| http://purl.uniprot.org/citations/17595061 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17595061 | http://www.w3.org/2000/01/rdf-schema#comment | "Alpha-enolase is a bifunctional gene encoding both a glycolytic enzyme and a DNA binding protein, c-myc binding protein (MBP-1). MBP-1 binds the c-myc promoter and downregulates c-myc transcription. Since these alpha-enolase gene products have important functions in glucose metabolism and growth regulation, this gene may play a central role in regulating the abnormal proliferative characteristics of transformed cells. To determine the role of alpha-enolase and MBP-1 in the cellular response to altered exogenous glucose concentration, MCF-7 cells were cultured in low (1 nM), physiological (5 mM), or high (25 mM) levels of glucose. Levels of alpha-enolase, MBP-1, and c-myc expression were compared to levels of cell proliferation and lactate production. At all glucose concentrations, MCF-7 cells demonstrated an initial increase in MBP-1 expression and a parallel decrease in c-myc transcript levels, which were accompanied by decreased proliferation. Cells grown in low glucose maintained the increased MBP-1 expression through 48 h, resulting in persistently lower rates of proliferation. However, physiologic or high glucose levels resulted in decreased MBP-1 expression, which was associated with increased cellular proliferation and lactate production. In these cells, c-myc mRNA returned to control levels as MBP-1 expression decreased. Cells grown in low glucose demonstrated a dramatic increase in c-myc mRNA at 48 h, which was associated with a loss in c-myc P2 promoter binding by MBP-1. This suggests that post-translational modifications of MBP-1 likely alter its DNA binding activity. These results demonstrate an important role for MBP-1 in the altered cell proliferation and energy utilization that occur in response to an altered glucose concentration."xsd:string |
| http://purl.uniprot.org/citations/17595061 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi7003558"xsd:string |
| http://purl.uniprot.org/citations/17595061 | http://purl.uniprot.org/core/author | "Thomas S.D."xsd:string |
| http://purl.uniprot.org/citations/17595061 | http://purl.uniprot.org/core/author | "Miller D.M."xsd:string |
| http://purl.uniprot.org/citations/17595061 | http://purl.uniprot.org/core/author | "Sedoris K.C."xsd:string |
| http://purl.uniprot.org/citations/17595061 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17595061 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/17595061 | http://purl.uniprot.org/core/pages | "8659-8668"xsd:string |
| http://purl.uniprot.org/citations/17595061 | http://purl.uniprot.org/core/title | "c-myc promoter binding protein regulates the cellular response to an altered glucose concentration."xsd:string |
| http://purl.uniprot.org/citations/17595061 | http://purl.uniprot.org/core/volume | "46"xsd:string |
| http://purl.uniprot.org/citations/17595061 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17595061 |
| http://purl.uniprot.org/citations/17595061 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17595061 |
| http://purl.uniprot.org/uniprot/#_Q6IB68-mappedCitation-17595061 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17595061 |
| http://purl.uniprot.org/uniprot/#_Q99417-mappedCitation-17595061 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17595061 |
| http://purl.uniprot.org/uniprot/Q6IB68 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/17595061 |
| http://purl.uniprot.org/uniprot/Q99417 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/17595061 |