title: cDNA structure of the mouse and rat subtilisin/kexin-like PC5: a candidate proprotein convertase expressed in endocrine and nonendocrine cells.
abstract: By using reverse transcriptase/PCR and oligonucleotide sequences derived from conserved segments (including the conserved RRGDL sequence) of the known proprotein convertases (PCs) PC1, PC2, furin, and PC4, we identified a subtilisin/kexin-like PC called PC5 in both mouse and rat tissues. The composite structure (2.85 kb) was deduced from the analysis of the reverse transcription/PCR products combined with the sequence from a clone isolated from a cDNA library made from corticotropin-activated mouse adrenocortical Y1 cells. The deduced cDNA structures of mouse PC5 and rat PC5 showed that the closest homologue is PACE4. Furthermore, like furin, Drosophila melanogaster (d) dfurin2, and PACE4, PC5 shows the presence of a C-terminal Cys-rich domain containing either 5 (PC5 and PACE4) or 10 (dfurin2) repeats of the consensus motif Cys-Xaa2-Cys-Xaa3-Cys-Xaa(5-7)-Cys-Xaa2-Cys-Xaa (8-15)-Cys-Xaa3-Cys-Xaa(9-16). The richest sources of rat PC5 mRNA (3.8 kb) are the adrenal and gut, but it can also be detected in many endocrine and nonendocrine tissues. Corticotropin-stimulated adrenocortical Y1 cells showed an increased expression of PC5 mRNA, suggesting an upregulation by cAMP. In situ hybridization of rat brain sections demonstrated a unique distribution of PC5 compared to PC1, PC2, and furin.
authors.affiliation: J. A. DeSève Laboratorie of Biochemical Neuroendocrinology, Clinical Research Institute of Montreal, PQ, Canada.
authors.forename: J
authors.initials: J
authors.lastname: Lusson
authors.forename: D
authors.initials: D
authors.lastname: Vieau
authors.forename: J
authors.initials: J
authors.lastname: Hamelin
authors.forename: R
authors.initials: R
authors.lastname: Day
authors.forename: M
authors.initials: M
authors.lastname: Chrétien
authors.forename: N G
authors.initials: NG
authors.lastname: Seidah
mesh_terms: D000311:Adrenal Glands / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001923:Brain Chemistry; D017403:In Situ Hybridization; D051379:Mice; D008969:Molecular Sequence Data; D045702:Proprotein Convertase 5; D043484:Proprotein Convertases; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012333:RNA, Messenger / Q000235:genetics* / Q000302:isolation & purification; D051381:Rats; D029701:Saccharomyces cerevisiae Proteins; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics* / Q000302:isolation & purification; D013381:Subtilisins / Q000235:genetics; D014018:Tissue Distribution
chemical_list: D011498:Protein Precursors; D012333:RNA, Messenger; D029701:Saccharomyces cerevisiae Proteins; C513086:Pcsk6 protein, mouse; C513087:Pcsk6 protein, rat; D045702:Proprotein Convertase 5; D043484:Proprotein Convertases; D012697:Serine Endopeptidases; D013381:Subtilisins; C473805:propeptide convertase 5, mouse; C473807:propeptide convertase 5, rat; C058751:KEX2 protein, S cerevisiae