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Protein Tyrosine Dephosphorylation and the Maintenance of Cell Adhesions in the Pancreas
Author(s) -
SCHNEKENBURGER J.,
MAYERLE J.,
SIMON P.,
DOMSCHKE W.,
LERCH M. M.
Publication year - 1999
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1999.tb09518.x
Subject(s) - adherens junction , microbiology and biotechnology , cadherin , cell adhesion , protein tyrosine phosphatase , dephosphorylation , cell , tyrosine , chemistry , biology , tyrosine phosphorylation , morphogenesis , phosphorylation , biochemistry , phosphatase , gene
A bstract : Cell‐cell contacts are important regulatory elements in tissue development, organ morphogenesis and malignant tumor invasion. In recent in vivo studies we have identified the members of the cadherin/catenin family of cell adhesion proteins that are differentially expressed in the pancreas and have determined their cell biological dynamics during dissociation and repair of adherens junctions. To further characterize these events, epithelial cell culture systems were used and a number of type II protein tyrosine phosphatases (PTPs) were found to colocalize and interact with the cadherin/catenin complex. These observations suggest that tyrosine dephosphorylation in general and PTPs in particular are involved in cell contact formation. Our most recent experiments indicate 1) that inhibition of PTPs alone dissociates pancreatic adherens junctions, 2) that cytosolic and transmembrane PTPs are differentially expressed in acinar cells, and 3) that a subset of them can associate with proteins of the cadherin/catenin complex at pancreatic cell‐cell adhesions.