HAEMATOLOGY RESEARCH GROUP
Platelet proteomics
Our high-sensitivity label free mass spectrometry analysis of platelet lysates from healthy donors identified >3,800 proteins. We have developed the most sensitive analysis to date of the platelet releasate proteome with the detection of >1,300 proteins. Unbiased scanning for post-translational modifications within releasate proteins highlighted O-O-glycosylation as being a major component. For the first time, we detected O-O-fucosylation on previously uncharacterised sites including multimerin-1.
Scatterplot of proteins significantly regulated in the high-dose (a) and low-dose (b) thrombin stimulated releasate. Significantly regulated proteins are shown in orange, non-significant proteins are shown in blue. The log2 fold-change (thrombin stimulated/resting) for both the each corresponding releasate (x-axis) and the corresponding lysate (y-axis) was used for plotting.
Callum B. Houlahan, Yvonne Kong, et.al. Molecular & Cellular Proteomics,