Cytotoxic activities of a fusion protein comprised of TGFα and Pseudomonas exotoxin
Cytotoxic activities of a fusion protein comprised of TGFα and Pseudomonas exotoxin
复制标题
由 TGFα 和假单胞菌外毒素组成的融合蛋白的细胞毒活性
DOI：
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发表时间：
1989
期刊：
影响因子：
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通讯作者：
I. Pastan
中科院分区：
文献类型：
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作者：
C. Siegall;Yong Hua Xu;V. Chaudhary;S. Adhya;D. FitzGerald;I. Pastan
A cDNA encoding transforming growth factor type alpha (TGFα) was fused to the 5' end of a gene encoding a modified form of Pseudomonas exotoxin A (PE), which is devoid of the cell recognition domain (domain Ia). The chimeric molecule, termed TGFα‐PE40, was expressed in Escherichia coli and isolated from the periplasm or inclusion bodies depending on the construction expressed. TGFα‐PE40 was found to be extremely cytotoxic to cells displaying epidermal growth factor (EGF) receptors. Comparison with a similar molecule in which TGFa was placed at the carboxyl end of PE40 demonstrated the importance of the position of the cell recognition element; TGFα‐PE40 was found to be about 30‐fold more cytotoxic to cells bearing EGF receptors than PE40‐TGFα. In addition, TGFα‐PE40 was shown to be extremely cytotoxic to a variety of cancer cell lines including liver, ovarian, and colon cancer cell lines, indicating high levels of EGF receptor expression in these cells.—Siegall, C. B.; Xu, Y.‐H.; Chaudhary, V. K.; Adhya, S.; FitzGerald, D.; Pastan, I. Cytotoxic activities of a fusion protein comprised of TGFα and Pseudomonas exotoxin. FASEB J. 3: 2647‐2652; 1989.
影响因子：
11.2
作者：
J. B. Santon;M. Cronin;C. Macleod;J. Mendelsohn;H. Masui;G. Gill
通讯作者：
J. B. Santon;M. Cronin;C. Macleod;J. Mendelsohn;H. Masui;G. Gill