{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T02:52:00Z","timestamp":1791168720694,"version":"4.1.0"},"reference-count":51,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2011,8,10]],"date-time":"2011-08-10T00:00:00Z","timestamp":1312934400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Cancer"],"published-print":{"date-parts":[[2011,12]]},"abstract":"<jats:title>Abstract<\/jats:title>\n          <jats:sec>\n            <jats:title>Background<\/jats:title>\n            <jats:p>Activation Induced cytidine Deaminase (AID) targets the immunoglobulin genes of activated B cells, where it converts cytidine to uracil to induce mutagenesis and recombination. While essential for immunoglobulin gene diversification, <jats:italic>AID<\/jats:italic> misregulation can result in genomic instability and oncogenic transformation. This is classically illustrated in Burkitt's lymphoma, which is characterized by AID-induced mutation and reciprocal translocation of the <jats:italic>c-MYC<\/jats:italic> oncogene with the IgH loci. Originally thought to be B cell-specific, <jats:italic>AID<\/jats:italic> now appears to be misexpressed in several epithelial cancers, raising the specter that AID may also participate in non-B cell carcinogenesis.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Methods<\/jats:title>\n            <jats:p>The mutagenic potential of AID argues for the existence of cellular regulators capable of repressing inappropriate <jats:italic>AID<\/jats:italic> expression. MicroRNAs (miRs) have this capacity, and we have examined the publically available human <jats:italic>AID<\/jats:italic> EST dataset for miR complementarities to the human <jats:italic>AID<\/jats:italic> 3'UTR. In this work, we have evaluated the capacity of two candidate miRs to repress human AID expression in MCF-7 breast carcinoma cells.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>We have discovered moderate miR-155 and pronounced miR-93 complementary target sites encoded within the human <jats:italic>AID<\/jats:italic> mRNA. Luciferase reporter assays indicate that both miR-93 and miR-155 can interact with the 3'UTR of <jats:italic>AID<\/jats:italic> to block expression. In addition, over-expression of either miR in MCF-7 cells reduces endogenous AID protein, but not mRNA, levels. Similarly indicative of <jats:italic>AID<\/jats:italic> translational regulation, depletion of either miR in MCF-7 cells increases AID protein levels without concurrent increases in <jats:italic>AID<\/jats:italic> mRNA.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusions<\/jats:title>\n            <jats:p>Together, our findings demonstrate that miR-93 and miR-155 constitutively suppress <jats:italic>AID<\/jats:italic> translation in MCF-7 cells, suggesting widespread roles for these miRs in preventing genome cytidine deaminations, mutagenesis, and oncogenic transformation. In addition, our characterization of an obscured miR-93 target site located within the <jats:italic>AID<\/jats:italic> 3'UTR supports the recent suggestion that many miR regulations have been overlooked due to the prevalence of truncated 3'UTR annotations.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/1471-2407-11-347","type":"journal-article","created":{"date-parts":[[2011,8,10]],"date-time":"2011-08-10T18:25:28Z","timestamp":1313000728000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":51,"title":["Repression of human activation induced cytidine deaminase by miR-93 and miR-155"],"prefix":"10.1186","volume":"11","author":[{"given":"Glen M","family":"Borchert","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nathaniel W","family":"Holton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erik D","family":"Larson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2011,8,10]]},"reference":[{"key":"2818_CR1","doi-asserted-by":"publisher","first-page":"432","DOI":"10.1016\/j.molmed.2006.07.001","volume":"12","author":"VG de Yebenes","year":"2006","unstructured":"de Yebenes VG, Ramiro AR: Activation-induced deaminase: light and dark sides. 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