Regulation of the Type II Hemidesmosomal Plaque Assembly in Intestinal Epithelial Cells

Fontao, Lionel; Stutzmann, J; Gendry, Patrick; Launay, Jean-François

doi:10.1006/excr.1999.4549

Cited by 27 publications

(21 citation statements)

References 60 publications

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“…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%

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

et al. 2003

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“…Integrin α6β4 is a major component of both the type I and II hemidesmosome structures [30, 31]. Type I are found in stratified and pseudostratified epithelia such as the skin, while type II are found in simple epithelia such as the uroepithelial layers [32–34]. There are reports of junctional epidermolysis bullosa patients with either α6 or β4 mutations that have a dilated renal pelvis and hydronephrosis[16, 23–25], features similar to those seen in the aged mice.…”

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confidence: 99%

Integrin alpha6 maintains the structural integrity of the kidney collecting system

Viquez

Yazlovitskaya

et al. 2017

Matrix Biology

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Laminins are a major constituent of the basement membranes of the kidney collecting system. Integrins, transmembrane receptors formed by non-covalently bound α and β subunits, serve as laminin receptors, but their role in development and homeostasis of the kidney collecting system are poorly defined. Integrin α3β1, one of the major laminin receptors, plays a minor role in kidney collecting system development, while the role of α6 containing integrins (α6β1 and α6β4), the other major laminin receptors, is unknown. Patients with mutations in α6 containing integrins not only develop epidermolysis bullosa, but also have abnormalities in the kidney collecting system. In this study, we show that selectively deleting the α6 or β4 integrin subunits at the initiation of ureteric bud development in mice does not affect morphogenesis. However, the collecting system becomes dilated and dysmorphic as the mice age. The collecting system in both null genotypes were also highly susceptible to unilateral ureteric obstruction injury with evidence of excessive tubule dilatation and epithelial cell apoptosis. Mechanistically, integrin α6-null collecting duct cells are unable to withstand high mechanical force when adhered to laminin. Thus, we conclude that α6 integrins are important for maintaining the integrity of the kidney collecting system by enhancing tight adhesion of the epithelial cells to the basement membrane. These data give a mechanistic explanation for the association between kidney collecting system abnormalities in patients and epidermolysis bullosa.

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“…These fragments retain the ability to bind ␣6 integrin, resulting in altered ␣6␤4 dimers that participate in the formation of both altered type I HDs and altered type II HDs (47) (Figures 5A and B). Concomitantly, ADAM-17 degrades BP180, thus generating LAD-1 (120 kd), which no longer binds to ␣6 integrin.…”

Section: Discussionmentioning

confidence: 99%

Alterations in type I hemidesmosome components suggestive of epigenetic control in the salivary glands of patients with Sjögren's syndrome

González

Aguilera

Alliende

et al. 2011

Arthritis & Rheumatism

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Objective. Acinar cells in the salivary glands of patients with Sjögren's syndrome (SS) display severe alterations in anchorage to the basal lamina. Bioinformatics analysis of the BP230 gene sequence has revealed the presence of CpG islands that might be involved in epigenetic control of gene expression, and methylation of the BP230 promotor region may be implicated as an epigenetic control mechanism in salivary gland damage. Thus, the present study was undertaken to evaluate the protein BP230, as well as proteins BP180, ␣6␤4 integrin, and cytokeratin-18, for their expression levels, localization, and ability to form hemidesmosome adhesion complexes.Methods. Eighteen patients with primary SS and 14 healthy control subjects were studied. Levels of messenger RNA (mRNA) and protein were measured by reverse transcription-polymerase chain reaction and Western blotting, respectively. BP230 methylation was determined by methylation-sensitive polymerase chain reaction. Protein complexes were analyzed by immunoprecipitation and assessed for localization by immunofluorescence.Results. In patients with SS as compared with controls, BP230 mRNA levels were decreased while protein levels were increased, and the gene promotor region was hypermethylated. Augmented proteolysis of BP180 was detected, since levels of linear IgA disease fragment 1 were increased. The complex-forming ability of BP230, BP180, ␣6␤4 integrin, and cytokeratin-18 was maintained in patients with SS, in contrast to that in controls. BP230 and BP180 colocalized at the basal membrane of acinar cells, and cleavage of BP180 coincided with a loss of colocalization.Conclusion. The decrease in BP230 mRNA levels may be explained by gene hypermethylation. We postulate that local epigenetic modifications of BP230 are produced in response to factors present in the damaged salivary glands of patients with SS. Additionally, the paradoxical increase in BP230 protein levels and the formation of both normal and altered adhesion complexes may help avoid cell death induced by the loss of anchorage.Severe alterations in acinar cells and the extracellular matrix (ECM) are recurrent observations in the labial salivary glands (LSGs) of patients with primary Sjögren's syndrome (SS) (1-4). LSG epithelial cells are linked to the basal lamina (BL) through several transmembrane protein complexes that have important functions in adhesion and cell signaling (5). These adhesion complexes include ␣6␤1 and ␣6␤4 integrins as a central

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Regulation of the Type II Hemidesmosomal Plaque Assembly in Intestinal Epithelial Cells

Cited by 27 publications

References 60 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

Integrin alpha6 maintains the structural integrity of the kidney collecting system

Alterations in type I hemidesmosome components suggestive of epigenetic control in the salivary glands of patients with Sjögren's syndrome

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