Peptidomic analysis of human cell lines.

Peptidomic analysis of human cell lines.
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DOI:
10.1021/pr100952f
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发表时间:
2011-04-01
影响因子:
4.4
通讯作者:
Fricker, Lloyd D.
Fricker, Lloyd D.
中科院分区:
生物学2区
文献类型:
--
作者:
Gelman, Julia S.;Sironi, Juan;Castro, Leandro M.;Ferro, Emer S.;Fricker, Lloyd D.

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肽被认为在细胞质内的细胞内信号传导中发挥作用。尽管细胞质中的肽被认为是高度不稳定的,但在小鼠大脑和其他生物样本中已经检测到大量的肽。在本研究中,我们评估了三种不同细胞系(SH - SY5Y、MCF7和HEK293细胞)的肽组。对肽组的比较显示,在每种细胞系中发现的肽的身份有相当大的重叠。观察到的大多数肽并非来自细胞中最丰富或最不稳定的蛋白质,并且大约一半的细胞肽对应于前体蛋白质的N - 末端或C - 末端。切割位点分析显示在P1位置偏好疏水残基。定量肽组分析表明,大多数细胞肽的水平不会因细胞内钙升高而改变,这表明钙蛋白酶与它们的产生无关。三种细胞系肽组的相似性以及与预测的细胞降解组缺乏相关性意味着这些肽是选择性形成或保留的,这与它们在细胞中具有功能的假设是一致的。
Peptides have been proposed to function in intracellular signaling within the cytosol. Although cytosolic peptides are considered to be highly unstable, a large number of peptides have been detected in mouse brain and other biological samples. In the present study, we evaluated the peptidome of three diverse cell lines: SH-SY5Y, MCF7, and HEK293 cells. A comparison of the peptidomes revealed considerable overlap in the identity of the peptides found in each cell line. The majority of the observed peptides are not derived from the most abundant or least stable proteins in the cell, and approximately half of the cellular peptides correspond to the N- or C- termini of the precursor proteins. Cleavage site analysis revealed a preference for hydrophobic residues in the P1 position. Quantitative peptidomic analysis indicated that the levels of most cellular peptides are not altered in response to elevated intracellular calcium, suggesting that calpain is not responsible for their production. The similarity of the peptidomes of the three cell lines and the lack of correlation with the predicted cellular degradome implies the selective formation or retention of these peptides, consistent with the hypothesis that they are functional in the cells.
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