Literature DB >> 27818121

Evidence for APOBEC3B mRNA and protein expression in oral squamous cell carcinomas.

Galinos Fanourakis1, Konstantinos Tosios2, Nikolaos Papanikolaou3, Ioulia Chatzistamou4, Marios Xydous5, Sofia Tseleni-Balafouta6, Alexandra Sklavounou2, Gerassimos E Voutsinas7, Heleni Vastardis8.   

Abstract

It has been demonstrated that APOBEC3B possesses cytidine deaminase activity, which is likely to result in C-to-T signature mutations. Increased expression of the APOBEC3B gene has been shown to correlate with higher incidence of such mutations in various cancer types, such as breast, bladder, lung, and head and neck carcinomas. In the current study, we used in silico methods, immunohistochemistry and qRT-PCR to detect the presence of APOBEC3B signature mutations and examine the levels and patterns of APOBEC3B expression in oral squamous cell carcinomas (OSCCs). Using the Cancer Genome Atlas (TCGA) database, we have found a high incidence of C-to-T transitions in head and neck squamous cell carcinomas (HNSCCs), of which OSCCs constitute the largest subgroup. Additionally, we compared APOBEC3B expression, at both mRNA and protein level, between OSCCs and non-cancerous samples. APOBEC3B was detected in both groups, but nuclear localization was consistent only in normal oral cells. APOBEC3B mRNA levels were clearly higher in OSCCs than in controls. These results suggest that while in normal oral cells APOBEC3B has an important nuclear function to fulfill, this activity may be hindered in a subgroup of tumor cells, due to the more prominent localization of the enzyme in the cytoplasm.
Copyright © 2016 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  APOBEC3B; Genomics; Head and neck squamous cell carcinoma; Immunohistochemistry; Oral squamous cell carcinoma

Mesh:

Substances:

Year:  2016        PMID: 27818121     DOI: 10.1016/j.yexmp.2016.11.001

Source DB:  PubMed          Journal:  Exp Mol Pathol        ISSN: 0014-4800            Impact factor:   3.362


  4 in total

1.  The DNA deaminase APOBEC3B interacts with the cell-cycle protein CDK4 and disrupts CDK4-mediated nuclear import of Cyclin D1.

Authors:  Jennifer L McCann; Madeline M Klein; Evelyn M Leland; Emily K Law; William L Brown; Daniel J Salamango; Reuben S Harris
Journal:  J Biol Chem       Date:  2019-06-19       Impact factor: 5.157

2.  APOBEC3B Nuclear Localization Requires Two Distinct N-Terminal Domain Surfaces.

Authors:  Daniel J Salamango; Jennifer L McCann; Özlem Demir; William L Brown; Rommie E Amaro; Reuben S Harris
Journal:  J Mol Biol       Date:  2018-05-19       Impact factor: 5.469

Review 3.  APOBEC3B, a molecular driver of mutagenesis in human cancers.

Authors:  Jun Zou; Chen Wang; Xiangyi Ma; Edward Wang; Guang Peng
Journal:  Cell Biosci       Date:  2017-05-30       Impact factor: 7.133

4.  Enzyme cycling contributes to efficient induction of genome mutagenesis by the cytidine deaminase APOBEC3B.

Authors:  Madison B Adolph; Robin P Love; Yuqing Feng; Linda Chelico
Journal:  Nucleic Acids Res       Date:  2017-11-16       Impact factor: 16.971

  4 in total

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