Differential adhesion of metastatic RAW117 large-cell lymphoma cells under static or hydrodynamic conditions: role of integrin alpha(v) beta3.
RGD-containing substrates were used to study static and hydrodynamic adhesion of murine RAW117 large-cell lymphoma sublines with differential liver-metastatic potentials. Highly liver-metastatic RAW117-H10 cells had higher rates of static adhesion to vitronectin, fibronectin and (GRGDS)4 than poorly metastatic RAW117-P and moderately liver-metastatic RAW117-L17 cells. Under hydrodynamic conditions, adhesion stabilization was more rapid for H10 cells compared to P or L17 cells. Among the RGD peptides, only the polymeric RGD peptide (GRGDS)4 mediated strong static adhesion of H10 cells. Interestingly, all the RGD peptides mediated adhesion stabilization for H10 cells but still not for L17 or P cells under hydrodynamic conditions. Integrin alpha(v) beta3 was involved in stabilizing hydrodynamic adhesion to (GRGDS)4, monomeric RGD peptide R1, but was less important in static adhesion to monomeric RGD peptides. Differential adhesion to liver sinusoidal endothelial cell-derived extracellular matrix (H10 >> L17 > P) was observed under hydrodynamic but not static conditions. Integrin alpha(v) beta3 was also important in hydrodynamic adhesion to liver sinusoidal endothelial cell-derived extracellular matrix. We believe that strong static and hydrodynamic adhesion of H10 cells and their capability of altering adhesive behavior in response to fluid shear may contribute to liver metastasis.
Yun
Z
Z
Department of Tumor Biology, The University of Texas M. D. Anderson Cancer Center, Houston, USA.
Smith
T W
TW
Menter
D G
DG
McIntire
L V
LV
Nicolson
G L
GL
D000595:Amino Acid Sequence; D000818:Animals; D002448:Cell Adhesion; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism; D008113:Liver Neoplasms / Q000556:secondary*; D016403:Lymphoma, Large B-Cell, Diffuse / Q000473:pathology*; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000502:physiology*; D009842:Oligopeptides / Q000378:metabolism / Q000502:physiology*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000378:metabolism; D019030:Receptors, Vitronectin / Q000502:physiology*; D012212:Rheology; D013314:Stress, Mechanical; D014407:Tumor Cells, Cultured; D019096:Vitronectin / Q000378:metabolism
D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D009363:Neoplasm Proteins; D009842:Oligopeptides; D010446:Peptide Fragments; D019030:Receptors, Vitronectin; D019096:Vitronectin; C047981:arginyl-glycyl-aspartic acid; C049554:glycyl-arginyl-glycyl-aspartyl-serine