Cell adhesive activity of two animal lectins through different recognition mechanisms

FEBS Letters

Ozeki, Yasuhiro¹  Titani, Koiti¹  Matsui, Taei¹ 

[1] Institute for Comprehensive Medical Science, Fujita Health University School of Medicine, Toyoake, Aichi 470-11, Japan

关键词: β-Galactoside binding lectin;    Echinoidin;    Cell adhesion;    Integrin;    Human rhabdomyosarcoma cell;   

DOI  :  10.1016/0014-5793(91)81055-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cell adhesive activity of two animal lectins. frog (Rama 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 coatce 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.

【 授权许可】

Unknown