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Clues to occludin. Focus on "Knockdown of occludin expression leads to diverse phenotypic alterations in epithelial cells"

Clues to occludin. Focus on "Knockdown of occludin expression leads to diverse phenotypic... Clues to occludin. Focus on "Knockdown of occludin expression leads to diverse phenotypic alterations in epithelial cells" Karl S. Matlin Laboratory of Epithelial Pathobiology, Department of Surgery, University of Cincinnati College of Medicine, Cincinnati, Ohio FOR MANY YEARS AFTER ITS SYSTEMATIC morphological description by Farquhar and Palade in 1963 ( 7 ), the tight junction remained a puzzle. The freeze-fracture knife exposed anastomosing ridges in platinum/carbon replicas resembling the bones of ancient fossils, and, like fossils, provided few clues to living, breathing function. Speculation abounded about the true nature of the tight junction, with those favoring protein or lipid structures squared off in competing camps ( 14 ) while others counted strands and developed models, waiting for new breakthroughs ( 4 ). All of this began to change in 1986 with the identification of ZO-1 ( 15 ), proudly named as the first bona fide component of the zonula occludens, as tight junctions were formally bestowed by Farquhar and Palade ( 7 ). Enthusiasm was tempered, however, with the recognition that ZO-1 was not an integral membrane protein, but one that associated with the cytoplasmic face of the tight junction and thus could not account for the intercellular http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Cell Physiology The American Physiological Society

Clues to occludin. Focus on "Knockdown of occludin expression leads to diverse phenotypic alterations in epithelial cells"

AJP - Cell Physiology , Volume 288 (6): C1191 – Jun 1, 2005

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Publisher
The American Physiological Society
Copyright
Copyright © 2010 the American Physiological Society
ISSN
0363-6143
eISSN
1522-1563
DOI
10.1152/ajpcell.00067.2005
pmid
15897320
Publisher site
See Article on Publisher Site

Abstract

Clues to occludin. Focus on "Knockdown of occludin expression leads to diverse phenotypic alterations in epithelial cells" Karl S. Matlin Laboratory of Epithelial Pathobiology, Department of Surgery, University of Cincinnati College of Medicine, Cincinnati, Ohio FOR MANY YEARS AFTER ITS SYSTEMATIC morphological description by Farquhar and Palade in 1963 ( 7 ), the tight junction remained a puzzle. The freeze-fracture knife exposed anastomosing ridges in platinum/carbon replicas resembling the bones of ancient fossils, and, like fossils, provided few clues to living, breathing function. Speculation abounded about the true nature of the tight junction, with those favoring protein or lipid structures squared off in competing camps ( 14 ) while others counted strands and developed models, waiting for new breakthroughs ( 4 ). All of this began to change in 1986 with the identification of ZO-1 ( 15 ), proudly named as the first bona fide component of the zonula occludens, as tight junctions were formally bestowed by Farquhar and Palade ( 7 ). Enthusiasm was tempered, however, with the recognition that ZO-1 was not an integral membrane protein, but one that associated with the cytoplasmic face of the tight junction and thus could not account for the intercellular

Journal

AJP - Cell PhysiologyThe American Physiological Society

Published: Jun 1, 2005

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