IntroductionProtein tyrosine phosphorylation is considered to be a fundamental mechanism for regulating many cellular functions. In this specific phosphorylation, a phosphate group is added to the amino acid tyrosine on a protein. Disorders of tyrosine phosphorylation are believed to lead to many serious human diseases (Hunter, ). For example, protein tyrosine phosphorylation is tightly regulated in normal cells, but tyrosine kinases, whose activity controls tyrosine phosphorylation, are found to be mutated or over‐expressed in many human malignancies (Paul and Mukhopadhyay, ). Accurate and robust assessment of tyrosine phosphorylation in tumor biopsy samples is thus necessary for understanding intracellular signaling networks and for developing targeted therapies for cancer patients (Bonnas et al., ); Gajadhar et al., ).However, there may exist pre‐analytic variations due to inconsistencies during sample collection and processing in a clinical laboratory. One of these sources of variations is cold ischemia. Also known as freezing delay time, cold ischemia is the time between tissue specimen excision and the freezing of the sample. Although it has been shown that global protein levels do not change up to 1‐hour cold ischemia, significant changes are observed in phosphorylated proteins at the phosphorylation sites. Some of the phosphorylation sites even have rapid
Biometrics – Wiley
Published: Jan 1, 2018
Keywords: ; ; ;
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