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17. Interferon-[gamma] inhibits enterocyte migration by reversibly displacing connexin43 from lipid rafts

Author

Leaphart, Cynthia L., Dai, Shipan, Gribar, Steven C., Richardson, Ward, Ozolek, John, Shi, Xia-hua, Bruns, Jennifer R., Branca, Maria, Li, Jun, Weisz, Ora A., Sodhi, Chhinder, and Hackam, David J.

Subjects
Interferon gamma -- Properties, Cell migration -- Evaluation, Cell junctions -- Properties, Enterocolitis, Neonatal necrotizing -- Development and progression, Enterocolitis, Pseudomembranous -- Development and progression, Cytokines -- Properties, Biological sciences
Abstract

Necrotizing enterocolitis (NEC) is associated with the release of interferon-[gamma] (IFN) by enterocytes and delayed intestinal restitution. Our laboratory has recently demonstrated that IFN inhibits enterocyte migration by impairing enterocyte gap junctions, intercellular channels that are composed of connexin43 (Cx43) monomers and that are required for enterocyte migration to occur. The mechanisms by which IFN inhibits gap junctions are incompletely understood. Lipid rafts are cholesterol-sphingolipid-rich microdomains of the plasma membrane that play a central role in the trafficking and signaling of various proteins. We now hypothesize that Cx43 is present on enterocyte lipid rafts and that IFN inhibits enterocyte migration by displacing Cx43 from lipid rafts in enterocytes. We now confirm our previous observations that intestinal restitution is impaired in NEC and demonstrate that Cx43 is present on lipid rafts in IEC-6 enterocytes. We show that lipid rafts are required for enterocyte migration, that IFN displaces Cx43 from lipid rafts, and that the phorbol ester phorbol 12-myristate 13-acetate (PMA) restores Cx43 to lipid rafts after treatment with IFN in a protein kinase C-dependent manner. IFN also reversibly decreased the phosphorylation of Cx43 on lipid rafts, which was restored by PMA. Strikingly, restoration of Cx43 to lipid rafts by PMA or by transfection of enterocytes with adenoviruses expressing wild-type Cx43 but not mutant Cx43 is associated with the restoration of enterocyte migration after IFN treatment. Taken together, these findings suggest an important role for lipid raft-Cx43 interactions in the regulation of enterocyte migration during exposure to IFN, such as NEC. gap junctions; connexin; necrotizing enterocolitis; cytokine; phorbol ester

Published
2008

18. Contributors

Author

Albright, Deborah, Arnold, Georgianne, Arora, Gaurav, Balest, Arcangela L., Baumhardt, Heather, Cannon, Glenn M., Carrasco, Mary M., Cassidy, Elaine, Chapman, Mary, Chaudhry, Rajeev, Chaves-Gnecco, Diego, Chi, David H., Jin Chong, Hey, Cleves-Bayon, Catalina, Cooper, James D., D’alesio, Alene, Davit, Alexander J., III, Debrunner, Mark, Dede, Ozgur, Eichman, Adelaide L., Escobar, Oscar, Feldman, Heidi M., Formeck, Cassandra L., Gaesser, Jenna, Gehris, Robin P., Glaser, Daniel, Goldstein, Jesse A., Grunwaldt, Lorelei J., Guerrero, Angela M., Gurtunca, Nursen, Landeo Gutierrez, Jeremy S., Koch, Ellen, Larkin, Allyson, Li, Xiaoxiao, Losee, Joseph E., Madan-Khetarpal, Suneeta, Malek, Marcus, Mcclincy, Michael P., Mccormick, Andrew A., Michaels, Marian G., Miyashita, Yosuke, Mollen, Kevin, Montano, Gerald T., Moon, Mackenzie, Moritz, Michael L., Narayanan, Srikala, Nischal, Ken K., O’donnell, Brighid, Olgun, Z. Deniz, Ortiz, Damara, Poholek, Catherine H., Richardson, Ward, Riley, Melissa M., Rudolph, Jeffrey A., Safier, Robert A., Squires, Judy H., Srinath, Arvind, Stevens, Erica L., Tadros, Sameh, Tersak, Jean M., Tobey, Allison, Torres, Orquidia A., Trucco, Sara M., Viswanathan, Pushpa, Weiner, Daniel J., Williams, John V., Witchel, Selma Feldman, Wolford, Jennifer E., Woods, Katelyn, and Zarit, Jennifer S.

Published
2023
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20. Contributors

Author

Abdalla, Wael Abdel Kawy, Allada, Vivek, Arnold, Georgianne, Balest, Arcangela Lattari, Baumhardt, Heather, Beerman, Lee B., Bogen, Debra L., Carrasco, Mary M., Cassidy, Elaine, Chaves-Gnecco, Diego, Chemaitilly, Wassim, Cheng, Kenneth P., Chi, David H., Chong, Hey Jin, Cooper, James D., D'Alesio, Alene, Deeney, Vincent F., Ellis, Demetrius, Escobar, Oscar, Feldman, Heidi M., Finder, Jonathan D., Gehris, Robin P., Goldstein, Jesse A., Green, Todd, Grunwaldt, Lorelei J., Hofkosh, Dena, Joyce, Emily, Katz, Aviva, Kreutzer, Jacqueline, Larkin, Allyson, Losee, Joseph E., Madan-Khetarpal, Suneeta, Martin, Brian, McCormick, Andrew A., McIntire, Sara C., Michaels, Marian G., Miyashita, Yosuke, Murray, Pamela J., Narayanan, Srikala, Nowalk, Andrew J., Ost, Michael C., Richardson, Ward, Riley, Melissa M., Rosenkranz, Margalit, Rudolph, Jeffrey A., Stephany, Heidi A., Sucato, Gina S., Szentpetery, Sylvia, Tadros, Sameh, Tersak, Jean M., Torok, Kathryn, Varma, Rajiv, Viswanathan, Pushpa, Weiner, Daniel J., Williams, John V., Williams, Shelley D., Witchel, Selma Feldman, Wolford, Jennifer E., Woods, Katelyn, Yellon, Robert F., Rose, Fateema Turay, and Zitelli, Basil J.

Published
2018
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21. A Role for Connexin43 in Macrophage Phagocytosis and Host Survival after Bacterial Peritoneal Infection1

Author

Anand, Rahul J., Dai, Shipan, Gribar, Steven C., Richardson, Ward, Kohler, Jeff W., Hoffman, Rosemary A., Branca, Maria F., Li, Jun, Shi, Xiao-Hua, Sodhi, Chhinder P., and Hackam, David J.

Subjects
Male, Mice, Knockout, Macrophages, Peritonitis, Survival Analysis, Article, Cell Line, Mice, Inbred C57BL, Mice, Liver, Connexin 43, Phagosomes, cardiovascular system, Macrophages, Peritoneal, Animals, Humans, Female, sense organs, biological phenomena, cell phenomena, and immunity, Escherichia coli Infections, HeLa Cells
Abstract

The pathways that lead to the internalization of pathogens via phagocytosis remain incompletely understood. We now demonstrate a previously unrecognized role for the gap junction protein connexin43 (Cx43) in the regulation of phagocytosis by macrophages and in the host response to bacterial infection of the peritoneal cavity. Primary and cultured macrophages were found to express Cx43, which localized to the phagosome upon the internalization of IgG-opsonized particles. The inhibition of Cx43 using small interfering RNA or by obtaining macrophages from Cx43 heterozygous or knockout mice resulted in significantly impaired phagocytosis, while transfection of Cx43 into Fc-receptor expressing HeLa cells, which do not express endogenous Cx43, conferred the ability of these cells to undergo phagocytosis. Infection of macrophages with adenoviruses expressing wild-type Cx43 restored phagocytic ability in macrophages from Cx43 heterozygous or deficient mice, while infection with viruses that expressed mutant Cx43 had no effect. In understanding the mechanisms involved, Cx43 was required for RhoA-dependent actin cup formation under adherent particles, and transfection with constitutively active RhoA restored a phagocytic phenotype after Cx43 inactivation. Remarkably, mortality was significantly increased in a mouse model of bacterial peritonitis after Cx43 inhibition and in Cx43 heterozygous mice compared with untreated and wild-type counterparts. These findings reveal a novel role for Cx43 in the regulation of phagocytosis and rearrangement of the F-actin cytoskeleton, and they implicate Cx43 in the regulation of the host response to microbial infection.

Published
2008

23. A Critical Role for TLR4 Induction of Autophagy in the Regulation of Enterocyte Migration and the Pathogenesis of Necrotizing Enterocolitis

Author

Neal, Matthew D., primary, Sodhi, Chhinder P., additional, Dyer, Mitchell, additional, Craig, Brian T., additional, Good, Misty, additional, Jia, Hongpeng, additional, Yazji, Ibrahim, additional, Afrazi, Amin, additional, Richardson, Ward M., additional, Beer-Stolz, Donna, additional, Ma, Congrong, additional, Prindle, Thomas, additional, Grant, Zachary, additional, Branca, Maria F., additional, Ozolek, John, additional, and Hackam, David J., additional

Published
2013
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28. Extracellular High Mobility Group Box-1 (HMGB1) Inhibits Enterocyte Migration via Activation of Toll-like Receptor-4 and Increased Cell-Matrix Adhesiveness

Author

Dai, Shipan, primary, Sodhi, Chhinder, additional, Cetin, Selma, additional, Richardson, Ward, additional, Branca, Maria, additional, Neal, Matthew D., additional, Prindle, Thomas, additional, Ma, Congrong, additional, Shapiro, Richard A., additional, Li, Bin, additional, Wang, James H.-C., additional, and Hackam, David J., additional

Published
2010
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34. The NOD2 agonist muramyl-di-peptide (MDP) reverses the inhibitory effects of TLR4 activation on enterocyte proliferation through effects on beta-catenin signaling, and attenuates the severity of experimental necrotizing enterocolitis

Author

Richardson, Ward M., primary, Shi, Xiao-Hua, additional, Gribar, Steven C., additional, Branca, Maria, additional, Dubowski, Theresa, additional, Li, Jun, additional, Sodhi, Chhindler, additional, and Hackam, David J., additional

Published
2008
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38. 204. The TLR9 Agonist CpG-DNA Protects Against LPS-Induced Enterocyte Apoptosis Through the Up-Regulation of Heat Shock Protein 70 and Reduces the Severity of Necrotizing Enterocolitis in Mice

Author

Gribar, Steven C., primary, Evans, Anna C., additional, Richardson, Ward M., additional, Anand, Rahul J., additional, Kohler, Jeffrey W., additional, Branca, Maria F., additional, Dubowski, Theresa D., additional, Li, Jun, additional, Sodhi, Chhinder P., additional, and Hackam, David J., additional

Published
2008
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40. Typical Junior High School Physical Education Period

Author

Violet Richardson-Ward

Subjects
Medical education, Pedagogy, Psychology, Period (music), Physical education
Abstract

(1934). Typical Junior High School Physical Education Period. The Journal of Health and Physical Education: Vol. 5, No. 5, pp. 32-59.

Published
1934

42. Extracellular High Mobility Group Box-1 (HMGB1) Inhibits Enterocyte Migration via Activation of Toll-like Receptor-4 and Increased Cell-Matrix Adhesiveness.

Author

Shipan Dai, Sodhi, Chhinder, Cetin, Selma, Richardson, Ward, Branca, Maria, NeaI, Matthew D., Prindle, Thomas, Congrong Ma, Shapiro, Richard A., Bin Li, Wang, James H.-C., and Hackam, David J.

Subjects
*PHOSPHORYLATION, *CELL migration, *NEWBORN infants, *CARRIER proteins, *GENE expression, *DNA damage
Abstract

Toll-like receptor-4 (TLR4) is the receptor for bacterial lipopolysaccharide, yet it may also respond to a variety of endogenous molecules. Necrotizing enterocolitis (NEC) is the leading cause of death from gastrointestinal disease in newborn infants and is characterized by intestinal mucosal destruction and impaired enterocyte migration due to increased TLR4 signaling on enterocytes. The endogenous ligands for TLR4 that lead to impaired enterocyte migration remain unknown. High mobility group box-1 (HMGB1) is a DNA-binding protein that is released from injured cells during inflammation. We thus hypothesize that extracellular HMGB1 inhibits enterocyte migration via activation of TLR4 and sought to define the pathways involved. We now demonstrate that murine and human NEC are associated with increased intestinal HMGB1 expression, that serum HMGB1 is increased in murine NEC, and that HMGB1 inhibits enterocyte migration in vitro and in vivo in a TLR4-dependent manner. This finding was unique to enterocytes as HMGB1 enhanced migration of inflammatory cells in vitro and in vivo. In seeking to understand the mechanisms involved, TLR4-dependent HMGB1 signaling increased RhoA activation in enterocytes, increased phosphorylation of focal adhesion kinase, and increased phosphorylation of cofilin, resulting in increased stress fibers and focal adhesions. Using single cell force traction microscopy, the net effect of HMGB1 signaling was a TLR4-dependent increase in cell force adhesion, accounting for the impaired enterocyte migration. These findings demonstrate a novel pathway by which TLR4 activation by HMGB1 delays mucosal repair and suggest a novel potential therapeutic target in the amelioration of intestinal inflammatory diseases like NEC. [ABSTRACT FROM AUTHOR]

Published
2010
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43. DNA attenuates enterocyte Toll-like receptor 4-mediated intestinal mucosal injury after remote trauma.

Author

Sodhi C, Levy R, Gill R, Neal MD, Richardson W, Branca M, Russo A, Prindle T, Billiar TR, and Hackam DJ

Subjects
Adenoviridae genetics, Animals, Bacterial Translocation, Cell Proliferation drug effects, Cells, Cultured, DNA metabolism, Electrophoresis, Polyacrylamide Gel, Electrophoretic Mobility Shift Assay, Enterocytes drug effects, Genetic Vectors, Green Fluorescent Proteins, HMGB1 Protein metabolism, Immunity, Innate physiology, Immunohistochemistry, Intestinal Mucosa drug effects, Mice, Mice, Inbred C3H, Mutation physiology, NF-kappa B physiology, Reverse Transcriptase Polymerase Chain Reaction, Toll-Like Receptor 9 drug effects, Toll-Like Receptor 9 genetics, DNA pharmacology, Enterocytes pathology, Intestinal Mucosa injuries, Intestinal Mucosa pathology, Toll-Like Receptor 4 drug effects, Toll-Like Receptor 4 physiology
Abstract

Intestinal mucosal injury occurs after remote trauma although the mechanisms that sense remote injury and lead to intestinal epithelial disruption remain incompletely understood. We now hypothesize that Toll-like receptor 4 (TLR4) signaling on enterocytes after remote injury, potentially through the endogenous TLR4 ligand high-mobility group box-1 (HMGB1), could lead to intestinal dysfunction and bacterial translocation and that activation of TLR9 with DNA could reverse these effects. In support of this hypothesis, exposure of TLR4-expressing mice to bilateral femur fracture and systemic hypotension resulted in increased TLR4 expression and signaling and disruption of the ileal mucosa, leading to bacterial translocation, which was not observed in TLR4-mutant mice. TLR4 signaling in enterocytes, not immune cells, was required for this effect, as adenoviral-mediated inhibition of TLR4 in enterocytes prevented these findings. In seeking to identify the endogenous TLR4 ligands involved, the expression of HMGB1 was increased in the intestinal mucosa after injury in wild-type, but not TLR4-mutant, mice, and administration of anti-HMGB1 antibodies reduced both intestinal mucosal TLR4 signaling and bacterial translocation after remote trauma. Strikingly, mucosal injury was significantly increased in TLR9-mutant mice, whereas administration of exogenous DNA reduced the extent of TLR4-mediated enterocyte apoptosis, restored mucosal healing, and maintained the histological integrity of the intestinal barrier after remote injury. Taken together, these findings identify a novel link between remote injury and enterocyte TLR4 signaling leading to barrier injury, potentially through HMGB1 as a ligand, and demonstrate the reversal of these adverse effects through activation of TLR9.

Published
2011
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