Cytotoxicity of ribosome-inactivating protein saporin is not mediated through α2-macroglobulin receptor

被引：26

作者：

Bagga, S

Hosur, MV

Batra, JK

机构：

[1] Natl Inst Immunol, Immunochem Lab, New Delhi 110067, India

[2] Bhabha Atom Res Ctr, Div Solid State Phys, Bombay 400085, Maharashtra, India

来源：

FEBS LETTERS | 2003年 / 541卷 / 1-3期

关键词：

ribosome-inactivating protein; toxin; ribosome; inummotoxin; ribotoxin;

D O I：

10.1016/S0014-5793(03)00280-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Saporin is a single chain ribosome-inactivating protein produced by the plant Saponaria officinalis. Several isoforms of saporin have been isolated from various parts of the plant. In the present study recombinant saporin isoforms 5 and 6 were produced in Escherichia coli. Saporin-6 was found to be more active than saporin-5 in its N-glycosidase, cytotoxic, and genomic DNA fragmentation activities. Earlier, saporin has been shown to bind low-density lipoprotein receptor-related protein (LRP), however, in this study the sensitivities of LRP-negative and LRP-positive cell lines were found to be similar towards saporin-6 toxicity suggesting the internalization of saporin not to be solely dependent on the expression of LRP on eukaryotic cells. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：16 / 20

页数：5

共 29 条

[1] The cytotoxic activity of ribosome-inactivating protein saporin-6 is attributed to its rRNA N-glycosidase and internucleosomal DNA fragmentation activities [J].