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Am J Physiol Renal Physiol 278: F847-F852, 2000;
0363-6127/00 $5.00
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Vol. 278, Issue 5, F847-F852, May 2000

Selective degradation of E-cadherin and dissolution of E-cadherin-catenin complexes in epithelial ischemia

Kevin T. Bush1, Tatsuo Tsukamoto2, and Sanjay K. Nigam1

1 Department of Medicine, University of California, San Diego, La Jolla, CA 92093-0693; 2 3rd Division, Department of Medicine, Kobe University School of Medicine, Chuo-ku, Kobe 650-0017, Japan

Ischemic epithelial cells are characterized by disruption of intercellular junctions and loss of apical-basolateral protein polarity, which are normally dependent on the integrity of the adherens junction (AJ). Biochemical analysis of both whole ischemic kidneys and ATP-depleted Madin-Darby canine kidney (MDCK) cells demonstrated a striking loss of E-cadherin (the transmembrane protein of the AJ) with the appearance and accumulation of an ~80-kDa fragment reactive with anti-E-cadherin antibodies on Western blots of ATP-depleted MDCK cells. This apparent ischemia-induced degradation of E-cadherin was not blocked by either inhibitors of the major proteolytic pathways (i.e., proteasome, lysosome, or calpain), or by chelation of intracellular calcium, suggesting the involvement of a protease capable of functioning at low ATP and low calcium levels. Immunocytochemistry revealed the movement of several proteins normally comprising the AJ, including E-cadherin and beta -catenin, away from lateral portions of the plasma membrane to intracellular sites. Moreover, rate-zonal centrifugation and immunoprecipitation with anti-E-cadherin and anti-beta -catenin antibodies indicated that ATP depletion disrupted normal E-cadherin-catenin interactions, resulting in the dissociation of alpha - and gamma -catenin from E-cadherin and beta -catenin-containing complexes. Because the generation and maintenance of polarized epithelial cells are dependent upon E-cadherin-mediated cell-cell adhesion and normal AJ function, we propose that the rapid degradation of E-cadherin and dissolution of the AJ is a key step in the development of the ischemic epithelial cell phenotype. Furthermore, we hypothesize that the reassembly of the AJ after ischemia/ATP depletion may require a novel bioassembly mechanism involving recombination of newly synthesized and sorted E-cadherin with preexisting pools of catenins that have (temporally) redistributed intracellularly.

Madin-Darby canine kidney; adenosine 5'-triphosphate; adherens junction; polyacrylamide gel electrophoresis; adenosine 5'-triphosphate depletion; antimycin A; 2-deoxyglucose; plakoglobin; cell adhesion


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