TY - JOUR
T1 - Reduced cell adhesion to fibronectin and laminin is associated with altered glycosylation of β1, integrins in a weakly metastatic glycosylation mutant
AU - Oz, O. K.
AU - Campbell, A.
AU - Tao, T.
PY - 1989/8/15
Y1 - 1989/8/15
N2 - A weakly metastatic wheat‐germ‐agglutinin‐resistant mutant Wa4‐b I was previously shown to be less adherent to endothelial cell extracellular matrix than the more metastatic parental B‐16 melanoma cells. This report describes reduced adhesion and spreading of Wa4‐bI cells on the cell‐binding domain of fibronectin (CBD) and laminin (LN). Cell surface receptors which mediate such interactions are members of the integrin family of membrane glycoproteins. An antibody that recognizes the 3, integrin subunit inhibited spreading on both the CBD and LN. The integrins of the mutant cells immunoprecipitated by the antibody appeared to be structurally altered, showing a greater electrophoretic mobility. The mobility difference between the parent and the mutant receptors was abolished following removal of the glycan moieties of the receptors enzymatically using glycopeptidase F, or chemically using trifluoromethanesulfonic acid, suggesting that the structural alteration of the mutant receptors is in glycosylation. The altered receptors may be responsible for the observed decrease in cell adhesion and spreading of the mutant cells to the CBD and LN. Such a decrease in Wa4‐bI cell interaction with extracellular matrix components may play a role in their decreased metastatic potential.
AB - A weakly metastatic wheat‐germ‐agglutinin‐resistant mutant Wa4‐b I was previously shown to be less adherent to endothelial cell extracellular matrix than the more metastatic parental B‐16 melanoma cells. This report describes reduced adhesion and spreading of Wa4‐bI cells on the cell‐binding domain of fibronectin (CBD) and laminin (LN). Cell surface receptors which mediate such interactions are members of the integrin family of membrane glycoproteins. An antibody that recognizes the 3, integrin subunit inhibited spreading on both the CBD and LN. The integrins of the mutant cells immunoprecipitated by the antibody appeared to be structurally altered, showing a greater electrophoretic mobility. The mobility difference between the parent and the mutant receptors was abolished following removal of the glycan moieties of the receptors enzymatically using glycopeptidase F, or chemically using trifluoromethanesulfonic acid, suggesting that the structural alteration of the mutant receptors is in glycosylation. The altered receptors may be responsible for the observed decrease in cell adhesion and spreading of the mutant cells to the CBD and LN. Such a decrease in Wa4‐bI cell interaction with extracellular matrix components may play a role in their decreased metastatic potential.
UR - http://www.scopus.com/inward/record.url?scp=0024435102&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024435102&partnerID=8YFLogxK
U2 - 10.1002/ijc.2910440226
DO - 10.1002/ijc.2910440226
M3 - Article
C2 - 2788145
AN - SCOPUS:0024435102
SN - 0020-7136
VL - 44
SP - 343
EP - 347
JO - International Journal of Cancer
JF - International Journal of Cancer
IS - 2
ER -