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Research Article |
1 is required for IGF-I protection from cell death induced by loss of extracellular matrix adhesion
1 Department of Biochemistry, Vanderbilt University School of Medicine,
Nashville, Tennessee, TN 37232-0146, USA
2 Department of Medicine, Vanderbilt University School of Medicine, Nashville,
Tennessee, TN 37232-0146, USA
* Author for correspondence (e-mail: graham.carpenter{at}mcmail.vanderbilt.edu )
Accepted 20 February 2002
Phospholipase C-
1, a tyrosine kinase substrate, hydrolyses
phosphatidylinositol 4,5-bisphosphate to produce inositol 1,4,5-trisphosphate
and diacylglycerol, which act as second messenger moleculesto mobilize
intracellular calcium and activate protein kinase C, respectively. We have
investigated the role of phospholipase C-
1 in anoikis, or cell death,
induced by the loss of extracellular matrix adhesion. Spontaneously
immortalized mouse embryonic fibroblasts nullizygous at the Plcg1
locus (Plcg1-/-), referred to as Null cells, were derived
from targeted gene disruption experiments. Subsequently, phospholipase
C-
1 was re-expressed in these cells to derive Null+ cells. The Null and
Null+ cells were then placed in suspension to induce cell death, which was
measured directly as well as by the induction of caspase 3, as an index of
programmed cell death or apoptosis. The results demonstrate that insulin-like
growth factor can rescue Null+ cells but not Null cells from
suspension-induced cell death. This demonstrates that phospholipase C-
1
is required for insulin-like growth factor dependent cell survival under these
conditions. Lastly, the data demonstrate that insulinlike growth factor
stimulated tyrosine phosphorylation of phospholipase C-
1 in both
adherent and suspension cells.
Key words: Phospholipase C, Anoikis, Insulin-like growth factor
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