Transcription factor p53 exhibits increased binding to the A2-macroglobulin gene promotor and decreased glycosylation in fetal and adult rat liver during the acute-phase response

• Published in: Archives of biological sciences Vol. 60; no. 3
• Main Authors: Mihailovic, M, Poznanovic, G, Dinic, S, Grdovic, N, Vidakovic, M, Martinovic, V, Bogojevic, D., Institute for Biological Research Sinisa Stankovic, Belgrade (Serbia). Department of Molecular Biology
• Format: Journal Article
• Language: English
• Published: 2008
• Subjects: FACTEUR DE TRANSCRIPTION; FACTORES DE TRANSCRIPCION; FETO; FOETUS; FOIE; GENE; GENES; HIGADO; http://www.fao.org/aos/agrovoc#c_3006; http://www.fao.org/aos/agrovoc#c_3214; http://www.fao.org/aos/agrovoc#c_35345; http://www.fao.org/aos/agrovoc#c_4395; http://www.fao.org/aos/agrovoc#c_6464; LIVER; RAT; RATA; RATS; TRANSCRIPTION FACTORS
• ISSN: 0354-4664

The binding affinity of p53 for the MG promotor was assessed by DNA-affinity chromatography with the extended alfa2-macroglobulin (MG) gene promotor (-852/+12) and immunoblot analysis. During the increased MG gene transcription observed in the fetus and the acute-phase (AP) response in both the fetus and the adult, p53 exhibited increased binding to the MG promotor. This increase was accompanied by decreased O-linked N-acetyl glucosamine glycosylation of p53. We suggest that the enzymatic removal of sugar moieties in vivo serves to activate the MG gene promotor binding potential of p53 and its participation in upregulated MG gene transcription.