Tu1830 The Trans-Golgi Network Protein Aftiphilin Regulates Colonic Epithelial Cell Permeability Through Modulating Expression of Genes Involved in Cell Junctions in Colonic Epithelial Cells

2016 ◽  
Vol 150 (4) ◽  
pp. S955
Author(s):  
Ivy Ka Man Law ◽  
Ryan G. Rogero ◽  
Charalabos Pothoulakis
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Cell Junctions ◽  
Cell Permeability ◽  
Colonic Epithelial Cell ◽  
Colonic Epithelial Cells ◽  
Trans Golgi Network ◽  
Expression Of Genes ◽  
Golgi Network

scholarly journals Redistribution of Cellular and Herpes Simplex Virus Proteins from the Trans-Golgi Network to Cell Junctions without Enveloped Capsids

2004 ◽  
Vol 78 (21) ◽  
pp. 11519-11535 ◽  
Author(s):  
Todd W. Wisner ◽  
David C. Johnson
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Epithelial Cell ◽  
Cellular Protein ◽  
Cell Junctions ◽  
Specific Cell ◽  
Trans Golgi Network ◽  
Simplex Virus ◽  
Golgi Network ◽  
Virus Egress

ABSTRACT Herpes simplex virus (HSV) and other alphaherpesviruses assemble enveloped virions in the trans-Golgi network (TGN) or endosomes. Enveloped particles are formed when capsids bud into TGN/endosomes and virus particles are subsequently ferried to the plasma membrane in TGN-derived vesicles. Little is known about the last stages of virus egress from the TGN/endosomes to cell surfaces except that the HSV directs transport of nascent virions to specific cell surface domains, i.e., epithelial cell junctions. Previously, we showed that HSV glycoprotein gE/gI accumulates extensively in the TGN at early times after infection and also when expressed without other viral proteins. At late times of infection, gE/gI and a cellular membrane protein, TGN46, were redistributed from the TGN to epithelial cell junctions. We show here that gE/gI and a second glycoprotein, gB, TGN46, and another cellular protein, carboxypeptidase D, all moved to cell junctions after infection with an HSV mutant unable to produce cytoplasmic capsids. This redistribution did not involve L particles. In contrast to TGN membrane proteins, several cellular proteins that normally adhere to the cytoplasmic face of TGN, Golgi, and endosomal membranes remained primarily dispersed throughout the cytoplasm. Therefore, cellular and viral membrane TGN proteins move to cell junctions at late times of HSV infection when the production of enveloped particles is blocked. This is consistent with the hypothesis that there are late HSV proteins that reorganize or redistribute TGN/endosomal compartments to promote virus egress and cell-to-cell spread.

scholarly journals Endothelin-3 stimulates survival of goblet cells in organotypic cultures of fetal human colonic epithelium

2008 ◽  
Vol 295 (6) ◽  
pp. G1182-G1189 ◽  
Author(s):  
Jiri Kalabis ◽  
Gang Li ◽  
Mizuho Fukunaga-Kalabis ◽  
Anil K. Rustgi ◽  
Meenhard Herlyn
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Organotypic Culture ◽  
Goblet Cells ◽  
Endothelin Receptors ◽  
Colonic Epithelium ◽  
Colonic Epithelial Cell ◽  
Colonic Epithelial Cells ◽  
Endothelin 3 ◽  
Human Colonic Epithelial Cell

Cells within the normal human colonic epithelium undergo a dynamic cycle of growth, differentiation, and death. The organotypic culture system of human fetal colonic epithelial cells seeded on top of collagen gels with embedded colonic fibroblasts allowed prolonged culture of the colonic epithelial cells (Kalabis J, Patterson MJ, Enders GM, Marian B, Iozzo RV, Rogler G, Gimotty PA, Herlyn M. FASEB J 17: 1115–1117, 2003). Herein, we have evaluated the role of endothelin-3 (ET3) and both cognate endothelin receptors (ETRA, ETRB) for human colonic epithelial cell growth and survival. ET3 was produced continuously by the fibroblasts as a result of adenovirus-mediated gene transfer. The presence and function of the endothelin receptors (ETRs) in epithelial cells was evaluated by [3H]thymidine incorporation using primary epithelial cells in monoculture and by immunohistochemistry on human fetal and adult paraffin-embedded tissues. In organotypic culture, ET3 increased the number of goblet cells but not of enteroendocrine cells. The increase in goblet cells was caused by prolonged cell survival and differentiation. The inhibition of both ETRA and ETRB significantly decreased the number of goblet cells and proliferation in epithelial cells, whereas the number of enteroendocrine cells remained unchanged. ET3 induced activation of IκB and MAPK in the epithelial cells, suggesting that these signaling pathways mediate its proproliferation and prosurvival activities. Our results demonstrate that ET3 is involved in regulating human colonic epithelial cell proliferation and survival, particularly for goblet cells, and may be an important component of colonic homeostasis.

scholarly journals Ocrl1, a PtdIns(4,5)P2 5-Phosphatase, Is Localized to the Trans-Golgi Network of Fibroblasts and Epithelial Cells

2000 ◽  
Vol 48 (2) ◽  
pp. 179-189 ◽  
Author(s):  
Marlene Armitage Dressman ◽  
Isabelle M. Olivos-Glander ◽  
Robert L. Nussbaum ◽  
Sharon F. Suchy
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Cell Metabolism ◽  
Cell Types ◽  
Cell Phenotype ◽  
Epithelial Cell Line ◽  
Specific Cell ◽  
Trans Golgi Network ◽  
Kidney Epithelial Cell ◽  
Golgi Network

PtdIns(4,5)P2 and PtdIns(4,5)P2 5-phosphatases play important roles in diverse aspects of cell metabolism, including protein trafficking. However, the relative importance of the PtdIns(4,5)P2 5-phosphatases in regulating PtdIns(4,5)P2 levels for specific cell processes is not well understood. Ocrl1 is a PtdIns(4,5)P2 5-phosphatase that is deficient in the oculocerebrorenal syndrome of Lowe, a disorder characterized by defects in kidney and lens epithelial cells and mental retardation. Ocrl1 was originally localized to the Golgi in fibroblasts, but a subsequent report suggested a lysosomal localization in a kidney epithelial cell line. In this study we defined the localization of ocrl1 in fibroblasts and in two kidney epithelial cell lines by three methods: immunofluorescence, subcellular fractionation, and a dynamic perturbation assay with brefeldin A. We found that ocrl1 was a Golgi-localized protein in all three cell types and further identified it as a protein of the trans-Golgi network (TGN). The TGN is a major sorting site and has the specialized function in epithelial cells of directing proteins to the apical or basolateral domains. The epithelial cell phenotype in Lowe syndrome and the localization of ocrl1 to the TGN imply that this PtdIns(4,5)P2 5-phosphatase plays a role in trafficking.

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