Adhesion complexes implicated in intestinal epithelial cell-matrix interactions

Stutzmann, J; Bellissent‐Waydelich, Anne; Fontao, Lionel; Launay, Jean-François; Simon‐Assmann, Patricia

doi:10.1002/1097-0029(20001015)51:2<179::aid-jemt9>3.0.co;2-4

Cited by 40 publications

(23 citation statements)

References 98 publications

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“…The 67LR has been shown to be coregulated and to associate physically with ␣6␤4 integrin in A431 cells, where it acts as an auxiliary molecule involved in regulating or stabilizing the interaction of laminin with the integrin (1). The integrin ␣6␤4 is the principal agent for accomplishing integration of the cytoskeleton with laminin in the extracellular matrix (51), and changes in its expression or ligand affinity lead to extensive blistering or exfoliation (45). HPE-induced dome formation is associated with dramatic changes in the pattern of expression of ␣6, ␤4, and ␤1 integrins, as well as the 67LR.…”

Section: Discussionmentioning

confidence: 99%

“…The enterocytes perform the barrier function by maintaining their polarity and tightly associating with each other through lateral adherents and tight junctions (35,59). These cells also maintain a stable connection to basement membranes through adhesive interactions between the cells and extracellular matrix proteins (51), and the principal agent mediating the integration of the cytoskeleton and extracellular matrix is the integrin heterodimer ␣6␤4 (16,51).…”

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confidence: 99%

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Soluble Extracts fromHelicobacter pyloriInduce Dome Formation in Polarized Intestinal Epithelial Monolayers in a Laminin-Dependent Manner

et al. 2003

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Helicobacter pylori colonizes the stomach at the interface between the mucus layer and the apical pole of gastric epithelial cells. A number of secreted and shed products from the bacteria, such as proteins and lipopolysaccharide, are likely to have a role in the pathogenesis at the epithelial level. To determine the physiological response of transporting polarized epithelia to released soluble factors from the bacterium, we used the T84 cell line. Monolayers of T84 cells were exposed to soluble extracts from H. pylori. The extracts induced rapid "dome" formation as well as an immediate decrease in transepithelial electrical resistance. Domes are fluid-filled blister-like structures unique to polarized epithelia. Their formation has been linked to sodium-transporting events as well as to diminished adherence of the cells to the substrate. H. pylori-induced dome formation in T84 monolayers was exacerbated by amiloride and inhibited by ouabain. Furthermore, it was associated with changes in the expression of the laminin binding ␣6␤4 integrin and the 67-kDa laminin receptor. Domes formed primarily on laminin-coated filters, rather than on fibronectin or collagen matrices, and their formation was inhibited by preincubating the bacterial extract with soluble laminin. This effect was specific to H. pylori and independent of the urease, vacA, cagA, and Lewis phenotype of the strains. These data indicate that released elements from H. pylori can alter the physiological balance and integrity of the epithelium in the absence of an underlying immune response.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Soluble Extracts fromHelicobacter pyloriInduce Dome Formation in Polarized Intestinal Epithelial Monolayers in a Laminin-Dependent Manner

et al. 2003

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“…Most of integrin ␣ and ␤ subunits have short cytoplasmic segments that serve as a site for the assembly of multimeric signaling complexes and actin-binding proteins, by which integrins interact with actin filaments. The ␤ 1 subunit is abundantly expressed in intestinal epithelial cells (9,44), localized at the leading edge of migrating T84 cells (Fig. 4), and, according to Ab-blocking experiments, is critically involved in T84 cell migration (45).…”

Section: Ifn-␥ Alters Intracellular Trafficking Pathway For ␤ 1 Integrinmentioning

confidence: 99%

Interferon-γ Inhibits T84 Epithelial Cell Migration by Redirecting Transcytosis of β1 Integrin from the Migrating Leading Edge

Qiao

Vassilieva

Ivanov

et al. 2005

The Journal of Immunology

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Intestinal inflammation is associated with epithelial damage and formation of mucosal wounds. Epithelial cells migration is required for wound closure. In inflammatory status, migrating epithelial cells are exposed to proinflammatory cytokines such as IFN-γ. However, influence of such cytokines on intestinal epithelial wound closure remains unknown. The present study was designed to investigate the effect of IFN-γ on migration of model T84 intestinal epithelial cells and recovery of epithelial wounds. IFN-γ significantly inhibited rate of T84 cell migration and closure of epithelial wounds. This effect was accompanied by the formation of large aberrant lamellipodia at the leading edge as well as significant decrease in the number of β1 integrin containing focal adhesions. IFN-γ exposure increased endocytosis of β1 integrin and shifted its accumulation from early/recycling endosomes at the leading edge to a yet unidentified compartment at the cell base. This redirection in β1 integrin transcytosis was inhibited by depolymerization of microtubules with nocodazole and was unaffected by stabilization of microtubules with docetaxel. These results suggest that IFN-γ attenuates epithelial wound closure by microtubule-dependent redirection of β1 integrin transcytosis from the leading edge of migrating cells thereby inhibiting adequate turnover of focal adhesion complexes and cell migration.

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“…Differentiated epithelial cells on villi in the small intestine (enterocytes) are the main targets of infection, leading to cell death, a reduction in villus epithelium area, loss of absorptive capacity, and osmotic dysregulation (3,7,48,53). Enterocytes are attached to the basement membrane through interactions between the basement matrix and cell-surface adhesion molecules, mainly members of the integrin family (4,6,49,64). Increased enterocyte loss is a feature of rotavirus disease, suggesting that reduced enterocyte adhesion occurs (9).…”

Section: Blockade Of Integrin Regulation By Pi3k Inhibition Led To Dementioning

confidence: 99%

Rotavirus Replication in Intestinal Cells Differentially Regulates Integrin Expression by a Phosphatidylinositol 3-Kinase-Dependent Pathway, Resulting in Increased Cell Adhesion and Virus Yield

Halász

Holloway

Turner

et al. 2008

J Virol

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Changes in the interactions between intestinal cells and their surrounding environment during virus infection have not been well documented. The growth and survival of intestinal epithelial cells, the main targets of rotavirus infection, are largely dependent on the interaction of cell surface integrins with the extracellular matrix. In this study, we detected alterations in cellular integrin expression following rotavirus infection, identified the signaling components required, and analyzed the subsequent effects on cell binding to the matrix component collagen. After rotavirus infection of intestinal cells, expression of ␣2␤1 and ␤2 integrins was up-regulated, whereas that of ␣V␤3, ␣V␤5, and ␣5␤1 integrins, if present, was down-regulated. This differential regulation of integrins was reflected at the transcriptional level. It was unrelated to the use of integrins as rotavirus receptors, as both integrin-using and integrin-independent viruses induced integrin regulation. Using pharmacological agents that inhibit kinase activity, integrin regulation was shown to be dependent on phosphatidylinositol 3-kinase (PI3K) but independent of the activities of the mitogen-activated protein kinases p38 and ERK1/2, and cyclooxygenase-2. Replication-dependent activation of the PI3K/Akt pathway was observed following infection of intestinal and nonintestinal cell lines. Rotavirus activation of PI3K was important for regulation of ␣2␤1 expression. Blockade of integrin regulation by PI3K inhibition led to decreased adherence of infected intestinal cells to collagen and a concomitant decrease in virus titer. These findings indicate that rotavirus-induced PI3K activation causes regulation of integrin expression in intestinal cells, leading to prolonged adherence of infected cells to collagen and increased virus production.Rotavirus is a major cause of dehydrating gastroenteritis in infant humans and animals throughout the world. Differentiated epithelial cells on villi in the small intestine (enterocytes) are the main targets of infection, leading to cell death, a reduction in villus epithelium area, loss of absorptive capacity, and osmotic dysregulation (3,7,48,53). Enterocytes are attached to the basement membrane through interactions between the basement matrix and cell-surface adhesion molecules, mainly members of the integrin family (4,6,49,64). Increased enterocyte loss is a feature of rotavirus disease, suggesting that reduced enterocyte adhesion occurs (9). However, the molecules involved in changes in attachment of enterocytes to the matrix during rotavirus infection and how this process relates to viral replication and pathogenesis have not been analyzed.Integrins provide a means for cells to respond to their environment through intracellular signaling networks controlling crucial cellular processes such as adhesion, proliferation, migration, differentiation, and survival (1,20,38,55,69). These ␣␤ heterodimeric glycoproteins have been identified as cellular receptors or entry cofactors for many viruses, including rotavi...

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Adhesion complexes implicated in intestinal epithelial cell-matrix interactions

Cited by 40 publications

References 98 publications

Soluble Extracts fromHelicobacter pyloriInduce Dome Formation in Polarized Intestinal Epithelial Monolayers in a Laminin-Dependent Manner

Soluble Extracts fromHelicobacter pyloriInduce Dome Formation in Polarized Intestinal Epithelial Monolayers in a Laminin-Dependent Manner

Interferon-γ Inhibits T84 Epithelial Cell Migration by Redirecting Transcytosis of β1 Integrin from the Migrating Leading Edge

Rotavirus Replication in Intestinal Cells Differentially Regulates Integrin Expression by a Phosphatidylinositol 3-Kinase-Dependent Pathway, Resulting in Increased Cell Adhesion and Virus Yield

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