The interaction of extracellular matrix with cells plays a key role in the regulation of cell adhesion, migration, proliferation as well as differentiation. Transformed cells express a different profile of adhesion molecules, which may mediate
metastasis under specific matrix microenvironment. We here found that ROS 17/2.8
osteosarcoma cells and osteoblasts have different expression of
alpha5 integrin, executing different
fibronectin fibrillogenesis. As compared with ROS 17/2.8 cells, osteoblasts have higher expression of
fibronectin,
collagen, alpha5, beta1, alpha2
integrins and
focal adhesion kinase as examined by immunostaining and flow cytometry.
Crovidisin, a PIII
snake venom metalloproteinase (SVMP) purified from
venom of Crotalus viridis, exhibits
collagen-binding activity and
matrix metalloproteinase activity.
Crovidisin selectively caused the detachment of ROS 17/2.8
osteosarcoma cells but not of primary cultured osteoblasts. On the other hand,
triflavin, an RGD-dependent
disintegrin purified from
venom of Trimeresurus flavoviridis, did not cause the detachment of both osteoblasts and ROS 17/2.8 cells. Although ROS 17/2.8 cells detached from substratum after
crovidisin treatment for 24 h, the loss of mitochondrial membrane potential was not observed unless a prolonged treatment for longer than 36 h. These results suggest that cultured primary rat osteoblasts and ROS 17/2.8
osteosarcoma cells possess different expression of
integrins and matrix environment, and ROS 17/2.8 is much more susceptible to be detached by
crovidisin. The matrix degradation by
crovidisin may be responsible for the preferential detachment of ROS 17/2.8
osteosarcoma cells.