1993•Unpublished venueRequires access
cDNAstructure ofthemouseandratsubtilisin/kexin -like PC5:A candidate proprotein convertase expressed inendocrine and nonendocrine cells
Biochemical andtMolecular Neuroendocrinology
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Abstract
ABSTRACT Byusingreverse transcriptase/PCR andoli- gonucleotide sequences derived fromconserved segments (in- cluding the conserved RRGDLsequence) ofthe known pro-protein convertases (PCs) PC1, PC2, furin, and PC4, weidentifieda subtilisin/kexin-like PC cafled PC5in bothmouseand rat tissues. Thecompositestructure(2.85kb)wasdeducedfromthe analysis ofthe reverse transcription/PCR productscombinedwiththe sequence fromacloneisolatedfrom a cDNAlibrary madefrom corticotropin-activated mouse adrenocor- tical Y1 cells. ThededucedcDNAstructuresofmousePC5andrat PC5showed that the closest homologue is PACE4. Fur-thermore,like furin,Drosophila melanogaster(d) dfurin2, and PACE4, PC5 shows the presence of a C-terminal Cys-rich domain containing either 5 (PC5 andPACE4) or 10 (dfurin2) repeats of the consensus motif CYs-Xaa2-Cys-Xaa3-Cys- Xaa57-Cys-Xaa2-Cys-Xaas15-Cys-Xaa3-Cys-Xaag96. Therich- estsources of rat PC5mRNA (3.8kb) are theadrenalandgut,butitcanalsobedetectedinmanyendocrineandnonendocrinetissues. Corticotropin-stimulated adrenocortical Y1 cellsshowedanincreasedexpressionofPC5mRNA,suggesting anupregulation by cAMP. In situ