PrP27-30 is a normal soluble prion protein fragment released by human platelets.
PrP27-30 is a normal soluble prion protein fragment released by human platelets.
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PrP27-30 是人血小板释放的正常可溶性朊病毒蛋白片段。
DOI：
10.1006/bbrc.1996.0936
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Prelli,F
中科院分区：
文献类型：
--
作者：
Perini,F;Vidal,R;Ghetti,B;Tagliavini,F;Frangione,B;Prelli,F
朊病毒病是一种神经退行性疾病，其特征是朊病毒蛋白（PrPSc）异常亚型在中枢神经系统中的积累。PrPS同功异型体与其正常同源物（PrPC）的不同之处在于它们具有增加的β-折叠构象，是部分蛋白酶抗性的，并且可能与淀粉样蛋白沉积有关。淀粉样蛋白被认为来源于存在于生物流体中的可溶性前体或其片段，其在疾病状态下经历构象变化，导致聚集和沉积在靶组织中。我们在这里报告，血小板携带PrP mRNA和释放PrPC，唾液酸糖蛋白结合到细胞表面的糖基磷脂酰肌醇（GPI）锚。可溶性PrPC和N-末端截短PrPC亚型从位置90开始由静息和激动剂刺激的血小板分泌，并且在释放物部分去糖基化后可检测到。可溶性27-30 kDa同种型GQGGGTHSQ（W）NKP的N-末端序列分析显示与羊瘙痒病PrP 27 -30（源自PrPSc的蛋白酶抗性核心）同源。这些发现表明，除了PrPC，血小板加工可溶性PrP 27 - 30亚型。该亚型能否转化为羊瘙痒病PrP 27 - 30尚待确定。
Prion diseases are neurodegenerative disorders characterized by the accumulation of abnormal isoforms of prion protein (PrPSc) in the central nervous system. PrPScisoforms differ from their normal homologue (PrPC), in that they possess increased β-sheet conformation, are partially protease resistant and may be associated with amyloid deposition. Amyloid proteins are thought to derive from soluble precursors or fragments thereof, present in biological fluids, which in the disease state undergo conformational change leading to aggregation and deposition in target tissues. We report here that platelets carry PrP mRNA and release PrPC, a sialoglycoprotein bound to the cell surface by a glycosylphosphatidylinositol (GPI) anchor. Soluble PrPCand a N-terminal truncated PrPCisoform starting at position 90 are secreted by resting and agonist-stimulated platelets and are detectable after partial deglycosylation of releasates. N-terminal sequence analysis of the soluble 27–30 kDa isoform, GQGGGTHSQ(W)NKP, revealed homology to scrapie PrP27–30, the protease resistant core derived from PrPSc. These findings indicate that in addition to PrPC, platelets process a soluble PrP27–30isoform. Whether this isoform can be converted into scrapie PrP27–30remains to be determined.