Wj. Checovich et Df. Mosher, LYSOPHOSPHATIDIC ACID ENHANCES FIBRONECTIN-BINDING TO ADHERENT CELLS, Arteriosclerosis and thrombosis, 13(11), 1993, pp. 1662-1667
1-Oleoyl lysophosphatidic acid (LPA) enhanced binding of I-125-labeled
fibronectin by cultured MG-63 osteosarcoma cells and human fibroblast
s in monolayer cultures up to threefold over control levels. For osteo
sarcoma cells, LPA was minimally active at 0.1 ng/mL (0.2 nmol/L) and
reached maximal activity at 10 ng/mL (20 nmol/L). Increased binding wa
s evident within 10 minutes of treatment of cycloheximide-treated cell
s with LPA and was due to an increase in the number of fibronectin bin
ding sites. LPA also increased the binding of a fragment containing th
e 70-kDa amino-terminal region of fibronectin that is primarily respon
sible for the reversible binding of fibronectin to matrix assembly sit
es on cell surfaces. Removal of LPA resulted in prompt return of fibro
nectin binding to baseline levels. These results indicate that LPA is
an important enhancer of fibronectin-rich matrix deposition by culture
d cells, and it may be the active component in serum and lipoprotein f
ractions that is responsible for enhancing fibronectin deposition.