C-terminal KDEL-modified cystatin C is retained in transfected CHO cells

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 -