Salivary Cystatins: Exploring New Post-Translational Modifications and Polymorphisms by Top-Down High-Resolution Mass Spectrometry.
Barbara ManconiBarbara LioriTiziana CabrasFederica VincenzoniFederica IavaroneMassimo CastagnolaIrene MessanaAlessandra OlianasPublished in: Journal of proteome research (2018)
Cystatins are a complex family of cysteine peptidase inhibitors. In the present study, various proteoforms of cystatin A, cystatin B, cystatin S, cystatin SN, and cystatin SA were detected in the acid-soluble fraction of human saliva and characterized by a top-down HPLC-ESI-MS approach. Proteoforms of cystatin D were also detected and characterized by an integrated top-down and bottom-up strategy. The proteoforms derive from coding sequence polymorphisms and post-translational modifications, in particular, phosphorylation, N-terminal processing, and oxidation. This study increases the current knowledge of salivary cystatin proteoforms and provides the basis to evaluate possible qualitative/quantitative variations of these proteoforms in different pathological states and reveal new potential salivary biomarkers of disease. Data are available via ProteomeXchange with identifier PXD007170.
Keyphrases
- ms ms
- high resolution mass spectrometry
- mass spectrometry
- endothelial cells
- liquid chromatography
- multiple sclerosis
- genome wide
- dna methylation
- single cell
- gene expression
- climate change
- big data
- hydrogen peroxide
- risk assessment
- gas chromatography
- electronic health record
- induced pluripotent stem cells
- high performance liquid chromatography
- deep learning
- solid phase extraction