Nonenzymatic glycation alters properties of collagen as a substratum for cells.
Acid-soluble collagen from rat skin was glycated in vitro by incubating with 0.2 M D-ribose at 37 degrees C for several days, and properties of the glycated collagen as a substratum for fibroblasts 3 Y 1 were studied. The cells attached but spread poorly on the glycated collagen as compared with on the untreated collagen. Thymidine incorporation by the cells on the glycated collagen was higher than that by the cells on untreated collagen. These results indicate that the glycation significantly alters properties of collagen as a substratum for cells.
Kawano
E
E
Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture, Japan.
Takahashi
S
S
Sakano
Y
Y
Fujimoto
D
D
D000818:Animals; D002241:Carbohydrates / Q000494:pharmacology; D002448:Cell Adhesion; D003094:Collagen / Q000187:drug effects* / Q000494:pharmacology; D046508:Culture Techniques; D004261:DNA Replication / Q000187:drug effects; D005347:Fibroblasts / Q000166:cytology* / Q000378:metabolism / Q000648:ultrastructure; D006031:Glycosylation; D010969:Plastics; D051381:Rats
D002241:Carbohydrates; D010969:Plastics; D003094:Collagen