Altered neuropeptide profile of Caenorhabditis elegans lacking the chaperone protein 7B2 as analyzed by mass spectrometry
Altered neuropeptide profile of Caenorhabditis elegans lacking the chaperone protein 7B2 as analyzed by mass spectrometry
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DOI：
10.1016/j.febslet.2007.08.003
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发表时间：
2007-09-04
期刊：
影响因子：
3.5
通讯作者：
Schoofs, Liliane
中科院分区：
文献类型：
--
作者：
Husson, Steven J.;Schoofs, Liliane
天然存在的生物活性肽的细胞合成需要前蛋白转化酶PC 2/EGL-3从较大的肽前体裂解。如在小鼠模型中广泛研究的，proPC 2的蛋白水解激活需要神经内分泌伴侣7132。为了确定其直向同源物在秀丽隐杆线虫中的作用，我们通过HPLC和基质辅助激光解吸电离飞行时间质谱法分析了野生型和7132无效菌株，从而鉴定了一种新的神经肽基因flp-33。7132缺失动物中某些神经肽的存在和/或不存在与野生型中的肽谱有很大不同，表明7132在C中具有特异性和确定的作用。优美的(c)2007年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Cellular synthesis of naturally occurring, bioactive peptides requires the proprotein convertase PC2/EGL-3 for cleavage from the larger peptide precursors. A neuroendocrine chaperone 7132 is needed for the proteolytical activation of proPC2, as extensively studied in mouse models. To determine the role of its orthologue in Caenorhabditis elegans, we analyzed wild-type and 7132-null strains by HPLC and matrix-assisted laser desorption ionization time-of-flight mass spectrometry, which allowed the identification of a novel neuropeptide gene, flp-33. The presence and/or absence of some neuropeptides in 7132-null animals strongly differs form the peptide profile in wild-type, suggesting a specific and determined action of 7132 in C. elegans. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.