Mapping Extracellular Matrix Proteins in Formalin-Fixed, Paraffin-Embedded Tissues by MALDI Imaging Mass Spectrometry

被引:65
|
作者
Angel, Peggi M. [1 ]
Comte-Walters, Susana [1 ]
Ball, Lauren E. [1 ]
Talbot, Kacey [1 ]
Mehta, Anand [1 ]
Brockbank, Kelvin G. M. [2 ,3 ,4 ]
Drakes, Richard R. [1 ]
机构
[1] Med Univ South Carolina, Dept Cell & Mol Pharmacol, Charleston, SC 29425 USA
[2] Med Univ South Carolina, Dept Regenerat Med, Charleston, SC 29425 USA
[3] Tissue Testing Technol LLC, N Charleston, SC 29406 USA
[4] Clemson Univ, Dept Bioengn, Clemson, SC 29634 USA
关键词
imaging mass spectrometry; proteomics; peptide imaging; extracellular matrix; formalin-fixed; paraffin-embedded tissue imaging; tissue imaging; MALDI imaging mass spectrometry; HUMAN ELASTIN GENE; BRAIN-TISSUE; IDENTIFICATION; COLLAGEN; CANCER; METALLOPROTEINASES; MUTATIONS; PEPTIDES; SECTIONS; BREAST;
D O I
10.1021/acs.jproteome.7b00713
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:635 / 646
页数:12
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