Mapping Extracellular Matrix Proteins in Formalin-Fixed, Paraffin-Embedded Tissues by MALDI Imaging Mass Spectrometry
Mapping Extracellular Matrix Proteins in Formalin-Fixed, Paraffin-Embedded Tissues by MALDI Imaging Mass Spectrometry
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DOI：
10.1021/acs.jproteome.7b00713
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发表时间：
2018-01-01
影响因子：
4.4
通讯作者：
Drakes, Richard R.
中科院分区：
文献类型：
--
作者：
Angel, Peggi M.;Comte-Walters, Susana;Drakes, Richard R.
胶原蛋白和弹性蛋白形成所有组织和器官的基本框架，并且它们的表达和翻译后加工在疾病和健康中受到严格调控。由于其独特的结构组成和性质，在复杂的组织微环境中访问这些蛋白质结构以了解局部变化如何调节组织健康是公认的挑战。我们描述了一种新的工作流程，使用基质辅助激光解吸/电离成像质谱（MALDI IMS）与基质金属蛋白酶（MMP）酶的组合，以访问和报告福尔马林固定，石蜡包埋（FFPE）组织中胶原蛋白和弹性蛋白序列的空间定位。开发的技术提供了新的途径，以胶原蛋白和弹性蛋白序列定位于组织功能，以前无法实现。这种高通量技术进步应适用于任何组织，无论疾病类型、组织来源或疾病状态如何，因此与所有研究相关：基础、转化或临床。
Collagens and elastin form the fundamental framework of all tissues and organs, and their expression and post-translational processing are tightly regulated in disease and health. Because of their unique structural composition and properties, it is a recognized challenge to access these protein structures within the complex tissue micro environment to understand how localized changes modulate tissue health. We describe a new workflow using a combination of matrix assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) with matrix metalloproteinase (MMP) enzymes to access and report on spatial localization of collagen and elastin sequences in formalin-fixed, paraffin-embedded (FFPE) tissues. The developed technology provides new access to collagens and elastin sequences localized to tissue features that were previously unattainable. This high-throughput technological advance should be applicable to any tissue regardless of disease type, tissue origin, or disease status and is thus relevant to all research: basic, translational, or clinical.