Effect of hepatocyte growth factor on assembly of zonula occludens-1 protein at the plasma membrane

Grisendi, Silvia; Arpin, Monique; Crepaldi, Tiziana

doi:10.1002/(sici)1097-4652(199809)176:3<465::aid-jcp3>3.0.co;2-m

Cited by 45 publications

(22 citation statements)

References 31 publications

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“…Alterations in the distribution of key TJ proteins have been reported in response to hepatocyte growth factor in renal epithelial cells (68) and IL-4/ IL-13 in lung epithelial cells, (69); however, we (unpublished results) and others did not observe any alterations in intestinal epithelial cells exposed to the same cytokines (17,34).…”

Section: Discussioncontrasting

confidence: 56%

Proinflammatory Cytokines Disrupt Epithelial Barrier Function by Apoptosis-Independent Mechanisms

Bruewer

Luegering

Kucharzik

et al. 2003

The Journal of Immunology

793

643

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It is well known that inflammatory conditions of the intestinal mucosa result in compromised barrier function. Inflammation is characterized by an influx into the mucosa of immune cells that influence epithelial function by releasing proinflammatory cytokines such as IFN-γ and TNF-α. Mucosal barrier function is regulated by the epithelial apical junctional complex (AJC) consisting of the tight junction and the adherens junction. Since the AJC regulates barrier function, we analyzed the influence of IFN-γ and TNF-α on its structure/function and determined the contribution of apoptosis to this process using a model intestinal epithelial cell line, T84, and IFN-γ and TNF-α. AJC structure/function was analyzed by confocal microscopy, biochemical analysis, and physiologic measurement of epithelial gate/fence function. Apoptosis was monitored by determining cytokeratin 18 cleavage and caspase-3 activation. IFN-γ induced time-dependent disruptions in epithelial gate function that were potentiated by coincubation with TNF-α. Tight junction fence function was somewhat disrupted. Cytokine treatment was associated with internalization of AJC transmembrane proteins, junction adhesion molecule 1, occludin, and claudin-1/4 with minimal effects on the cytoplasmic plaque protein zonula occludens 1. Detergent solubility profiles of junction adhesion molecule 1 and E-cadherin and their affiliation with “raft-like” membrane microdomains were modified by these cytokines. Inhibition of cytokine-induced apoptosis did not block induced permeability defects; further emphasizing their primary influence on the epithelial AJC structure and barrier function. Our findings for the first time clearly separate the proapoptotic effects of IFN-γ and TNF-α from their abilities to disrupt barrier function.

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Section: Discussioncontrasting

confidence: 56%

Proinflammatory Cytokines Disrupt Epithelial Barrier Function by Apoptosis-Independent Mechanisms

Bruewer

Luegering

Kucharzik

et al. 2003

The Journal of Immunology

793

643

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“…HGF/SF-induced cell scattering/motility in MDCK cells involves changes in cell-matrix interactions and disassembly of cell-cell junctions, with adherent junctions disassembled before the disruption of tight junctions (Grisendi et al, 1998;Kamei et al, 1999). Immunofluorescent localization of Ecadherin and ZO-1 indicated persistent E-cadherin at adherent junctions and ZO-1 at the tight junctions in MDCK 5aa cells compared with control cells after exposure to HGF/SF.…”

Section: Discussionmentioning

confidence: 94%

“…HGF/SF-induced disruption of cell-cell junction was inhibited in MDCK 5aa cells During cell scattering, the adherent and tight junctions are disrupted/dissociated, and the adherent junction protein Ecadherin and the tight junction protein ZO-1 are both translocated to the cytoplasm (Grisendi et al, 1998;Kamei et al, 1999). During HGF/SF-induced tubulogenesis, epithelial cell polarity is transiently lost and components of cell-cell junctional complexes, including E-cadherin and ZO-1, undergo profound rearrangements (Pollack et al, 1998).…”

Section: Construction Of Hb-egf Mutant Plasmid Constructsmentioning

confidence: 99%

Membrane-associated HB-EGF modulates HGF-induced cellular responses in MDCK cells

Singh

Tsukada

Zent

et al. 2004

Journal of Cell Science

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In MDCK cells, hepatocyte growth factor/scatter factor (HGF/SF) induces epithelial cell dissociation, scattering, migration, growth and formation of branched tubular structures. By contrast, these cells neither scatter nor form tubular structures in response to the epidermal growth factor (EGF) family of growth factors. Heparin-binding EGF-like growth factor (HB-EGF) is a member of the EGF family of growth factors and is synthesized as a membrane-associated precursor molecule (proHB-EGF). ProHB-EGF is proteolytically cleaved to release a soluble ligand (sHB-EGF) that activates the EGF receptor. Although recent studies suggest possible physiological functions, the role of proHB-EGF remains largely undefined. Using MDCK cells stably expressing proHB-EGF, a noncleavable deletion mutant of proHB-EGF or soluble HB-EGF, we show that epithelial cell functions differ depending on the form of HB-EGF being expressed. Expression of noncleavable membrane-anchored HB-EGF promoted cell-matrix and cell-cell interactions and decreased cell migration, HGF/SF-induced cell scattering and formation of tubular structures. By contrast, expression of soluble HB-EGF induced increased cell migration, decreased cell-matrix and cell-cell interactions and promoted the development of long unbranched tubular structures in response to HGF/SF. These findings suggest that HB-EGF can not only modulate HGF/SF-induced cellular responses in MDCK cells but also that membrane-bound HB-EGF and soluble HB-EGF give rise to distinctly different effects on cell-cell and cell-extracellular matrix interactions.

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“…This suggests that an elevated level of the protein interferes with the signaling for lamellipodial protrusion, possibly by acting via the actin cytoskeleton directly or indirectly by modulating the Rac GTPase pathway. In comparison, the same MDCK cells are capable of migration after the application of SF, suggesting that the inhibitory action of PMP22 on wound-induced migration is likely dependent upon epithelial cell-cell contacts, because SF induces a junction-disrupting EMT (Grisendi et al, 1998).…”

Section: Discussionmentioning

confidence: 98%

Modulation of Epithelial Morphology, Monolayer Permeability, and Cell Migration by Growth Arrest Specific 3/Peripheral Myelin Protein 22

Roux

Amici

Fletcher

et al. 2005

MBoC

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Peripheral myelin protein 22 (PMP22) is associated with a subset of hereditary peripheral neuropathies. Although predominantly recognized as a transmembrane constituent of peripheral nerve myelin, PMP22 is localized to epithelial and endothelial cell-cell junctions, where its function remains unknown. In this report, we investigated the role of PMP22 in epithelial biology. Expression of human PMP22 (hPMP22) slows cell growth and induces a flattened morphology in Madin-Darby canine kidney (MDCK) cells. The transepithelial electrical resistance (TER) and paracellular flux of MDCK monolayers are elevated by hPMP22 expression. After calcium switch, peptides corresponding to the second, but not the first, extracellular loop of PMP22 perturb the recovery of TER and paracellular flux. Finally, subsequent to wounding, epithelial monolayers expressing hPMP22 fail to migrate normally. These results indicate that PMP22 is capable of modulating several aspects of epithelial cell biology, including junctional permeability and wound closure. INTRODUCTIONThe tetraspan glycoprotein peripheral myelin protein 22 (PMP22), also known as growth arrest specific 3 (gas3) gene, has proposed roles in peripheral nerve myelin formation, cell-cell interactions, and cell proliferation (Suter and Snipes, 1995). Although the highest expression levels are found in myelin-forming Schwann cells, PMP22 mRNA can be detected in a multitude of developing and mature nonneural tissues, including epithelia of the intestine (Baechner et al., 1995;Taylor et al., 1995;Wulf and Suter, 1999) and the choroid plexus (Roux et al., 2004). The specific role of PMP22 in Schwann cells remains undefined, although it is known that altered expression is associated with heritable demyelinating peripheral neuropathies (Naef and Suter, 1998). Similarly, the function of the protein at nonneural locations remains undetermined.In vitro studies have identified a role for PMP22 in the regulation of cell proliferation and morphology. In Schwann cells, elevated expression delays the transition from G0/G1 to the S phase of the cell cycle (Zoidl et al., 1995), and can lead to apoptosis in some instances (Fabbretti et al., 1995;Zoidl et al., 1997). Conversely, reduced PMP22 mRNA levels are associated with enhanced DNA synthesis and entry into the S ϩ G2/M phases (Zoidl et al., 1995). In NIH 3T3 fibroblasts, PMP22 overexpression regulates cell spreading, an effect that is dependent on the Rho-GTPase pathway (Brancolini et al., 1999). Recent studies have detected exogenous PMP22 in ADP-ribosylation factor 6 (Arf-6)-positive plasma membrane-endosomal recycling vacuoles before apoptosis or changes in cell shape (Chies et al., 2003). This pathway is known to be involved in modulating the actin cytoskeleton, cell polarity, adhesion, and migration (Donaldson, 2003). Together, these findings support the notion that PMP22 has a significant role in basic cellular processes, extending beyond an involvement in Schwann cell myelination.We previously described PMP22 as a constituent of apical ...

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Effect of hepatocyte growth factor on assembly of zonula occludens-1 protein at the plasma membrane

Cited by 45 publications

References 31 publications

Proinflammatory Cytokines Disrupt Epithelial Barrier Function by Apoptosis-Independent Mechanisms

Proinflammatory Cytokines Disrupt Epithelial Barrier Function by Apoptosis-Independent Mechanisms

Membrane-associated HB-EGF modulates HGF-induced cellular responses in MDCK cells

Modulation of Epithelial Morphology, Monolayer Permeability, and Cell Migration by Growth Arrest Specific 3/Peripheral Myelin Protein 22

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