TY - JOUR
T1 - Involvement of cortactin and phosphotyrosine proteins in cell-cell contact formation in cultured bovine corneal endothelial cells
AU - Kredy-Farhan, Lily
AU - Kotev-Emeth, Shlomo
AU - Savion, Naphtali
N1 - Funding Information:
Acknowledgments This study was supported by a grant from the Claire and Amedee Marateir Institute for the Study of Blindness and Visual Disorders. The authors thank Yair Andegeko, Tel-Aviv University, Tel-Aviv, for his contribution to the immunoXuorescence studies and to Mark Tarshis, Ph.D. The Hebrew University of Jerusalem, Jerusalem, for his devoted technical support to the confocal microscopy studies. This work was conducted in partial fulWllment of the requirements for Ph.D. degree of Lily Kredy-Farhan, Sackler faculty of medicine, Tel Aviv University, Tel Aviv, Israel.
PY - 2008/2
Y1 - 2008/2
N2 - Phosphotyrosine proteins involvement, particularly cortactin, was studied in cell-cell contacts of cultured bovine corneal endothelial (BCE) cells. These proteins, including α-catenin, vinculin and cortactin, are localized at cell-cell contacts separate from the cortical actin ring. Approximately 50% of cortactin isoforms p80 and p85 were associated with the Triton-insoluble fraction while phosphotyrosine proteins were in the soluble fraction. Disruption of cell-cell contacts by EDTA treatment was associated with a decrease in cortactin isoforms p80 (26%) and p85 (57%). Cortactin isoform p85 was phosphorylated at Y466, expressed in reattaching cells and associated with the Triton-soluble fraction, whereas cortactin isoform p80 was phosphorylated at Y421 and associated with the Triton-insoluble fraction. In sub-confluent cultures, pY421-cortactin was localized at the leading edge and pY466-cortactin at a perinuclear area. In confluent cultures both pY466- and pY421-cortactin isoforms were localized at the cell-cell contacts. In conclusion, in BCE cells, the most prominent appearance of cortactin was at the cell-cell contacts separate from the cortical actin ring. Isoform p80 was phosphorylated at Y 421 and associated with the Triton-insoluble fraction and isoform p85 was phosphorylated at Y466 and associated with the Triton-insoluble fraction.
AB - Phosphotyrosine proteins involvement, particularly cortactin, was studied in cell-cell contacts of cultured bovine corneal endothelial (BCE) cells. These proteins, including α-catenin, vinculin and cortactin, are localized at cell-cell contacts separate from the cortical actin ring. Approximately 50% of cortactin isoforms p80 and p85 were associated with the Triton-insoluble fraction while phosphotyrosine proteins were in the soluble fraction. Disruption of cell-cell contacts by EDTA treatment was associated with a decrease in cortactin isoforms p80 (26%) and p85 (57%). Cortactin isoform p85 was phosphorylated at Y466, expressed in reattaching cells and associated with the Triton-soluble fraction, whereas cortactin isoform p80 was phosphorylated at Y421 and associated with the Triton-insoluble fraction. In sub-confluent cultures, pY421-cortactin was localized at the leading edge and pY466-cortactin at a perinuclear area. In confluent cultures both pY466- and pY421-cortactin isoforms were localized at the cell-cell contacts. In conclusion, in BCE cells, the most prominent appearance of cortactin was at the cell-cell contacts separate from the cortical actin ring. Isoform p80 was phosphorylated at Y 421 and associated with the Triton-insoluble fraction and isoform p85 was phosphorylated at Y466 and associated with the Triton-insoluble fraction.
KW - Cortactin
KW - Cortical actin ring
KW - Phospho-cortactin
KW - Vinculin
KW - α-Catenin
UR - http://www.scopus.com/inward/record.url?scp=39149145498&partnerID=8YFLogxK
U2 - 10.1007/s00418-007-0357-8
DO - 10.1007/s00418-007-0357-8
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AN - SCOPUS:39149145498
SN - 0948-6143
VL - 129
SP - 193
EP - 202
JO - Histochemistry and Cell Biology
JF - Histochemistry and Cell Biology
IS - 2
ER -