TY - JOUR
T1 - C-terminal KDEL-modified cystatin C is retained in transfected CHO cells
AU - Johansen, Teit Eliot
AU - Vogel, Charlotte Katrine
AU - Schwartz, Thue W.
N1 - Keywords: Amino Acid Sequence; Animals; Base Sequence; Cell Line; Chromatography, Gel; Cricetinae; Cricetulus; Cystatin C; Cystatins; DNA; Endoplasmic Reticulum; Molecular Sequence Data; Mutation; Transfection
PY - 1990
Y1 - 1990
N2 - 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.
AB - 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.
U2 - 10.1016/0006-291X(90)91603-P
DO - 10.1016/0006-291X(90)91603-P
M3 - Journal article
C2 - 2244918
SN - 0006-291X
VL - 172
SP - 1384
EP - 1391
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -