Wang Y M, Ingoglia N A
Department of Pharmacology and Physiology, New Jersey Medical School, UMDNJ, Newark 07103, USA.
Neurochem Res. 1997 Dec;22(12):1453-9. doi: 10.1023/a:1021998227237.
N-terminal protein arginylation has been demonstrated in vitro and in situ and has been reported to increase following injury to sciatic nerves of rats. The present study attempts to demonstrate these reactions in vivo by applying [3H]Arg to the cut end of sciatic nerves in anesthetized rats and assaying for N-terminal arginylation using Edman chemistry and acid precipitation of labeled proteins in the proximal nerve segment. No evidence was found for arginylation in an aqueous soluble fraction. However, N-terminal arginylation was detected in a urea soluble fraction at 2 hours after nerve crush. The data show that arginylation of rat sciatic nerve proteins occurs in vivo and suggest that the arginylated proteins formed an aqueous insoluble/urea soluble aggregate after arginylation. In other experiments, rat brains were injured and assayed for arginylation in vitro to test the hypothesis that injury causes an up-regulation of these reactions. Results showed an activation of the reaction at 2 hours post crush and indicate that increases in N-terminal arginylation are likely to be a general response to injury in nervous tissue.
N 端蛋白质精氨酰化已在体外和原位得到证实,据报道,大鼠坐骨神经损伤后该反应会增强。本研究试图通过向麻醉大鼠的坐骨神经切断端施加[3H]精氨酸,并使用埃德曼化学法和对近端神经节段中标记蛋白质进行酸沉淀来检测 N 端精氨酰化,从而在体内证实这些反应。在水溶性部分未发现精氨酰化的证据。然而,在神经挤压后 2 小时,在尿素可溶性部分检测到了 N 端精氨酰化。数据表明大鼠坐骨神经蛋白的精氨酰化发生在体内,提示精氨酰化后的蛋白形成了水不溶性/尿素可溶性聚集体。在其他实验中,对大鼠脑进行损伤并在体外检测精氨酰化,以检验损伤会导致这些反应上调的假说。结果显示挤压后 2 小时反应被激活,表明 N 端精氨酰化增加可能是神经组织损伤后的一种普遍反应。