CDNA STRUCTURE OF THE MOUSE AND RAT SUBTILISIN KEXIN-LIKE PC5 - A CANDIDATE PROPROTEIN CONVERTASE EXPRESSED IN ENDOCRINE AND NONENDOCRINE CELLS

CDNA STRUCTURE OF THE MOUSE AND RAT SUBTILISIN KEXIN-LIKE PC5 - A CANDIDATE PROPROTEIN CONVERTASE EXPRESSED IN ENDOCRINE AND NONENDOCRINE CELLS
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DOI:
10.1073/pnas.90.14.6691
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发表时间:
1993-07-15
影响因子:
11.1
通讯作者:
SEIDAH, NG
SEIDAH, NG
中科院分区:
综合性期刊1区
文献类型:
--
作者:
LUSSON, J;VIEAU, D;SEIDAH, NG

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通过使用逆转录酶/PCR和从已知蛋白转化酶PC1、PC2、furin和PC4的保守片段(包括保守的RRGDL序列)衍生的寡核苷酸序列,我们在小鼠和大鼠组织中鉴定了一种名为PC5的枯草杆菌素/键合蛋白样PC。从促肾上腺皮质激素激活小鼠肾上腺皮质Y1细胞cDNA文库中分离的克隆序列,通过反转录/PCR产物分析,推断出复合结构(2.85 kb)。小鼠PC5和大鼠PC5的cDNA结构分析表明,最接近的同源基因是PACE4。此外,与furin、Drosophila melanogaster (d) dfurin2和PACE4一样,PC5显示出c端富含cys结构域的存在,该结构域含有5个(PC5和PACE4)或10个(dfurin2)重复的共识基序cys - xa02 - cys - xaa3 - cys - xaa5 -7- cys - xaa2 - cys - xaa8 -15- cys - xaa3 - cys - xaa9 -16。大鼠PC5 mRNA (3.8 kb)最丰富的来源是肾上腺和肠道,但它也可以在许多内分泌和非内分泌组织中检测到。促肾上腺皮质激素刺激的肾上腺皮质Y1细胞显示PC5 mRNA表达增加,提示cAMP上调。与PC1、PC2和furin相比,大鼠脑切片的原位杂交显示PC5的独特分布。
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-Xaa5-7-Cys-Xaa2-Cys-Xaa8-15-Cys-Xaa3-Cys-Xaa9-16. 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.