scholarly journals Synergistic Induction of Chicken Antimicrobial Host Defense Peptide Gene Expression by Butyrate and Sugars

2021 ◽  
Vol 12 ◽  
Author(s):  
Qing Yang ◽  
Li-An Fong ◽  
Wentao Lyu ◽  
Lakshmi T. Sunkara ◽  
Kan Xiao ◽  
...  
Keyword(s):  
Gene Expression ◽  
Disease Control ◽  
Host Defense ◽  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Control And Prevention ◽  
Host Defense Peptide ◽  
Peptide Gene

Antimicrobial resistance is a major concern to public health demanding effective alternative strategies to disease control and prevention. Modulation of endogenous host defense peptide (HDP) synthesis has emerged as a promising antibiotic alternative approach. This study investigated a potential synergy between sugars and butyrate in inducing HDP gene expression in chickens. Our results revealed that sugars differentially regulated HDP expression in both gene- and sugar-specific manners in chicken HD11 macrophage cells. Among eight mono- and disaccharides tested, all were potent inducers of avian β-defensin 9 (AvBD9) gene (p<0.05), but only galactose, trehalose, and lactose obviously upregulated cathelicidin-B1 (CATHB1) gene expression. The expression of AvBD14 gene, on the other hand, was minimally influenced by sugars. Moreover, all sugars exhibited a strong synergy with butyrate in enhancing AvBD9 expression, while only galactose, trehalose, and lactose were synergistic with butyrate in CATHB1 induction. No synergy in AvBD14 induction was observed between sugars and butyrate. Although lactose augmented the expression of nearly all HDP genes, its synergy with butyrate was only seen with several, but not all, HDP genes. Mucin-2 gene was also synergistically induced by a combination of lactose and butyrate. Furthermore, lactose synergized with butyrate to induce AvBD9 expression in chicken jejunal explants (p<0.05). Mechanistically, hyper-acetylation of histones was observed in response to both butyrate and lactose, relative to individual compounds. Mitogen-activated protein kinase, NF-κB, and cyclic adenosine monophosphate signaling pathways were also found to be involved in butyrate- and lactose-mediated synergy in AvBD9 induction. Collectively, a combination of butyrate and a sugar with both HDP-inducing and barrier protective activities holds the promise to be developed as an alternative to antibiotics for disease control and prevention.

scholarly journals Modulation of Antimicrobial Host Defense Peptide Gene Expression by Free Fatty Acids

PLoS ONE ◽  
2012 ◽  
Vol 7 (11) ◽  
pp. e49558 ◽  
Author(s):  
Lakshmi T. Sunkara ◽  
Weiyu Jiang ◽  
Guolong Zhang
Keyword(s):  
Gene Expression ◽  
Fatty Acids ◽  
Free Fatty Acids ◽  
Host Defense ◽  
Host Defense Peptide ◽  
Peptide Gene

Acquired Exchange Protein Directly Activated by Cyclic Adenosine Monophosphate Activity Induced by p38 Mitogen-activated Protein Kinase in Primary Afferent Neurons Contributes to Sustaining Postincisional Nociception

2017 ◽  
Vol 126 (1) ◽  
pp. 150-162 ◽  
Author(s):  
Megumi Matsuda ◽  
Kentaro Oh-hashi ◽  
Isao Yokota ◽  
Teiji Sawa ◽  
Fumimasa Amaya
Keyword(s):  
Dorsal Root Ganglion ◽  
Prostaglandin E2 ◽  
Dorsal Root ◽  
Tissue Injury ◽  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Dorsal Root Ganglion Neurons ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Ganglion Neurons

Abstract Background The molecular mechanisms responsible for sustained pain after tissue injury are largely unknown. The aim of this study was to clarify the role of exchange protein directly activated by cyclic adenosine monophosphate (EPAC) in sustained postincisional nociception, using tissue injury-induced nociceptor priming, and involvement of p38 mitogen-activated protein kinase (p38MAPK) in EPAC-mediated nociceptor priming. Methods Plantar incisions were made in the hind paws of Sprague–Dawley rats (n = 144). Nociceptor priming was confirmed by behavior testing followed by prostaglandin E2 injection 14 to 21 days after the incision. ESI-09, a selective EPAC inhibitor, was administered to assess its effects on nociceptor priming. Expression of two isoforms of EPAC (EPAC1/EPAC2) in dorsal root ganglions from naive rats and those 14 days after the incision was detected by immunohistochemistry and Western blotting. Separately, FR167653, a selective p38MAPK inhibitor, was administered to assess its effect on EPAC1/EPAC2 expression and the development of nociceptor priming. Results Prostaglandin E2 injection 14 to 21 days after the plantar incision induced persistent mechanical hyperalgesia for 7 days. EPAC1/EPAC2 expression in dorsal root ganglion neurons was trivial in naive rats (7.7 ± 4.8% for EPAC1; 6.3 ± 4.1% for EPAC2) but markedly increased 14 days after the incision (21.0 ± 9.4% and 20.1 ± 3.8%, respectively). ESI-09 treatment inhibited prostaglandin E2-induced persistent mechanical hypersensitivity but had no effect on incision-induced acute nociceptive hypersensitivity. Treatment with FR167653 before the incision inhibited the development of nociceptor priming and incision-induced EPAC1/EPAC2 expression (8.5 ± 5.4% and 7.6 ± 3.3%, respectively). Conclusions Transient inflammatory stimulation causes long-lasting nociceptive hypersensitivity via nociceptor priming during the subacute period after incision. Acquired EPAC activity by p38MAPK in the dorsal root ganglion neurons is a key for this event.

scholarly journals A Conserved p38 Mitogen-Activated Protein Kinase Pathway Regulates Drosophila Immunity Gene Expression

1998 ◽  
Vol 18 (6) ◽  
pp. 3527-3539 ◽  
Author(s):  
Zhiqiang Stanley Han ◽  
Hervé Enslen ◽  
Xiaodi Hu ◽  
Xiangjun Meng ◽  
I-Huan Wu ◽  
...  
Keyword(s):  
Gene Expression ◽  
Immune Response ◽  
Map Kinase ◽  
Map Kinases ◽  
P38 Map Kinase ◽  
Insect Immunity ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Peptide Gene ◽  
Kinase Pathway

ABSTRACT Accumulating evidence suggests that the insect and mammalian innate immune response is mediated by homologous regulatory components. Proinflammatory cytokines and bacterial lipopolysaccharide stimulate mammalian immunity by activating transcription factors such as NF-κB and AP-1. One of the responses evoked by these stimuli is the initiation of a kinase cascade that leads to the phosphorylation of p38 mitogen-activated protein (MAP) kinase on Thr and Tyr within the motif Thr-Gly-Tyr, which is located within subdomain VIII. We have investigated the possible involvement of the p38 MAP kinase pathway in the Drosophila immune response. Two genes that are highly homologous to the mammalian p38 MAP kinase were molecularly cloned and characterized. Furthermore, genes that encode two novelDrosophila MAP kinase kinases, D-MKK3 and D-MKK4, were identified. D-MKK3 is an efficient activator of bothDrosophila p38 MAP kinases, while D-MKK4 is an activator of D-JNK but not D-p38. These data establish that Drosophilaindeed possesses a conserved p38 MAP kinase signaling pathway. We have examined the role of the D-p38 MAP kinases in the regulation of insect immunity. The results revealed that one of the functions of D-p38 is to attenuate antimicrobial peptide gene expression following exposure to lipopolysaccharide.

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