Regulation of proliferation of human colonic subepithelial myofibroblasts by mediators important in intestinal inflammation.

Jobson, T M; Billington, Charlotte K.; Hall, Irene

doi:10.1172/jci1876

Cited by 64 publications

(60 citation statements)

References 32 publications

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“…The various functions of intestinal SEMFs are regulated by a variety of cytokines and growth factors (18,20,24,31,36). For example, PDGF-BB, bFGF, and IGF-I stimulated the proliferation of intestinal SEMFs (20,31).…”

Section: Discussionmentioning

confidence: 99%

“…For example, PDGF-BB, bFGF, and IGF-I stimulated the proliferation of intestinal SEMFs (20,31). ECM secretion was induced by TGF-␤1 (31, Fig.…”

Section: Discussionmentioning

confidence: 99%

“…These cells are specialized mesenchymal cells that exhibit the ultrastructural features of both fibroblasts and smooth muscle cells and can be characterized by positive immunoreactivity for ␣-smooth muscle actin but negative immunoreactivity for desmin. These cells play a central role in the regulation of a number of epithelial cell functions, such as proliferation and differentiation and extracellular matrix (ECM) metabolism affecting the growth of the basement membrane (20,24,31,36). Recent studies from our laboratory (18) have suggested that SEMFs might play a role in the pathogenesis of intestinal inflammation via the secretion of proinflammatory cytokines, such as IL-6 and a variety of chemokines.…”

mentioning

confidence: 99%

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Regulation of IL-11 expression in intestinal myofibroblasts: role of c-Jun AP-1- and MAPK-dependent pathways

Bamba

Andoh

Yasui

et al. 2003

American Journal of Physiology-Gastrointestinal and Liver Physi

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IL-11 inhibits the activation of NF-κB and induces the Th2 polarization of CD4+ T cells. The clinical utility of IL-11 is being investigated in Crohn's disease. However, physiological secretion of IL-11 in the intestine remains unclear. In this study, we investigated IL-11 secretion in human intestinal subepithelial myofibroblasts (SEMFs). Intestinal SEMFs were isolated from the human colonic mucosa. IL-11 secretion and mRNA expression were determined by ELISA and Northern blot analysis. The activating protein (AP)-1-DNA binding activity was evaluated by EMSA. IL-11 secretion was induced by IL-1β and transforming growth factor (TGF)-β1. These were also observed at the mRNA level. The EMSAs demonstrated that both IL-1β and TGF-β1 induced AP-1 activation within 2 h after stimulation, and a blockade of AP-1 activation by the recombinant adenovirus containing a dominant negative c-Jun markedly reduced the IL-1β- and TGF-β1-induced IL-11 mRNA expression. IL-1β and TGF-β1 induced an activation of ERK p42/44 and p38 MAP kinases, and the MAP kinase inhibitors (SB-202190, PD-98059, and U-0216) significantly reduced the IL-1β- and TGF-β1-induced IL-11 secretion. The upregulation of IL-11 mRNA by IL-1β- and TGF-β1 was also mediated by a p38 MAP kinase-mediated mRNA stabilization. The combination of IL-1β and TGF-β1 additively enhanced IL-11 secretion. Intestinal SEMFs secreted IL-11 in response to IL-1β- and TGF-β1. Mucosal IL-11 secretion might be important as an anti-inflammatory response in the pathogenesis of intestinal inflammation.

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Section: Discussionmentioning

confidence: 99%

“…For example, PDGF-BB, bFGF, and IGF-I stimulated the proliferation of intestinal SEMFs (20,31). ECM secretion was induced by TGF-␤1 (31, Fig.…”

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Regulation of IL-11 expression in intestinal myofibroblasts: role of c-Jun AP-1- and MAPK-dependent pathways

Bamba

Andoh

Yasui

et al. 2003

American Journal of Physiology-Gastrointestinal and Liver Physi

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“…Cells were not used if viability did not exceed 90%. Phenotypical characterization of LPMCs was performed by FACScan flow cytometer (Becton Dickinson, UK) by using the following Primary cultures of myofibroblasts were obtained by following the method of Jobson et al 17 Briefly, samples of human adult normal jejunal mucosa harvested from three patients undergoing gastrectomy for carcinoma were separated from the underlying muscularis mucosae by microdissection. Mucosal strips were subsequently denuded of epithelial cells by treatment with 1-mmol/l ethylene diamine tetra-acetic acid and 1-mmol/l dithiothreitol (both from Sigma), and put on Dulbecco's-modified eagle whole growth medium containing 15% fetal calf serum, glutamine (2 mM), penicillin G (100 U/ml), streptomycin (100 mg/ml) and amphotericin-B (0.25 mg/ml).…”

Section: Cell Isolation Procedures and Functional Experimentsmentioning

confidence: 99%

Matrix metalloproteinase pattern in celiac duodenal mucosa

Ciccocioppo

Sabatino

Bauer

et al. 2005

Laboratory Investigation

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Matrix metalloproteinases (MMPs) are a family of endopeptidases playing a key role in tissue remodelling in both physiological and pathological conditions. Since little information is available about their role in celiac disease (CD), our aims were to quantify their expression/activity and to investigate their relation to proinflammatory cytokines in this condition. Duodenal biopsies from untreated, treated celiac patients and controls were used to quantify the expression of MMP-1, MMP-2, MMP-3, MMP-9, MMP-12, MMP-14, their inhibitor TIMP-1, IFN-c and TNF-a by using real-time reverse transcription-polymerase chain reaction and the gelatin/casein/elastin activities by gel zymography, and to isolate lamina propria mononuclear cells (LPMCs). These cells and myofibroblasts isolated from jejunal specimens were incubated in the absence or presence of IFN-c and TNF-a. MMP-1 and MMP-12 mRNA levels were significantly increased in active CD compared to treated (Po0.01 and Po0.0005, respectively) and normal mucosa (Po0.01 and Po0.0005, respectively), and this was paralleled by an upregulation of caseinolytic and elastolytic activities. Furthermore, MMP-12 levels significantly (Po0.05) correlated with those of IFN-c and the degree of villous flattening. MMP-2 turned out to be significantly (Po0.05) reduced in untreated and treated celiacs compared to controls. In active CD, transcripts of TIMP-1 were higher than in treated and controls (Po0.005 and Po0.05, respectively), such as those of IFN-c (Po0.05), whereas TNF-a levels were suppressed (P ¼ 0.0001). In physiological condition, myofibroblasts represent the main source of MMP-2, whereas LPMCs produce almost all MMPs only after cytokine stimulation. Conversely, cells isolated from active patients constitutively express MMPs without any increase after cytokine stimulation, while those from treated patients are in a resting condition. In conclusion, our results show the presence of a peculiar MMP pattern in active CD strongly dominated by MMP-12, correlating either with IFN-c or the degree of mucosal damage.

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“…Some show their beneficial features [39][40][41][42][43] and others cite harmful activities [44][45][46].…”

Section: Myofibroblasts Of the Intestinal Pericrypt Sheathmentioning

confidence: 99%

Histomorphometric study of role of lactoferrin in atrophy of the intestinal mucosa of rats

Caruso¹,

Demonte²,

Neves³

2012

Health

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The purpose of this work was to study the effects of oral administration of lactoferrin (Lf) in rats subjected to atrophy of the small intestine induced by a diet based on soy protein concentrate as the main protein source. We used 24 male Wistar rats aged 40 days, kept in individual cages under appropriate conditions of temperature, light and humidity. The animals were divided into four groups (n = 6); 1) group SL received soy-based food and, once a day, a supplement of 200mg/kg of Lf administered by gavage; 2) group Si received the soy feed without supplement of Lf; 3) group CL received a diet based on casein plus Lf; 4) group Ci received the casein diet without supplement of Lf. At the end of fifteen days, a 10 mm segment of the initial portion of the small intestine was sectioned and subjected to morphometry of the intestinal crypts and villi and assessment of the number and size of myofibroblasts. Comparison between groups showed that the length of the villi was similar in groups Ci and CL and higher in CL than in SL; SL than in Si, in Ci than in SL, and in Ci than in Si to Ci. The crypt depth was similar in SL and CL, SL and Ci and Ci and CL and was higher in Si than in Ci and in Si than in SL. The number of myofibroblasts was higher in SL than in CL, in SL than in Si, in CL than in Ci, and in SL than in and Ci; between Ci and Si there was no difference. The area of myofibroblasts was similar between the groups SL and CL and Si and Ci and higher in SL than in Si, and in Cl than in and Ci, and in SL than in Ci. All statistical analysis assumed significance when p < 0.05. From these results, we conclude that lactoferrin increases the number and size of the pericrypt myofibroblasts and stimulates rapidly the regeneration of atrophied villi.

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Regulation of proliferation of human colonic subepithelial myofibroblasts by mediators important in intestinal inflammation.

Cited by 64 publications

References 32 publications

Regulation of IL-11 expression in intestinal myofibroblasts: role of c-Jun AP-1- and MAPK-dependent pathways

Regulation of IL-11 expression in intestinal myofibroblasts: role of c-Jun AP-1- and MAPK-dependent pathways

Matrix metalloproteinase pattern in celiac duodenal mucosa

Histomorphometric study of role of lactoferrin in atrophy of the intestinal mucosa of rats

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