Premium
Depletion of Integrin‐Linked Kinase (ILK) from Primary Mouse Hepatocytes Leads to Apoptosis
Author(s) -
Gkretsi Vasiliki,
Mars Wendy,
Bell Aaron,
Dedhar Shoukat,
StArnaud Rene,
Wu Chuanyue,
Michalopoulos George
Publication year - 2006
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.20.4.a630-a
Subject(s) - integrin linked kinase , microbiology and biotechnology , integrin , extracellular matrix , apoptosis , chemistry , kinase , collagenase , biology , cell , protein kinase a , biochemistry , cyclin dependent kinase 2 , enzyme
Integrin‐linked kinase (ILK) is an important component of cell‐matrix adhesions, able to bind to β1‐integrins and it therefore connects the extracellular matrix to the inner compartment of the cell. ILK has been implicated in many fundamental cellular processes such as differentiation, proliferation, and survival. In this study, we investigated the role of ILK in primary mouse hepatocytes. Our results demonstrate that depletion of ILK from mouse hepatocytes leads to massive apoptosis. Mouse hepatocytes were first isolated from ILK‐floxed animals by collagenase perfusion, and were subsequently infected with either β‐gal or Cre‐recombinase adenovirus. Cells were then harvested at different time points for western blot analyses as well as caspase 3 activity measurements. Depletion of ILK in primary mouse hepatocytes was accompanied by increased caspase 3 activity and significant inhibition of PINCH, and α‐parvin, which along with ILK form a stable well‐characterized ternary complex at cell‐matrix adhesions. These results suggest that ILK is essential for the survival of primary hepatocytes therefore more experiments are underway to elucidate the molecular mechanism underlying this phenomenon. This work was supported by NIH grant CA35373.to G.K.M., and NIH grants GM65188 and DK54639 to C.W.