Extracellular matrix proteoglycans and cell-substratum adhesion of human endothelial cells: the effect of methyl beta-D-xylopyranoside.

The influence of methyl beta-D-xylopyranoside on human endothelial cell proteoglycans isolated from the medium and extracellular matrix was investigated. Confluent cultures of human endothelial cells incorporate significant amounts of heparan sulfate (78%), chondroitin sulfate (10%), and dermatan sulfate (12%) into the extracellular matrix. Chondroitin sulfate (35%) and dermatan sulfate (37%) were the major glycosaminoglycans present in the medium. In the presence of methyl beta-D-xylopyranoside, incorporation of labeled proteoglycans into extracellular matrix was diminished by approximately 70%. Heparan sulfate comprised the major proteoglycan present in extracellular matrix (89%) in cells grown in the presence of methyl beta-D-xylopyranoside. In contrast to the incorporation of proteoglycan into extracellular matrix, methyl beta-D-xylopyranoside stimulated the secretion of labeled glycosaminoglycan chains into the medium 2.5-fold. In the presence of methyl beta-D-xylopyranoside, secretion of chondroitin sulfate into the medium was markedly stimulated, with a slight increase in secretion of heparan sulfate. Chondroitin sulfate (62%) and heparan sulfate (34%) were the major labeled glycosaminoglycans present in medium from methyl beta-D-xylopyranoside-treated cultures. The effect of methyl beta-D-xylopyranoside on cell adhesion and detachment was investigated. Cell detachment from extracellular matrix depleted of proteoglycan was significantly faster than detachment from normal matrix. Conversely, human endothelial cells adhered faster to normal matrix than to matrix depleted of proteoglycan.