Effects of propeptide deletion on human renin secretion from mouse pituitary AtT‐20 cells

FEBS Letters

Nagahama, Masami²  Murakami, Kazuo²  Nakayama, Kazuhisa¹ 

[1] Institute of Biological Sciences, University of Tsukuba, Tsukuba, Ibaraki 305, Japan;Institute of Applied Biochemistry, University of Tsukuba, Tsukuba, Ibaraki 305, Japan

关键词: Renin;    Propeptide;    Oligonucleotide-directed mutagenesis;    Protein folding;    AtT-20 cell;    CHO;    Chinese hamster ovary;    DMEM;    Dulbecco's modified Eagle's medium;    FCS;    fetal calf serum;    AngI;    angiotensin I;   

DOI  :  10.1016/0014-5793(90)80766-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To study the role of the N-tenninal propeptide in the secretory process of renin, mouse pituitary AtT-20 cells were transfected with expression plasmids of human preprorenin and a mutant deleted of its propeptide. The transfectant of the native construct secreted inactive prorenin and active renin, and renin secretion was stimulated by a secretagogue, 8-Br-cAMP. On the contrary, the transfectant of the deleted construct secreted only active renin, whose release was also stimulated by the secretagogue. The amount of renin molecule secreted from the latter transfectant was lower than that from the former one, although a significant amount of fully active renin could be produced. These results suggest that the propeptide plays an important role in the secretory process of renin, probably folding and/or stabilizing the renin molecule, but it does not contain the signal for intracellular sorting to target renin to secretory granules.

【 授权许可】

Unknown