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A role of Desmoglein 2 in intestinal epithelial apoptosis.
Author(s) -
Nava Porfirio,
Hopkins Ann N.,
Laukoetter Mike G.,
Green Kathleen J.,
Parkos Charles A.,
Nusrat Asma
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a192
Subject(s) - microbiology and biotechnology , apoptosis , desmoglein , cadherin , chemistry , adherens junction , intracellular , cell junction , biology , cell , biochemistry
Intestinal epithelial intercellular junctions regulate barrier properties and have been linked to epithelial differentiation and programmed cell death (apoptosis). The intercellular junctions referred to as Desmosomes (DM) have been depicted as punctate structures that provide mechanical strength to epithelia. In simple intestinal epithelia, the DM cadherins, desmoglein 2 (Dsg2) and desmocollin 2 (Dsc2) affiliate with underlying intermediate filaments via linker plaque proteins. We used model intestinal epithelial cell lines to examine function of Dsg2. Our studies suggest that the cytoplasmic tail of Dsg2 but not Dsc2 is cleaved by caspase(s) during the onset of apoptosis induced by camptothecin. Furthermore, cleaved Dsg2 remains associated to the plasma membrane as shown by immunofluorescence labeling, while the underlying intermediate filaments retract from the plasma membrane. Additionally, siRNA‐mediated down‐regulation of Dsg2 protected epithelial cells from apoptosis. In summary, our findings suggest that Dsg2 is a target for caspase(s) and its cleavage sensitizes cells to stimulus induced apoptosis. These data also provide insight into a role of Dsg2 in apoptosis of intestinal epithelial cells during inflammation and differentiation.