Cloning and functional expression of a novel endoprotease involved in prohormone processing at dibasic sites.
We cloned and sequenced a cDNA from a library of mouse pituitary AtT-20 cells which are known to cleave an endogenous and various foreign prohormones at dibasic sites. This cDNA encodes a novel 753-residue protein, named PC3, which is structurally related to the yeast Kex2 protease involved in precursor cleavage at dibasic sites and to recently identified mammalian Kex2-like proteins, furin and PC2. Among examined cell lines and tissues, PC3 mRNA was only detected in AtT-20 cells. The substrate specificity of PC3 expressed in mammalian cells was similar to that observed in AtT-20 cells. We conclude that PC3 is a resident prohormone processing endoprotease in AtT-20 cells.
Nakayama
K
K
Institute of Biological Sciences, University of Tsukuba, Ibaraki.
Hosaka
M
M
Hatsuzawa
K
K
Murakami
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D015971:Gene Expression Regulation, Enzymologic; D006728:Hormones / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D011333:Pro-Opiomelanocortin / Q000096:biosynthesis / Q000235:genetics*; D043484:Proprotein Convertases; D011956:Receptors, Cell Surface / Q000378:metabolism; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
D006728:Hormones; D011956:Receptors, Cell Surface; D011333:Pro-Opiomelanocortin; D004247:DNA; D043484:Proprotein Convertases; D012697:Serine Endopeptidases