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

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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.
Original languageEnglish
JournalJournal of Cellular Physiology
Volume136
Issue number2
Pages (from-to)226-36
Number of pages10
ISSN0021-9541
DOIs
Publication statusPublished - 1988

Bibliographical note

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

ID: 5167343