Activation-induced cytidine deaminase: in sickness and in health
- PDF / 1,131,176 Bytes
- 10 Pages / 595.276 x 790.866 pts Page_size
- 36 Downloads / 184 Views
REVIEW – CANCER RESEARCH
Activation‑induced cytidine deaminase: in sickness and in health Leonardo Alves de Souza Rios1 · Benjamin Cloete1 · Shaheen Mowla1 Received: 7 May 2020 / Accepted: 4 August 2020 © Springer-Verlag GmbH Germany, part of Springer Nature 2020
Abstract Activation Induced cytidine Deaminase (AID) is an essential enzyme of the adaptive immune system. Its canonical activity is restricted to B lymphocytes, playing an essential role in the diversification of antibodies by enhancing specificity and changing affinity. This is possible through its DNA deaminase function, leading to mutations in DNA. In the last decade, AID has been assigned an additional function: that of a powerful DNA demethylator. Adverse cellular conditions such as chronic inflammation can lead to its deregulation and overexpression. It is an important driver of B-cell lymphoma due to its natural ability to modify DNA through deamination, leading to mutations and epigenetic changes. However, the deregulation of AID is not restricted to lymphoid cells. Recent findings have provided new insights into the role that this protein plays in the development of non-lymphoid cancers, with some research shedding light on novel AID-driven mechanisms of cellular transformation. In this review, we provide an updated narrative of the normal physiological functions of AID. Additionally, we review and discuss the recent research studies that have implicated AID in carcinogenesis in varying tissue types including lymphoid and non-lymphoid cancers. We review the mechanisms, whereby AID promotes carcinogenesis and highlight important areas of future research. Keywords Activation induced cytidine deaminase · Deaminase · Demethylator · Lymphomagenesis · Cancer Abbreviations A-EJ Alternative end-joining AID Activation induced cytidine deaminase AIDS Acquired immune deficiency disorder AOM Azoxymethane APE1 Apyrimidinic endonuclease APOBEC Apolipoprotein B mRNA editing catalytic polypeptide-like ATP Adenosine triphosphate BER Base excision repair BL Burkitt lymphoma BUCC Bladder urothelial cell carcinoma CAC Colitis-associated cancers
* Shaheen Mowla [email protected] Leonardo Alves de Souza Rios [email protected] Benjamin Cloete [email protected] 1
Division of Haematology, Department of Pathology, Faculty of Health Sciences, University of Cape Town, Observatory, Cape Town 7925, South Africa
CHOP Cyclophosphamide, doxorubicin hydrochloride, vincristine sulfate and prednisone CRM-1 Chromosome maintenance 1 CSR Class switch recombination dC Deoxycytidine DLBCL Diffuse large B cell lymphoma DSS Dextran sulfate sodium dU Deoxyuridine EBNA2 Epstein-Barr virus nuclear antigen 2 EBNA3C Epstein-Barr virus nuclear antigen 3C EBV Epstein-Barr virus EGFR Epidermal growth factor receptor EMT Epithelial-to-mesenchymal transition GC Germinal centre HAART Highly active antiretroviral therapy HIV Human immunodeficiency virus IECs Intestinal epithelial cells IRC Inflammation-related carcinogenesis LMP1 Latent Membrane P
Data Loading...
