NDLI: Rho protein regulates tight junctions and perijunctional actin organization in polarized epithelia.

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Rho protein regulates tight junctions and perijunctional actin organization in polarized epithelia.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Parkos, C. A. Lemichez, E. Colgan, S. P. Giry, M. Madara, J. L. Turner, J. R. Carnes, D. Nusrat, A. Boquet, P.
Description	Author Affiliation: Nusrat A ( Department of Pathology, Brigham and Women's Hospital, Boston, MA 02115, USA.);
Abstract	The rho family of GTP-binding proteins regulates actin filament organization. In unpolarized mammalian cells, rho proteins regulate the assembly of actin-containing stress fibers at the cell-matrix interface. Polarized epithelial cells, in contrast, are tall and cylindrical with well developed intercellular tight junctions that permit them to behave as biologic barriers. We report that rho regulates filamentous actin organization preferentially in the apical pole of polarized intestinal epithelial cells and, in so doing, influences the organization and permeability of the associated apical tight junctions. Thus, barrier function, which is an essential characteristic of columnar epithelia, is regulated by rho.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Actins Physiology Botulinum Toxins Cell Polarity GTP-Binding Proteins Metabolism Intestines Cytology Tight Junctions Rho GTP-Binding Proteins ADP Ribose Transferases Ultrastructure Blotting, Western Cadherins Cell Adhesion Cell Communication Cells, Cultured Epithelial Cells Fluorescent Antibody Technique Genetics Membrane Proteins Phosphoproteins Precipitin Tests Recombinant Proteins Signal Transduction Zonula Occludens-1 Protein Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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