction protein expression in intrinsic aging and photoaging in human skin in vivo

2016 ◽  
Vol 84 (1) ◽  
pp. 99-101 ◽  
Author(s):  
Seon-Pil Jin ◽  
Sang Bum Han ◽  
Yeon Kyung Kim ◽  
Elizabeth Eunkyung Park ◽  
Eun Jin Doh ◽  
...  
Keyword(s):  
Protein Expression ◽  
Tight Junction ◽  
Human Skin ◽  
Tight Junction Protein ◽  
Tight Junction Protein Expression ◽  
Junction Protein

scholarly journals Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo

Reproduction ◽  
2008 ◽  
Vol 135 (6) ◽  
pp. 867-877 ◽  
Author(s):  
Gerard A Tarulli ◽  
Sarah J Meachem ◽  
Stefan Schlatt ◽  
Peter G Stanton
Keyword(s):  
Tight Junction ◽  
Adaptor Protein ◽  
Tight Junction Protein ◽  
Mrna Levels ◽  
Tight Junction Proteins ◽  
Djungarian Hamster ◽  
Junction Protein ◽  
Protein Localisation ◽  
Junction Proteins

This study aimed to assess the effect of gonadotrophin suppression and FSH replacement on testicular tight junction dynamics and blood–testis barrier (BTB) organisation in vivo, utilising the seasonal breeding Djungarian hamster. Confocal immunohistology was used to assess the cellular organisation of tight junction proteins and real-time PCR to quantify tight junction mRNA. The effect of tight junction protein organisation on the BTB permeability was also investigated using a biotin-linked tracer. Tight junction protein (claudin-3, junctional adhesion molecule (JAM)-A and occludin) localisation was present but disorganised after gonadotrophin suppression, while mRNA levels (claudin-11, claudin-3 and occludin) were significantly (two- to threefold) increased. By contrast, both protein localisation and mRNA levels for the adaptor protein zona occludens-1 decreased after gonadotrophin suppression. FSH replacement induced a rapid reorganisation of tight junction protein localisation. The functionality of the BTB (as inferred by biotin tracer permeation) was found to be strongly associated with the organisation and localisation of claudin-11. Surprisingly, JAM-A was also recognised on spermatogonia, suggesting an additional novel role for this protein in trans-epithelial migration of germ cells across the BTB. It is concluded that gonadotrophin regulation of tight junction proteins forming the BTB occurs primarily at the level of protein organisation and not gene transcription in this species, and that immunolocalisation of the organised tight junction protein claudin-11 correlates with BTB functionality.

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