Processing of prodynorphin by the prohormone convertase PC1 results in high molecular weight intermediate forms

FEBS Letters

Dupuy, A.²  Lindberg, I.¹  Lazure, C.²  Chrétien, M.²  Day, R.²  Seidah, N.G.²  Zhou, Y.¹  Akil, H.³ 

[1] Biochemistry and Molecular Biology Department, Louisiana State University Medical Center, New Orleans, LA 70112, USA;J.A. DeSève Laboratory of Biochemical Neuroendocrinology, Clinical Research Institute of Montreal, 110 Pine Avenue West, Montreal, Quebec H2W 1R7, Canada;Mental Health Research Institute, University of Michigan, Ann Arbor, MI 48109, USA

关键词: Vaccinia virus;    Dynorphin;    Processing;    Overexpression;    PC12 cell;   

DOI  :  10.1016/0014-5793(94)80630-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Processing of rat prodynorphin (proDyn) by the mouse prohormone convertase PCI was investigated. Recombinant vaccinia virus vectors were used to coexpress proDyn and PC1 in rat PC12 pheochromocytoma and mouse AtT-20 corticotroph cells. In vitro experiments were also conducted by co-incubating purified proDyn and PC1. The results demonstrate that PC1 cleaves proDyn at pairs of basic residues to yield 10 and 16 kDa high molecular weight (HMW) intermediates. Additionally, PC1 cleaves proDyn at a single arginine residue to yield an 8 kDa product and the C-peptide. This demonstrates that PC1 cleaves proDyn at single and pairs of basic residues.

【 授权许可】

Unknown