Analysis of the glycopeptides derived from the extracellular matrix secreted by cultured bovine aortic smooth muscle cells.
Modulation of smooth muscle cell behaviour in culture has been associated with changes in the extracellular matrix. In the present study cultures of bovine aortic smooth muscle cells were compared in the rapidly proliferating and confluent phases of growth. The extracellular matrix was similar in both phases of growth and consisted of glycoproteins ranging from molecular weight 20,000 to over 200,000. The glycopeptides derived from these components displayed several differences. N-linked heteropolysaccharides of the biantennary and complex (more than two branches) types were predominant in the matrix of the confluent phase. Larger amounts of high mannose glycopeptides were present in the preparations from proliferating cells. O-Glycosidic glycopeptides were minor components in both preparations, but a slight increase was noted in the confluent phase of growth. Some of the changes in glycopeptides were interpreted in terms of the levels of the major components of the matrix such as the interstitial procollagens and fibronectin. The results indicate that processing of oligosaccharides associated with secreted glycoproteins of the extracellular matrix correlates with the state of growth of smooth muscle cells in culture.
Leushner
J R
JR
Department of Pathology, University of Western Ontario, London, Canada.
D000818:Animals; D001011:Aorta / Q000166:cytology*; D002417:Cattle; D002478:Cells, Cultured; D004261:DNA Replication; D005109:Extracellular Matrix / Q000032:analysis; D006020:Glycopeptides / Q000032:analysis*; D008970:Molecular Weight; D009131:Muscle, Smooth, Vascular / Q000166:cytology*; D013936:Thymidine / Q000378:metabolism; D014316:Tritium
D006020:Glycopeptides; D014316:Tritium; D013936:Thymidine