Butyrate modulates inflammatory cytokines and tight junctions components along the gut of weaned pigs

Abstract Two experiments were conducted to determine the effects of protease supplementation on degradation of soybean meal (SBM) allergenic proteins (glycinin and β-conglycinin) and gut health of weaned pigs fed soybean meal-based diets. In experiment 1, 2 SBM samples from 2 different sources were subjected to porcine in vitro gastric degradation to determine the effects of protease (at 15,000 U/kg of feedstuff) on degradation of the soybean allergenic proteins. In experiment 2, 48 weaned pigs (body weight = 6.66 kg) were obtained in 2 batches of 24 pigs each. Pigs were individually housed in metabolic crates and fed 4 diets (12 pigs/diet). The diets were corn-based diet with SBM 1 or SBM 2 without or with protease at 15,000 U/kg of diet in 2 × 2 factorial arrangement. Diets were fed for 10 d and pigs were sacrificed on day 10 for measurement of small intestinal histomorphology, permeability of small intestine mounted in Ussing chambers, and serum concentration of pro-inflammatory cytokines. Two SBM sources (SBM 1 and SBM 2) contained 46.9% or 47.7% CP, 14.0% or 14.6% glycinin, and 9.90% or 10.3% β-conglycinin, respectively. Protease and SBM source did not interact on any of the response criteria measured in the current study. Protease supplementation tended to increase (P = 0.069) the in vitro gastric degradation of glycinin. Protease supplementation tended to reduce (P = 0.099) fluorescein isothiocyanate dextran 4,000 Da (which is a marker probe for intestinal permeability) flow in jejunum, and reduced (P = 0.037) serum TNF-α concentration. Protease did not affect small intestinal histomorphology. In conclusion, protease tended to increase gastric degradation of glycinin and reduce gut permeability, and serum concentration of pro-inflammatory cytokines, indicating that the protease used in the current study can be added to SBM-based diets for weanling pigs to improve gut health.

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Protective effects of baicalin on LPS-induced injury in intestinal epithelial cells and intercellular tight junctions

Canadian Journal of Physiology and Pharmacology ◽

10.1139/cjpp-2014-0262 ◽

2015 ◽

Vol 93 (4) ◽

pp. 233-237 ◽

Cited By ~ 24

Author(s):

Jian Chen ◽

Ren Zhang ◽

Jian Wang ◽

Peng Yu ◽

Quan Liu ◽

...

Keyword(s):

Epithelial Cells ◽

Protein Expression ◽

Tight Junctions ◽

Inflammatory Cytokines ◽

Intestinal Epithelial Cells ◽

Expression Level ◽

Protective Effects ◽

Intestinal Epithelial ◽

Tnf Α ◽

Mrna And Protein Expression

Aims: To investigate the protective effects and mechanisms of baicalin on lipopolysaccharide (LPS)-induced injury in intestinal epithelial cells and intercellular tight junctions. Methods: IEC-6 cells were stimulated with LPS (1.0 μg/mL), with or without baicalin, for 24 h. The levels of the inflammatory cytokines interleukin (IL)-6 and tumor necrosis factor (TNF)-α were determined using ELISA. Quantitative real-time PCR was used for determining the mRNA expression level of claudin-3, occludin, and ZO-1; Western blot and immunofluorescence analysis were used for analyzing the expression level and the distribution patterns of ZO-1 protein. Results: Pretreatment with baicalin (10.0 μg/mL) improved LPS-stimulated cell viability and repressed IL-6 and TNF-α levels. In addition, pretreatment with baicalin up-regulated mRNA and protein expression levels of ZO-1 and kept the protein intact in IEC-6 cells injured with LPS. Conclusion: Baicalin has the capacity to protect IEC-6 cells and the intercellular tight junctions from LPS-induced injury. The mechanisms may be associated with inhibiting the production of inflammatory cytokines, and up-regulating the mRNA and protein expression of ZO-1.

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PSV-20 Effects of fortified yeast cell wall extract on growth and health of newly weaned pigs under chronic dietary challenges of aflatoxin and deoxynivalenol

Journal of Animal Science ◽

10.1093/jas/skz122.349 ◽

2019 ◽

Vol 97 (Supplement_2) ◽

pp. 198-199

Author(s):

Debora Muratori Holanda ◽

Alexandros Yiannikouris ◽

Sung Woo Kim

Keyword(s):

Cell Wall ◽

Oxidative Damage ◽

Yeast Cell ◽

Growth Performance ◽

Inflammatory Cytokines ◽

Hepatic Function ◽

Weaned Pigs ◽

Mucosal Tissues ◽

Cell Wall Extract ◽

Pro Inflammatory Cytokines

Abstract Pigs are highly susceptible to both aflatoxin and deoxynivalenol. The study aim at investigating the effects of a fortified yeast cell wall extract (YCW-DTX; Mycosorb D+, Alltech, Lexington, KY) on growth and health of newly weaned pigs under chronic dietary challenges of aflatoxin and deoxynivalenol. Forty-eight newly weaned pigs (21 d old) were individually housed and allotted to 4 dietary treatments in a randomized complete block design (sex; initial BW) with 2 factors for 35 d based on 3 phases. Two factors were mycotoxins (deoxynivalenol: 0 or 2 mg/kg during all phases and aflatoxin: 0 or 0.2 mg/kg during phase 3) and YCW-DTX (0 or 0.2%). On d 35, all pigs were euthanized to collect mucosal tissues from the jejunum to measure pro-inflammatory cytokines (TNF-a and IL-8) and oxidative damage markers (malondialdehydes and protein carbonyls). Data were analyzed using MIXED procedure of SAS. Mycotoxins reduced (P < 0.05) ADFI and ADG during the entire period whereas YCW-DTX did not affect growth performance of pigs. Mycotoxins reduced (P < 0.05) serum albumin, creatinine, ALT, and total protein concentrations whereas YCW-DTX increased (P < 0.05) glucose, decreased (P < 0.05) CPK, and tended to decrease AST (P = 0.051) and BUN/creatinine (P = 0.087) in serum. Neither mycotoxins nor YCW-DTX affected pro-inflammatory cytokines and oxidative damage markers in jejunal mucosal tissues. In conclusion, mycotoxins impaired growth performance and hepatic function of newly weaned pigs. The commercial additive partly improved hepatic function and maintained growth performance.

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Effects of dietary xylooligosaccharide on growth, digestive enzymes activity, intestinal morphology, and the expression of inflammatory cytokines and tight junctions genes in triploid Oncorhynchus mykiss fed a low fishmeal diet

Aquaculture Reports ◽

10.1016/j.aqrep.2021.100941 ◽

2022 ◽

Vol 22 ◽

pp. 100941

Author(s):

Chang’an Wang ◽

Zhe Xu ◽

Shaoxia Lu ◽

Haibo Jiang ◽

Jinnan Li ◽

...

Keyword(s):

Oncorhynchus Mykiss ◽

Tight Junctions ◽

Inflammatory Cytokines ◽

Digestive Enzymes ◽

Intestinal Morphology ◽

Enzymes Activity

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Freeze-etch observations on the tight junctions of sertoli cells grown in organ culture with FSH

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010008256x ◽

1978 ◽

Vol 36 (2) ◽

pp. 340-341

Author(s):

Rita Meyer ◽

Zoltan Posalaky ◽

Dennis Mcginley

Keyword(s):

Organ Culture ◽

Tight Junctions ◽

Sertoli Cell ◽

Germ Cells ◽

Sertoli Cells ◽

Barrier Function ◽

Cell Junction ◽

Intramembranous Particles ◽

Junctional Complexes ◽

Oriented Parallel

The Sertoli cell tight junctional complexes have been shown to be the most important structural counterpart of the physiological blood-testis barrier. In freeze etch replicas they consist of extensive rows of intramembranous particles which are not only oriented parallel to one another, but to the myoid layer as well. Thus the occluding complex has both an internal and an overall orientation. However, this overall orientation to the myoid layer does not seem to be necessary to its barrier function. The 20 day old rat has extensive parallel tight junctions which are not oriented with respect to the myoid layer, and yet they are inpenetrable by lanthanum. The mechanism(s) for the control of Sertoli cell junction development and orientation has not been established, although such factors as the presence or absence of germ cells, and/or hormones, especially FSH have been implicated.

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Cytokine synergy, collagenases and cartilage collagen breakdown

Biochemical Society Symposium ◽

10.1042/bss0700125 ◽

2003 ◽

Vol 70 ◽

pp. 125-133 ◽

Cited By ~ 7

Author(s):

Tim E. Cawston ◽

Jenny M. Milner ◽

Jon B. Catterall ◽

Andrew D. Rowan

Keyword(s):

Matrix Metalloproteinases ◽

Inflammatory Cytokines ◽

Activator Protein 1 ◽

Activator Protein ◽

And Cartilage ◽

Pro Inflammatory Cytokines

We have investigated proteinases that degrade cartilage collagen. We show that pro-inflammatory cytokines act synergistically with oncastatin M to promote cartilage collagen resorption by the up-regulation and activation of matrix metalloproteinases (MMPs). The precise mechanisms are not known, but involve the up-regulation of c-fos, which binds to MMP promoters at a proximal activator protein-1 (AP-1) site. This markedly up-regulates transcription and leads to higher levels of active MMP proteins.

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