Abstract:
:Recombinant vaccinia virus vectors were used to coexpress each of the candidate prohormone convertases PC1, PC2, furin, PACE4 and PC5 with rat prosomatostatin (rProSOM) in the constitutive secreting cell line LoVo and in the endocrine corticotroph cell line AtT-20, which exhibits regulated secretion. Mammalian ProSOM is cleaved at a dibasic Arg-Lys decreases site to produce somatostatin-14 (S-14) and at a monobasic Gln-Arg decreases site to yield somatostatin-28 (S-28). The analysis of processed products by gel-permeation high performance liquid chromatography shows that in LoVo cells PC1, furin and PACE4 generate S-14, S-28 and a mixture of S-14 and S-28, respectively, while PC2 is unable to process ProSOM in these constitutive cells. In contrast, PC2 can generate S-14 in AtT-20 cells. The convertase PC5 is unable to process ProSOM in either cell line. These data suggest that PC2, PC1 and PACE4 are candidate S-14 convertases, while PACE4 and furin are candidate S-28 convertases.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Brakch N,Galanopoulou AS,Patel YC,Boileau G,Seidah NGdoi
10.1016/0014-5793(95)00229-3subject
Has Abstractpub_date
1995-04-03 00:00:00pages
143-6issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(95)00229-3journal_volume
362pub_type
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