Nuclear Factor-κB Is a Critical Mediator of Ste20-Like Proline-/Alanine-Rich Kinase Regulation in Intestinal Inflammation

Yan, Yutao; Dalmasso, Guillaume; Nguyen, Hang Thi Thu; Obertone, Tracy S.; Charrier-Hisamuddin, Laetitia; Sitaraman, Shanthi V.; Merlin, Didier

doi:10.2353/ajpath.2008.080339

Cited by 39 publications

(44 citation statements)

References 77 publications

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“…Furthermore, mutation of the NF-κB element itself resulted in a 50% decrease of the TNF-α stimulated luciferase signal, indicating that the element is involved in the increased transcription of SPAK observed under inflammation. These studies confirmed increased expression of NF-κB and its translocation to the nucleus, alongside with increased SPAK mRNA and protein levels in mice treated with dextran sodium sulfate to induce colitis (320). …”

Section: Physiological Roles Of Spak and Osr1 In Mammalian Systemsmentioning

confidence: 54%

“…As pro-inflammatory cytokines also lead to activation of p38, Merlin and coworkers examined SPAK mRNA expression in Caco2-BBE cells exposed to IFN-γ, TGF-β, and TNF-α treatment. They showed a 2.5-fold increased SPAK mRNA expression with interferon (323) and TNF-α (320). Note that the precise signaling pathway modulated by SPAK is likely cell-specific, as in hematopoietic cells, SPAK interacts with the TNF receptor RELT (Receptor Expressed in Lymphoid Tissues), leading to activation of both p38 and JNK signaling (228).…”

Section: Physiological Roles Of Spak and Osr1 In Mammalian Systemsmentioning

confidence: 99%

“…Note that the precise signaling pathway modulated by SPAK is likely cell-specific, as in hematopoietic cells, SPAK interacts with the TNF receptor RELT (Receptor Expressed in Lymphoid Tissues), leading to activation of both p38 and JNK signaling (228). Transcriptional activation of SPAK in intestinal cells by TGF-β has been linked to the presence of a NF-κB element located some 350 bp upstream of the transcription initiation site (320). Using a luciferase reporter gene assay with a portion of the 5’ region of SPAK, the authors observed stimulation by TNFα.…”

Section: Physiological Roles Of Spak and Osr1 In Mammalian Systemsmentioning

confidence: 99%

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Molecular Physiology of SPAK and OSR1: Two Ste20-Related Protein Kinases Regulating Ion Transport

Gagnon

Delpire

2012

Physiological Reviews

116

108

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SPAK (Ste20-related proline alanine rich kinase) and OSR1 (oxidative stress responsive kinase) are members of the germinal center kinase VI sub-family of the mammalian Ste20 (Sterile20)-related protein kinase family. Although there are 30 enzymes in this protein kinase family, their conservation across the fungi, plant and animal kingdom confirms their evolutionary importance. Already, a large volume of work has accumulated on the tissue distribution, binding partners, signaling cascades, and physiological roles of mammalian SPAK and OSR1 in multiple organ systems. After reviewing this basic information, we will examine newer studies that demonstrate the pathophysiological consequences to SPAK and/or OSR1 disruption, discuss the development and analysis of genetically-engineered mouse models, and address the possible role these serine/threonine kinases might have in cancer proliferation and migration.

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Section: Physiological Roles Of Spak and Osr1 In Mammalian Systemsmentioning

confidence: 54%

Section: Physiological Roles Of Spak and Osr1 In Mammalian Systemsmentioning

confidence: 99%

Section: Physiological Roles Of Spak and Osr1 In Mammalian Systemsmentioning

confidence: 99%

See 1 more Smart Citation

Molecular Physiology of SPAK and OSR1: Two Ste20-Related Protein Kinases Regulating Ion Transport

Gagnon

Delpire

2012

Physiological Reviews

116

108

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“…Based on recent studies, the pathogenesis of IBD seems to involve a complex interplay between certain genetic, environmental, and immunological factors. In particular, an unbalanced activation of the mucosal immune system driven by the commensal flora in a genetically susceptible host appears to cause intestinal inflammation in IBD patients [1][2][3][4][5][6]. The activation of the mucosal immune system is characterized by production of proinflammatory cytokines [7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Effects of Trefoil Peptide 3 on Expression of TNF-α, TLR4, and NF-κB in Trinitrobenzene Sulphonic Acid Induced Colitis Mice

Zhou

et al. 2009

Inflammation

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The trefoil factor (TFF) peptides are major secretory products of mucus cells of the gastrointestinal tract. There were evidences that administration of recombinant human TFF3 is effective in treatment of models of colitis, but the mechanism of the effects of rTFF3 is not fully understood. The main aims of this study is to evaluate effects of intraperitoneal injection recombinant human TFF3 on the expression of tumour necrosis factor alpha (TNF-alpha), toll-like receptor 4(TLR4), and nuclear factor kappaB (NF-kappaB) in trinitrobenzene sulphonic acid (TNBS) induced colitis mice. Distal colitis was induced in BALB/C mice by intracolonic administration of TNBS in ethanol. Treated with administration rhTFF3 for treatment group(5 mg/ml; approximately 0.5 mg/mouse), and normal saline for control for 5 consecutive days. Colonic damage score, tissue myeloperoxidase (MPO) activity, TLR4, NF-kappaB mRNA expression, and tissue TNF-alpha, TLR4, NF-kappaB production were determined, respectively. Once daily application of hTFF3 for 5 days after TNBS/ethanol had been injected, both microscopic and macroscopic injury and inflammatory index had been reduced compared with controls. In addition, decreased tissue TNF-alpha, TLR4, NF-kappaB production, and TLR4, NF-kappaB mRNA expression had been found. This study has shown that hTFF3 may have therapeutic potential in the treatment of inflammatory bowel disease, and one of the mechanisms may related to inhibit the TLR4/NF-kappaB signaling pathways.

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“…lactis BI07-HT29 cell early interaction. TNF-␣ was selected because this cytokine has been reported to play a central role in intestinal inflammation (18,40).…”

mentioning

confidence: 99%

Tumor Necrosis Factor Alpha Modulates the Dynamics of the Plasminogen-Mediated Early Interaction between Bifidobacterium animalis subsp. lactis and Human Enterocytes

Centanni

Bergmann

Turroni

et al. 2012

Appl Environ Microbiol

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The capacity to intervene with the host plasminogen system has recently been considered an important component in the interaction process between Bifidobacterium animalis subsp. lactis and the human host. However, its significance in the bifidobacterial microecology within the human gastrointestinal tract is still an open question. Here we demonstrate that human plasminogen favors the B. animalis subsp. lactis BI07 adhesion to HT29 cells. Prompting the HT29 cell capacity to activate plasminogen, tumor necrosis factor alpha (TNF-␣) modulated the plasminogen-mediated bacterium-enterocyte interaction, reducing the bacterial adhesion to the enterocytes and enhancing migration to the luminal compartment.

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Nuclear Factor-κB Is a Critical Mediator of Ste20-Like Proline-/Alanine-Rich Kinase Regulation in Intestinal Inflammation

Abstract: Inflammatory bowel disease (IBD) is thought to result

Cited by 39 publications

References 77 publications

Molecular Physiology of SPAK and OSR1: Two Ste20-Related Protein Kinases Regulating Ion Transport

Molecular Physiology of SPAK and OSR1: Two Ste20-Related Protein Kinases Regulating Ion Transport

Effects of Trefoil Peptide 3 on Expression of TNF-α, TLR4, and NF-κB in Trinitrobenzene Sulphonic Acid Induced Colitis Mice

Tumor Necrosis Factor Alpha Modulates the Dynamics of the Plasminogen-Mediated Early Interaction between Bifidobacterium animalis subsp. lactis and Human Enterocytes

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