C-TERMINAL KDEL-MODIFIED CYSTATIN-C IS RETAINED IN TRANSFECTED CHO CELLS

被引：14

作者：

JOHANSEN, TE

VOGEL, CK

SCHWARTZ, TW

机构：

[1] Laboratory of Molecular Endocrinology, University Department of Clinical Chemistry, Rigshospitalet 6321, DK-2100 Copenhagen

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 172卷 / 03期

关键词：

D O I：

10.1016/0006-291X(90)91603-P

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：

The significance of a C-terminal tetrapeptide, Lys-Asp-Glu-Leu (KDEL), as a retention signal for the endoplasmatic reticulum was studied using cystatin C, a general thiol protease inhibitor, as the reporter protein. Clones of CHO cells were analyzed after stable transfection with eukaryotic expression vectors encoding either cystatin C, KDEL extended cystatin C, or cystatin C extended with a control sequence. It is concluded that cystatin C with the KDEL tetrapeptide as a C-terminal extension is retained intracellularly without apparent accumulation of the molecule. © 1990.

引用

页码：1384 / 1391

页数：8

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