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Connexin45 interacts with zonula occludens-1 in osteoblastic cellsConnexin43 (Cx43) and Cx45 are co-expressed in a number of different tissues. Studies demonstrated that Cx45 transfected ROS (ROS/Cx45) cells, were less permeable to low molecular weight dyes than untransfected ROS cells, that have gap junctions made of Cx43. This suggests that there may be a functionally important interaction between Cx43 and Cx45 in these cells. One way in which these proteins may interact is by associating with the same set of proteins. In order to isolate connexin interacting proteins, we isolated Cx45 from Cx45 transfected ROS cells (ROS/Cx45 cells) under mild detergent conditions. These studies showed that Cx45 co-purified with the tight junction protein, ZO-1. Immunofluorescence studies of ROS/Cx45 cells simultaneously stained with polyclonal Cx45 antibody and a monoclonal ZO-1 antibody showed that Cx45 and ZO-1 colocalized in ROS/Cx45 cells. Furthermore we found that ZO-1 could bind to peptides derived from the carboxyl terminal of Cx45 that had been covalently bound to an agarose resin. These data suggests that Cx45 and ZO-1 directly interact in ROS/Cx45 cells.
Document ID
20040088272
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Laing, J. G.
(Washington University School of Medicine St. Louis, Missouri 63110, United States)
Manley-Markowski, R. N.
Koval, M.
Civitelli, R.
Steinberg, T. H.
Date Acquired
August 21, 2013
Publication Date
January 1, 2001
Publication Information
Publication: Cell communication & adhesion
Volume: 8
Issue: 4-6
ISSN: 1541-9061
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
Non-NASA Center
NASA Discipline Cell Biology

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