Department of Chemistry and the Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana 61801, USA.
Analyst. 2017 Nov 20;142(23):4476-4485. doi: 10.1039/c7an01358b.
Measurement, identification, and quantitation of endogenous peptides in tissue samples by mass spectrometry (MS) contribute to our understanding of the complex molecular mechanisms of numerous biological phenomena. For accurate results, it is essential to arrest the postmortem degradation of ubiquitous proteins in samples prior to performing peptidomic measurements. Doing so ensures that the detection of endogenous peptides, typically present at relatively low levels of abundance, is not overwhelmed by protein degradation products. Heat stabilization has been shown to inactivate the enzymes in tissue samples and minimize the presence of protein degradation products in the subsequent peptide extracts. However, the efficacy of different heat treatments to preserve the integrity of full-length endogenous peptides has not been well documented; prior peptidomic studies of heat stabilization methods have not distinguished between the full-length (mature) and numerous truncated (possible artifacts of sampling) forms of endogenous peptides. We show that thermal sample treatment via rapid conductive heat transfer is effective for detection of mature endogenous peptides in fresh and frozen rodent brain tissues. Freshly isolated tissue processing with the commercial Stabilizor T1 heat stabilization system resulted in the confident identification of 65% more full-length mature neuropeptides compared to widely used sample treatment in a hot water bath. This finding was validated by a follow-up quantitative multiple reaction monitoring MS analysis of select neuropeptides. The rapid conductive heating in partial vacuum provided by the Stabilizor T1 effectively reduces protein degradation and decreases the chemical complexity of the sample, as assessed by determining total protein content. This system enabled the detection, identification, and quantitation of neuropeptides related to 22 prohormones expressed in individual rat hypothalami and suprachiasmatic nuclei.
通过质谱(MS)测量、识别和定量组织样品中的内源性肽,有助于我们理解许多生物现象的复杂分子机制。为了获得准确的结果,在进行肽组学测量之前,必须阻止样品中普遍存在的蛋白质的死后降解。这样可以确保检测到内源性肽,这些肽通常丰度相对较低,而不会被蛋白质降解产物所淹没。热稳定化已被证明可以使组织样品中的酶失活,并最大限度地减少随后的肽提取物中蛋白质降解产物的存在。然而,不同的热处理方法对保持全长内源性肽完整性的效果尚未得到很好的记录;先前的热稳定化方法的肽组学研究没有区分全长(成熟)和许多截断(采样可能的人工产物)形式的内源性肽。我们表明,通过快速传导热传递进行热样品处理,可有效检测新鲜和冷冻啮齿动物脑组织中的成熟内源性肽。与广泛使用的热水浴样品处理相比,使用商业 Stabilizor T1 热稳定化系统对新鲜分离的组织进行处理,可使全长成熟神经肽的鉴定增加 65%。通过对选定神经肽进行后续定量多重反应监测 MS 分析,验证了这一发现。Stabilizor T1 提供的部分真空下的快速传导加热可有效减少蛋白质降解并降低样品的化学复杂性,通过测定总蛋白质含量来评估。该系统能够检测、鉴定和定量与单个大鼠下丘脑和视交叉上核中表达的 22 种前激素相关的神经肽。