C8, a new member of the convertase family

Angela Bruzzaniti, Katrina Goodge, Philippe Jay, Sylvie A. Taviaux, Mark H.C. Lam, Philippe Berta, T. John Martin, Jane M. Moseley, Matthew T. Gillespie

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Abstract

A novel subtilisin-like protein, PC8, was identified by PCR using degenerate primers to conserved amino acid residues in the catalytic region of members of the prohormone convertase family. PC8 was predicted to be 785 residues long and was structurally related to the mammalian convertases furin, PACE4, PC1 and PC2, sharing more than 50% amino acid identity over the catalytic region with these family members. PC8 possessed the catalytically important Asp, His, Asn and Ser amino acids, the homo B domain of this family of enzymes and a C-terminal hydrophobic sequence indicative of a transmembrane domain. Structurally, PC8 is more related to furin and PACE4 than to PC1 or PC2. Like furin and PACE4, PC8 mRNA was found to be widely expressed; this is in contrast with PC1 and PC2, which have a restricted distribution. Two transcripts, of 4.5 and 3.5 kb, were detected in both human cell lines and rat tissues. Unlike furin and PACE4, both of which map to chromosome 15, PC8 maps to chromosome 11q23-11q24, suggesting that this gene may have resulted from an ancient gene duplication event from either furin or PACE4, or conversely that these genes arose from PC8.

Original languageEnglish (US)
Pages (from-to)727-731
Number of pages5
JournalBiochemical Journal
Volume314
Issue number3
DOIs
StatePublished - Mar 15 1996

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Bruzzaniti, A., Goodge, K., Jay, P., Taviaux, S. A., Lam, M. H. C., Berta, P., Martin, T. J., Moseley, J. M., & Gillespie, M. T. (1996). C8, a new member of the convertase family. Biochemical Journal, 314(3), 727-731. https://doi.org/10.1042/bj3140727