論文 - 詳細
| RRC ID | 58257 |
|---|---|
| 著者 | Nagahama M, Taniguchi T, Hashimoto E, Imamaki A, Mori K, Tsuji A, Matsuda Y. |
| タイトル | Biosynthetic processing and quaternary interactions of proprotein convertase SPC4 (PACE4). |
| ジャーナル | FEBS Lett |
| Abstract |
SPC4 (PACE4), a member of the eukaryotic family of subtilisin-like proprotein convertases, is synthesized as a proenzyme (proSPC4) which undergoes proteolytic removal of N-terminal propeptide during transit through the secretory pathway. As this propeptide processing seems to be a key event in the functional expression of SPC4, we have investigated its mechanism and the intracellular site where it occurs. In transfected fibroblast cells, the 110-kDa proSPC4 undergoes slow cleavage to generate a 103-kDa mature enzyme in the endoplasmic reticulum (ER). Site-directed mutagenesis studies demonstrate that the proteolytic activation of SPC4 occurs mainly through a unimolecular autocatalytic process and propeptide cleavage is a prerequisite for its export from the ER. Sedimentation velocity and chemical cross-linking analysis demonstrate that the precursor protein in the cells exists as both a monomer and a dimer-sized complex whereas mature SPC4 exists only as a monomer. These results suggest that the cleavage of the N-terminal propeptide of SPC4 plays a regulatory role in its activation and secretion through the change in its oligomeric state. |
| 巻・号 | 434(1-2) |
| ページ | 155-9 |
| 公開日 | 1998-8-28 |
| DOI | 10.1016/s0014-5793(98)00970-3 |
| PII | S0014-5793(98)00970-3 |
| PMID | 9738469 |
| MeSH | Animals Cell Line Humans Isoenzymes / biosynthesis* Isoenzymes / chemistry Proprotein Convertases Protein Conformation* Protein Processing, Post-Translational Serine Endopeptidases / biosynthesis* Serine Endopeptidases / chemistry |
| IF | 3.057 |
| 引用数 | 27 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | Patent(IFI CLAIMS) |
| 各媒体での言及数の合計 | 1 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 遺伝子材料 | Human PACE4 cDNA (RDB02938) |