Profiling the effects of short time‐course cold ischemia on tumor protein phosphorylation using a Bayesian approach

Profiling the effects of short time‐course cold ischemia on tumor protein phosphorylation using... 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 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biometrics Wiley

Profiling the effects of short time‐course cold ischemia on tumor protein phosphorylation using a Bayesian approach

Loading next page...
 
/lp/wiley/profiling-the-effects-of-short-time-course-cold-ischemia-on-tumor-AeKChPYgj6
Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
© 2018, The International Biometric Society
ISSN
0006-341X
eISSN
1541-0420
D.O.I.
10.1111/biom.12742
Publisher site
See Article on Publisher Site

Abstract

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

Journal

BiometricsWiley

Published: Jan 1, 2018

Keywords: ; ; ;

References

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 12 million articles from more than
10,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Unlimited reading

Read as many articles as you need. Full articles with original layout, charts and figures. Read online, from anywhere.

Stay up to date

Keep up with your field with Personalized Recommendations and Follow Journals to get automatic updates.

Organize your research

It’s easy to organize your research with our built-in tools.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve Freelancer

DeepDyve Pro

Price
FREE
$49/month

$360/year
Save searches from
Google Scholar,
PubMed
Create lists to
organize your research
Export lists, citations
Read DeepDyve articles
Abstract access only
Unlimited access to over
18 million full-text articles
Print
20 pages/month
PDF Discount
20% off