Cell adhesive activity of two animal lectins through different recognition mechanisms.
Cell adhesive activity of two animal lectins, frog (Rana catesbeiana) S-type 14K lectin and echinoidin (a C-type lectin from sea urchin plasma), was studied with human rhabdomyosarcoma (RD) cells. RD cells attached to and spread on plastic plates coated with each lectin. Cell adhesion by the frog lectin was completely inhibited by the addition of lactose or asialofetuin glycopeptide. Echinoidin-induced cell adhesion was only inhibited by peptide GRGDS. Since echinoidin is known to contain an RGD-sequence, our results clearly indicate that this sequence is active as the cell adhesive signal. These results suggest that some of the animal lectins may function as a cell adhesive molecule rather than using the carbohydrate-recognition mechanism.
Ozeki
Y
Y
Institute for Comprehensive Medical Science, Fujita Health University School of Medicine, Aichi, Japan.
Matsui
T
T
Titani
K
K
D000595:Amino Acid Sequence; D000818:Animals; D002240:Carbohydrate Sequence; D002448:Cell Adhesion / Q000187:drug effects*; D005947:Glucose / Q000494:pharmacology; D006384:Hemagglutination / Q000187:drug effects; D006801:Humans; D007785:Lactose / Q000494:pharmacology; D037102:Lectins; D008969:Molecular Sequence Data; D009842:Oligopeptides; D009844:Oligosaccharides; D011892:Rana catesbeiana; D012208:Rhabdomyosarcoma; D012617:Sea Urchins; D014407:Tumor Cells, Cultured
D037102:Lectins; D009842:Oligopeptides; D009844:Oligosaccharides; C052278:echinoidin; D005947:Glucose; D007785:Lactose