Seidah N G, Fournier H, Boileau G, Benjannet S, Rondeau N, Chrétien M
J.A. DeSève Laboratories of Biochemical, Clinical Research Institute of Montreal, Que., Canada.
FEBS Lett. 1992 Oct 5;310(3):235-9. doi: 10.1016/0014-5793(92)81339-n.
The complete cDNA structure of the porcine (p) pro-protein and pro-hormone convertase PC2 (pPC2) was obtained from a cDNA library of pituitary neurointermediate lobes mRNA. The deduced amino acid sequence revealed that pPC2 exhibits a 99-97% sequence identity to the human, mouse and rat homologues. The 3' end of the 2.1 kb cDNA is the least conserved segment. On Northern blots of pars intermedia poly A+ RNA two transcripts of 3 and 5 kb were detected. Molecular analysis of the N-terminal glycopeptide products of porcine pro-opiomelanocortin (pPOMC) co-expressed with vaccinia virus recombinants of PC1 or PC2, revealed that in cells devoid or containing secretory granules both convertases can cleave pPOMC with PC1 releasing the 1-80, 1-107 and 1-148 glycopeptide fragments, and PC2 cleaving pPOMC directly into pPOMC 1-107.
猪(p)前体蛋白和前激素转化酶PC2(pPC2)的完整cDNA结构是从垂体神经中间叶mRNA的cDNA文库中获得的。推导的氨基酸序列显示,pPC2与人、小鼠和大鼠的同源物具有99 - 97%的序列同一性。2.1 kb cDNA的3'端是保守性最低的区段。在中间部多聚A + RNA的Northern印迹上检测到3 kb和5 kb的两种转录本。对与PC1或PC2的痘苗病毒重组体共表达的猪阿黑皮素原(pPOMC)的N端糖肽产物进行分子分析,结果显示,在没有或含有分泌颗粒的细胞中,两种转化酶都能切割pPOMC,PC1释放出1 - 80、1 - 107和1 - 148糖肽片段,而PC2则将pPOMC直接切割成pPOMC 1 - 107。