On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissues.
On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissues.
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关于培养细胞和组织中早老素蛋白的虚假内切蛋白水解加工。
DOI：
10.1073/pnas.94.25.14031
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发表时间：
1997
影响因子：
11.1
通讯作者：
A. Nairn
中科院分区：
文献类型：
--
作者：
N. Dewji;Chau Do;A. J. Scheetz;A. Nairn
据广泛报道，早老素蛋白PS-1和PS-2在各种培养细胞和组织的提取物中被内源性蛋白水解加工事件广泛碎片化。一般认为，这种蛋白内溶是早老素表达后的生理正常细胞内事件，可能在这些分子与阿尔茨海默病相关的未知功能中发挥重要作用。然而，我们在此证明，如果在细胞损伤最小的条件下检查各种培养细胞和几种小鼠组织，则发现提取物中的早老素分子是完整的，但如果在更大的压力条件下制备细胞和组织，则观察到内蛋白水解片段。我们得出结论，这些特殊的蛋白内溶事件不是早老素生理正常处理的结果，而是在标本制备的共同过程中发生的人工产物。
It has been widely reported that the presenilin proteins PS-1 and PS-2 in extracts derived from a variety of cultured cells and from tissues are fragmented extensively by endoproteolytic processing events. It generally has been presumed that this endoproteolysis is a physiologically normal intracellular event following presenilin expression, which might play an important role in the still unknown functions of these molecules in connection with Alzheimer disease. We demonstrate herein, however, that, if a variety of cultured cells and several mouse tissues are examined under conditions minimizing cell trauma, the presenilin molecules in the extracts are found to be intact but that, if the cells and tissues are prepared under somewhat more stressful conditions, the endoproteolytic fragments are then observed. We conclude that these particular endoproteolytic events are not the result of physiologically normal processing of the presenilins but are rather artifacts occurring during the common procedures of specimen preparation.
影响因子：
56.9
作者：
BAILEY, CH;CHEN, M;KANDEL, ER
通讯作者：
KANDEL, ER
膜蛋白之间的特异性跨细胞结合对阿尔茨海默病至关重要。
DOI：
10.1073/pnas.93.22.12575
发表时间：
1996
影响因子：
11.1
作者：
Dewji,NN;Singer,SJ
通讯作者：
Singer,SJ