C-terminal KDEL-modified cystatin C is retained in transfected CHO cells
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | Biochemical and Biophysical Research Communications |
Volume | 172 |
Issue number | 3 |
Pages (from-to) | 1384-91 |
Number of pages | 7 |
ISSN | 0006-291X |
DOIs | |
Publication status | Published - 1990 |
Bibliographical note
Keywords: Amino Acid Sequence; Animals; Base Sequence; Cell Line; Chromatography, Gel; Cricetinae; Cricetulus; Cystatin C; Cystatins; DNA; Endoplasmic Reticulum; Molecular Sequence Data; Mutation; Transfection
ID: 9747045