TIGHT FOLDING OF ACIDIC FIBROBLAST GROWTH-FACTOR PREVENTS ITS TRANSLOCATION TO THE CYTOSOL WITH DIPHTHERIA-TOXIN AS VECTOR

被引：73

作者：

WIEDLOCHA, A ^{[1
]}

MADSHUS, IH ^{[1
]}

MACH, H ^{[1
]}

MIDDAUGH, CR ^{[1
]}

OLSNES, S ^{[1
]}

机构：

[1] MERCK SHARP & DOHME LTD,W POINT,PA 19486

来源：

EMBO JOURNAL | 1992年 / 11卷 / 13期

关键词：

ACIDIC FIBROBLAST GROWTH FACTOR; DIPHTHERIA TOXIN; MEMBRANE TRANSLOCATION;

D O I：

10.1002/j.1460-2075.1992.tb05589.x

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：

A fusion protein of acidic fibroblast growth factor and diphtheria toxin A-fragment was disulfide-linked to the toxin B-fragment. The complex bound specifically to diphtheria toxin receptors, and subsequent exposure to low pH induced the fusion protein to translocate to the cytosol. Heparin, inositol hexaphosphate and inorganic sulfate strongly increased the trypsin resistance of the growth factor part of the fusion protein, indicating tight folding, and they prevented translocation of the fusion protein to the cytosol. The data indicate that only a more disordered form of the growth factor is translocation competent.

引用

页码：4835 / 4842

页数：8

共 52 条

[51] 3-DIMENSIONAL STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH-FACTOR, A STRUCTURAL HOMOLOG OF INTERLEUKIN-1-BETA [J].