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Processing of prodynorphin by the prohormone convertase PC1 results in high molecular weight intermediate forms
Author(s) -
Dupuy A.,
Lindberg I.,
Zhou Y.,
Akil H.,
Lazure C.,
Chrétien M.,
Seidah N.G.,
Day R.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80630-6
Subject(s) - prohormone convertase , prohormone , dynorphin , proenkephalin , biochemistry , chemistry , in vitro , recombinant dna , arginine , yield (engineering) , cleavage (geology) , exopeptidase , biology , peptide , gene , hormone , enkephalin , receptor , opioid peptide , metallurgy , paleontology , materials science , amino acid , fracture (geology) , opioid
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.