TY - JOUR

T1 - Adhesion defective BHK cell mutant has cell surface heparan sulfate proteoglycan of altered properties.

AU - Couchman, J R

AU - Austria, R

AU - Woods, A

AU - Hughes, R C

N1 - Keywords: Animals; Cell Adhesion; Cell Line; Chondroitin Lyases; Chromatography, Affinity; Cricetinae; Glycosaminoglycans; Half-Life; Heparan Sulfate Proteoglycans; Heparitin Sulfate; Microscopy, Phase-Contrast; Proteochondroitin Sulfates; Proteoglycans; Surface Properties

PY - 1988

Y1 - 1988

N2 - In the light of accumulating data that implicate cell surface heparan sulfate proteoglycans (HSPGs) with a role in cell interactions with extracellular matrix molecules such as fibronectin, we have compared the properties of these molecules in wild-type BHK cells and an adhesion-defective ricin-resistant mutant (RicR14). Our results showed that the mutant, unlike BHK cells, cannot form focal adhesions when adherent to planar substrates in the presence of serum. Furthermore, while both cell lines possess similar amounts of cell surface HSPG with hydrophobic properties, that of RicR14 cells had decreased sulfation, reduced affinity for fibronectin and decreased half-life on the cell surface when compared to the normal counterpart. Our conclusions based on this data are that these altered properties may, in part, account for the adhesion defect in the ricin-resistant mutant. Whether this results from the known alteration in assembly of N-linked glycans affecting the carbohydrate chains on the proteoglycan or some other combination of factors is discussed.

AB - In the light of accumulating data that implicate cell surface heparan sulfate proteoglycans (HSPGs) with a role in cell interactions with extracellular matrix molecules such as fibronectin, we have compared the properties of these molecules in wild-type BHK cells and an adhesion-defective ricin-resistant mutant (RicR14). Our results showed that the mutant, unlike BHK cells, cannot form focal adhesions when adherent to planar substrates in the presence of serum. Furthermore, while both cell lines possess similar amounts of cell surface HSPG with hydrophobic properties, that of RicR14 cells had decreased sulfation, reduced affinity for fibronectin and decreased half-life on the cell surface when compared to the normal counterpart. Our conclusions based on this data are that these altered properties may, in part, account for the adhesion defect in the ricin-resistant mutant. Whether this results from the known alteration in assembly of N-linked glycans affecting the carbohydrate chains on the proteoglycan or some other combination of factors is discussed.

U2 - 10.1002/jcp.1041360204

DO - 10.1002/jcp.1041360204

M3 - Journal article

C2 - 2970466

VL - 136

SP - 226

EP - 236

JO - Journal of Cellular Physiology

JF - Journal of Cellular Physiology

SN - 0021-9541

IS - 2

ER -