A phosphorylation-related variant ADD1-rs4963 modifies the risk of colorectal cancer

PLoS One. 2015 Mar 27;10(3):e0121485. doi: 10.1371/journal.pone.0121485. eCollection 2015.

Abstract

It is well-established that abnormal protein phosphorylation could play an essential role in tumorgenesis by disrupting a variety of physiological processes such as cell growth, signal transduction and cell motility. Moreover, increasing numbers of phosphorylation-related variants have been identified in association with cancers. ADD1 (α-adducin), a versatile protein expressed ubiquitously in eukaryotes, exerts an important influence on membrane cytoskeleton, cell proliferation and cell-cell communication. Recently, a missense variant at the codon of ADD1's phosphorylation site, rs4963 (Ser586Cys), was reported to modify the risk of non-cardia gastric cancer. To explore the role of ADD1-rs4963 in colorectal cancer (CRC), we conducted a case-control study with a total of 1054 CRC cases and 1128 matched controls in a Chinese population. After adjustment for variables including age, gender, smoking and drinking, it was demonstrated that this variant significantly conferred susceptibility to CRC (G versus C: OR = 1.16, 95% CI = 1.03-1.31, P = 0.016; CG versus CC: OR = 1.25, 95% CI = 1.02-1.55, P = 0.036; GG versus CC: OR = 1.35, 95% CI = 1.06-1.72, P = 0.015). We further investigated the interaction of ADD1-rs4963 with smoking or drinking exposure, but found no significant result. This study is the first report of an association between ADD1 and CRC risk, promoting our knowledge of the genetics of CRC.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Asian People / genetics*
  • Calmodulin-Binding Proteins / genetics*
  • Calmodulin-Binding Proteins / metabolism
  • Case-Control Studies
  • China
  • Colorectal Neoplasms / genetics*
  • Female
  • Genetic Association Studies
  • Genetic Predisposition to Disease
  • Humans
  • Male
  • Middle Aged
  • Mutation, Missense
  • Phosphorylation
  • Polymorphism, Single Nucleotide

Substances

  • Calmodulin-Binding Proteins
  • adducin

Grants and funding

This work was supported by the National Program for Support of Top-notch Young Professionals, National Natural Science Foundation of China NSFC-81001275, 81171878, 81222038; the Fok Ying Tung Foundation for Young Teachers in the Higher Education Institutions of China-131038 and the Natural Science Foundation of Hubei-2012FFA011 furnished support to XM. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.