Abstract:
:Secretoneurin is a recently characterized neuropeptide present in the primary amino acid sequence of secretogranin II. We investigated the proteolytic processing of secretogranin II by prohormone convertases in vivo in a cellular system using the vaccinia virus system. Both PC1 and PC2 can cleave the secretogranin II precursor at sites of pairs of basic amino acids to yield intermediate-sized fragments. Other convertases like PACE4, PC5 and furin were not active. For the formation of the free neuropeptide secretoneurin a different pattern was found. Only PC1 but none of the other convertases tested including PC2 were capable of generating secretoneurin. Our results demonstrate that the prohormone convertases PC1 and PC2 are involved in proteolytic processing of secretogranin II. The neuropeptide secretoneurin can only be generated by PC1 suggesting tissue-specific processing of secretogranin II in neurons expressing different subsets of the prohormone convertases.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hoflehner J,Eder U,Laslop A,Seidah NG,Fischer-Colbrie R,Winkler Hdoi
10.1016/0014-5793(95)00127-usubject
Has Abstractpub_date
1995-03-06 00:00:00pages
294-8issue
3eissn
0014-5793issn
1873-3468pii
001457939500127Ujournal_volume
360pub_type
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