期刊
JOURNAL OF PROTEOME RESEARCH
卷 17, 期 1, 页码 635-646出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jproteome.7b00713
关键词
imaging mass spectrometry; proteomics; peptide imaging; extracellular matrix; formalin-fixed; paraffin-embedded tissue imaging; tissue imaging; MALDI imaging mass spectrometry
资金
- National Institute of General Medical Sciences [P20 GM103542]
- National Cancer Institute [1R21CA207779]
- American Heart Association [16GRNT31380005]
- South Carolina Centers of Economic Excellence SmartState program
- Office of the Provost
- South Carolina COBRE in Oxidants, Redox Balance and Stress Signaling [GM 103542]
- NATIONAL CANCER INSTITUTE [R21CA186799, R21CA207779] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P20GM103542] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [S10OD010731] Funding Source: NIH RePORTER
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.
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