caa a22 4500 47577504X CHVBK 20180406123629.0 cr unu---uuuuu 170329e20001101xx s 000 0 eng 10.1007/s00418-004-0718-5 doi (NATIONALLICENCE)springer-10.1007/s00418-004-0718-5 Association of connexin36 with zonula occludens-1 in HeLa cells, βTC-3 cells, pancreas, and adrenal gland [Elektronische Daten] [Xinbo Li*, Carl Olson*, Shijun Lu, James Nagy] The PDZ domain-containing protein zonula occludens-1 (ZO-1), a well-established component of tight junctions, has recently been shown to interact with various connexin proteins that form gap junctions. We investigated the association of connexin36 (Cx36) with ZO-1 in various cultured cells and tissues. Punctate immunofluorescence labeling for Cx36 was detected in Cx36-transfected HeLa cells, βTC-3 cells, pancreatic islets, and adrenal medulla. Immunofluorescence for ZO-1 was also punctate in cells and tissues, and was colocalized with Cx36 at points of cell-cell contact. Immunoprecipitation of either Cx36 or ZO-1 from cell lysates and tissue homogenates resulted in immunoblot detection of ZO-1 or Cx36, respectively, in immunoprecipitates. A 14-amino acid peptide corresponding to the carboxy-terminus of Cx36 showed binding capacity to the PDZ1 domain of ZO-1, which was eliminated after removal of the last 4 carboxy-terminus amino acids. Low micromolar concentrations of the 14-amino acid peptide produced up to 85% inhibition of Cx36 interaction with the PDZ1 domain of ZO-1. These results provide evidence for molecular interaction between Cx36 and ZO-1 in vitro, and in vivo, and suggest that the interference with Cx36/ZO-1 interaction by short carboxy-terminus peptides of Cx36 may be of value for functional studies of this interaction. Springer-Verlag, 2004 Connexin36 nationallicence Gap junctions nationallicence ZO-1 nationallicence Pancreas nationallicence Adrenal medulla nationallicence Li* Xinbo Department of Physiology, Faculty of Medicine, University of Manitoba, 730 William Avenue, R3E3J7, Winnipeg, Manitoba, Canada aut Olson* Carl Department of Physiology, Faculty of Medicine, University of Manitoba, 730 William Avenue, R3E3J7, Winnipeg, Manitoba, Canada aut Lu Shijun Department of Physiology, Faculty of Medicine, University of Manitoba, 730 William Avenue, R3E3J7, Winnipeg, Manitoba, Canada aut Nagy James Department of Physiology, Faculty of Medicine, University of Manitoba, 730 William Avenue, R3E3J7, Winnipeg, Manitoba, Canada aut Histochemistry and Cell Biology Springer-Verlag 122/5(2000-11-01), 485-498 0948-6143 122:5<485 2000 122 418 https://doi.org/10.1007/s00418-004-0718-5 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00418-004-0718-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Li* Xinbo Department of Physiology, Faculty of Medicine, University of Manitoba, 730 William Avenue, R3E3J7, Winnipeg, Manitoba, Canada aut NATIONALLICENCE 700 1- Olson* Carl Department of Physiology, Faculty of Medicine, University of Manitoba, 730 William Avenue, R3E3J7, Winnipeg, Manitoba, Canada aut NATIONALLICENCE 700 1- Lu Shijun Department of Physiology, Faculty of Medicine, University of Manitoba, 730 William Avenue, R3E3J7, Winnipeg, Manitoba, Canada aut NATIONALLICENCE 700 1- Nagy James Department of Physiology, Faculty of Medicine, University of Manitoba, 730 William Avenue, R3E3J7, Winnipeg, Manitoba, Canada aut NATIONALLICENCE 773 0- Histochemistry and Cell Biology Springer-Verlag 122/5(2000-11-01), 485-498 0948-6143 122:5<485 2000 122 418 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer