Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P51532 (transcriptional activator)
 6,546 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Desquamative inflammatory vaginitis (DIV) is a well-described but poorly understood vaginitis associated with yellow vaginal discharge and vulvovaginal pruritus, burning, and dyspareunia. Although etiologies of an inflammatory, infectious, and hormonal nature have been proposed, response to therapy has been inconsistent and complete resolution of symptoms has been disappointing. We propose that DIV is a mucous membrane manifestation of vitamin D deficiency that results in desquamation of the vaginal epithelium and discharge. Moreover, we suggest that the loss of this epithelium leads to altered vaginal pH levels, mucous membrane fragility, inflammation, and secondary infection. Because vitamin D is a known transcriptional activator, we suggest that vitamin D is necessary for the synthesis of specific vaginal structural proteins, such as cytokeratins. Vitamin D deficiency results in decreased amounts of these proteins, resulting in loss of epithelial structural integrity and desquamation. Correction of the vitamin D deficiency ultimately leads to regeneration of the vaginal epithelium and cessation of desquamation.
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PMID:Treatment of desquamative inflammatory vaginitis with vitamin D: a case report. 1830 53

The hematopoietic-specific transcription factor p45/NF-E2 is an important transcriptional activator in the erythroid and megakaryocytic lineages. We describe the first in vivo evidence for the interaction between p45/NF-E2 and the E3 ubiquitin ligase Itch, and the subsequent ubiquitination of p45/NF-E2 by Itch. Interestingly, Itch suppressed the transactivation activity of p45/NF-E2 by adding a Lys63-linked polyubiquitin chain. Confocal microscopy revealed that ubiquitinated p45/NF-E2 became localized in the cytoplasm when Itch was over-expressed. Thus, Itch-mediated ubiquitination of p45/NF-E2 does not target the protein for proteasomal degradation, but instead retains p45/NF-E2 in the cytoplasm, where it cannot function as a transactivator. Finally, we suggest that this Itch-dependent p45/NF-E2 ubiquitination mechanism may regulate NF-E2 function during the development of hematopoietic cell lineages.
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PMID:Itch regulates p45/NF-E2 in vivo by Lys63-linked ubiquitination. 1871 48