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B and Enhances Tumor Cell Adhesion and Invasion Through a 
1 Integrin-Dependent Mechanism
* Department of Academic Surgery, National University of Ireland, Cork University Hospital, Cork, Ireland; and
Department of Academic Surgery, Royal College of Surgeons in Ireland, Beaumont Hospital, Dublin, Ireland
1 integrins play a crucial role in
supporting tumor cell attachment to and invasion into the extracellular
matrix. Endotoxin/LPS introduced by surgery has been shown to enhance
tumor metastasis in a murine model. Here we show the direct effect of
LPS on tumor cell adhesion and invasion in extracellular matrix
proteins through a 1 integrin-dependent pathway. The
human colorectal tumor cell lines SW480 and SW620 constitutively
expressed high levels of the 1 subunit, whereas various
low levels of 
1, 2, 4, and
6 expression were detected. SW480 and SW620 did not
express membrane-bound CD14; however, LPS in the presence of soluble
CD14 (sCD14) significantly up-regulated 1 integrin
expression; enhanced tumor cell attachment to fibronectin, collagen I,
and laminin; and strongly promoted tumor cell invasion through the
Matrigel. Anti-1 blocking mAbs (4B4 and 6S6) abrogated
LPS- plus sCD14-induced tumor cell adhesion and invasion. Furthermore,
LPS, when combined with sCD14, resulted in NF-
B activation in both
SW480 and SW620 cells. Inhibition of the NF-B pathway significantly
attenuated LPS-induced up-regulation of 1 integrin
expression and prevented tumor cell adhesion and invasion. These
results provide direct evidence that although SW480 and SW620 cells do
not express membrane-bound CD14, LPS in the presence of sCD14 can
activate NF-B, up-regulate 1 integrin
expression, and subsequently promote tumor cell adhesion and invasion.
Moreover, LPS-induced tumor cell attachment to and invasion through
extracellular matrix proteins is 1
subunit-dependent.
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