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Mapping the Proteoform Landscape of Five Human Tissues
Bryon S Drown1, Kevin Jooß1, Rafael D Melani1
1Departments of Molecular Biosciences, Chemistry, and the Feinberg School of Medicine, Northwestern University, Evanston, Illinois 60208, United States.
Journal of Proteome Research
|April 12, 2022
Summary
This study mapped human proteoforms using advanced mass spectrometry, identifying thousands of new protein variants. These findings reveal tissue-specific protein differences, offering insights into human health and disease.
Area of Science:
- Proteomics
- Human Biology
- Biochemistry
Background:
- Understanding protein structure-function relationships is crucial for human biology.
- Proteins exist in various forms (proteoforms) due to complex regulation.
- Mapping the human proteoform landscape requires sensitive analytical methods.
Purpose of the Study:
- To comprehensively map and characterize human proteoforms across multiple organs.
- To identify novel proteoforms and quantify their abundance.
- To investigate tissue-specific proteoform differences and their biological implications.
Main Methods:
- Employed a top-down proteomics strategy.
- Utilized capillary zone electrophoresis (CZE) and nanoflow reversed-phase liquid chromatography (RPLC) coupled to mass spectrometry.
- Analyzed proteoforms from human lungs, heart, spleen, small intestine, and kidneys.
Main Results:
- Identified and characterized 11,466 proteoforms.
- Discovered 7,373 (64%) previously unreported proteoforms.
- Quantified significant protein and proteoform level differences across analyzed organs.
Conclusions:
- Combined CZE and RPLC enhanced proteome coverage and provided complementary proteoform selectivity.
- Observed differential proteoform regulation of key proteins (e.g., defensins, glutathione transferases, sarcomeric proteins) across tissues.
- Generated hypotheses regarding the functional roles and regulation of proteoforms in human health and disease.
