AI Article Synopsis
- Human saliva is gaining attention for biomarker studies due to its ease of collection and simpler processing compared to traditional methods like blood samples.
- The study analyzed saliva from four individuals over three days, finding that while there were consistent protein patterns, the expression levels of specific proteins varied.
- Notable differences in protein profiles between individuals were found, enabling the identification of unique protein patterns, and some proteins were shown to have multiple phosphorylation states.
Article Abstract
Human saliva is finding increasing interest for proteomic and biomarker-discovery studies, due to the ease of collection and potential for simpler processing workflows compared to serum or plasma. However, it is known that salivary protein composition can vary with physiological and environmental factors. In this work, we have examined intra- and inter-person variability of saliva protein composition using an LC/MS methodology to profile low molecular weight human salivary proteins. Whole saliva was analyzed from four individuals over three consecutive days. Additional samples were used to determine baseline analytical and sample processing variation and to identify phosphoproteins. Individuals were observed to have a similar salivary protein pattern over multiple days, although the expression levels of particular proteins were variable. Significant differences in protein profiles were observed between subjects, allowing for delineation of individuals based on their protein profile. Comparison with alkaline phosphatase treated saliva revealed that several identified proteins were singly, doubly, or triply phosphorylated.
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| http://dx.doi.org/10.1016/j.bbapap.2007.04.017 | DOI Listing |
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