Economical and easily detectable markers of digestive tumors: platelet parameters.

Aim: This study aimed to evaluate the clinical values of platelet parameters in patients with digestive tumors. Patients & methods: A total of 974 people were classified into three groups: malignant group, patients with digestive malignant tumors; benign group, patients with benign tumors; and normal group: healthy individuals. Results: Compared with the benign and normal groups, the malignant group showed significantly increased platelet count (PLT) and plateletcrit (PCT) and significantly reduced mean platelet volume (MPV) and platelet-large cell rate (P-LCR, p < 0.001). Elevated PLT and PCT and reduced MPV and P-LCR indicated poor overall survival in patients with digestive tumors. Conclusion: PLT, PCT, MPV and P-LCR were proven to be predictive biomarkers for patients with digestive malignant tumors. Elevated PLT and PCT or decreased MPV and P-LCR indicated poor overall survival.

Sensitive, Robust, and Cost-Effective Approach for Tyrosine Phosphoproteome Analysis.

Albeit much less abundant than Ser/Thr phosphorylation (pSer/pThr), Tyr phosphorylation (pTyr) is considered as a hallmark in cellular signal transduction. However, its analysis at the proteome level remains challenging. The conventional immunopurification (IP) approach using antibodies specific to pTyr sites is known to have low sensitivity, poor reproducibility and high cost. Our recent study indicated that SH2 domain-derived pTyr-superbinder is a good replacement of pTyr antibody for the specific enrichment of pTyr peptides for phosphoproteomics analysis. In this study, we presented an efficient SH2 superbinder based workflow for the sensitive analysis of tyrosine phosphoproteome. This new method can identify 41% more pTyr peptides than the previous method. Its excellent performance was demonstrated by the analysis of a variety of different samples. For the highly tyrosine phosphorylated sample, for example, pervanadate-treated Jurkat T cells, it identified over 1800 high confident pTyr sites from only 2 mg of proteins. For the unstimulated Jurkat cells, where the pTyr events rarely occurred, it identified 343 high confident pTyr sites from 5 mg of proteins, which was 31% more than that obtained by the antibody-based method. For the heterogeneous sample of tissue, it identified 197 high confident pTyr sites from 5 mg protein digest of mouse skeletal muscle. In general, it is a sensitive, robust and cost-effective approach and would have wide applications in the study of the regulatory role of tyrosine phosphorylation in diverse physiological and pathological processes.