IDENTIFICATION OF GLYCOINOSITOL PHOSPHOLIPID LINKED AND TRUNCATED FORMS OF THE SCRAPIE PRION PROTEIN
IDENTIFICATION OF GLYCOINOSITOL PHOSPHOLIPID LINKED AND TRUNCATED FORMS OF THE SCRAPIE PRION PROTEIN
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DOI：
10.1021/bi00490a001
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发表时间：
1990-09-25
期刊：
影响因子：
2.9
通讯作者：
PRUSINER, SB
中科院分区：
文献类型：
--
作者：
STAHL, N;BALDWIN, MA;PRUSINER, SB
对仓鼠朊病毒蛋白的痒病同种型的内切蛋白酶Lys-C酶衍生的羧基末端肽的分析表明，大多数分子是通过在丝氨酸-231处连接的乙醇胺连接的糖肌醇磷脂。然而，. apprx. 15%的PrPSc具有终止于甘氨酸-228的羧基末端肽。有趣的是，该甘氨酸是PrP序列Gly-Arg-Arg的一部分，该序列是用于蛋白水解和从较大前体释放生物活性肽的既定靶序列。其形成机制以及截短的羧基末端在羊瘙痒病传播和神经病理学中的作用仍有待确定。
Analysis of carboxy-terminal peptides derived from endoproteinase Lys-C digests of the scrapie isoform of the hamster prion protein revealed that the majority of the molecules are glycoinositol phospholipid linked through ethanolamie attached at serine-231. However, .apprx. 15% of PrPSc had a carboxy-terminal peptide that ends at glycine-228. It is intriguing that this glycine is part of the PrP sequence Gly-Arg-Arg, which is an established target sequence for the proteolysis and release of bioactive peptides from larger precursors. The mechanism of formation, as well as the role of the truncated carboxy terminus in the dissemination and neuropathology of scrapie, remains to be determined.