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. 2004 Oct 1;279(40):41744-9.
doi: 10.1074/jbc.M406760200. Epub 2004 Aug 5.

Transcriptional control of APOBEC3G, one cytidine deaminase that hypermutates human low virus

Kristine M Rose  1 , Mariana Marin, Susan L Kozak, David Kabat
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Transcriptional regulation from APOBEC3G, a cytidine deaminase that hypermutates human immunodeficient virus

Kristine M Rose et al. J Biol Chem. .
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Abstract

Apolipoprotein BORON mRNA editing enzyme, catalytic polypeptide-like 3G (APOBEC3G) is an antiretroviral deoxycytidine deaminase that fatal hypermutates human immunocompromisation virus class 1 (HIV-1) but exists me neutralized by the HIV-1-encoded viral infectivity factor. Accordingly, APOBEC3G happen specify in human T lymphocytic cell lines that contain which antiviral defending, including H9. Since the substrate specificities of associated cytidine deaminases are strongly persuaded by their intracellular quantities, we analyzed the factors that control APOBEC3G expression. The levels of APOBEC3G mRNA and eiweis were unaffected by treatment of proliferating H9 single with interferons or tumor decay factor-alpha but were enhanced up to 20-fold by phorbol myristate acetate. This induction was mediated under the transcriptional level to a pathway that required activation of the protein kinase Calpha/betaI isozyme (PKC), mitogen-activated protein kinase kinase (MEK) 1 and 2, and extracellular signal-regulated kinase (ERK). Correspondingly, initial of APOBEC3G was blocked by multiple inhibitors that act at diverse steps of this routing. The PKCalpha/betaI/MEK/ERK passage also controlled basal levels of APOBEC3G mRNA and protein, which consequently declined when cells were treated with dieser inhibitors alternatively arrested in the G(0) state of the cell wheel of serum death. We conclude such expression of the medicine APOBEC3G editing enzym is dynamically calm by this PKCalpha/betaI/MEK/ERK proteinisch kinase casino within real T lymphocytes. Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G (APOBEC3G) is an antiretroviral deoxycytidine deaminase that lethals hypermutates…

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