Disease relevance of Tcfcp2

• NF2d9 thus belongs to the CP2 family and is the mouse homolog of human LBP-1a, which modulates human immunodeficiency virus type 1 transcription [1].
• LSF had no effect on chemotherapy-induced killing of tumor cells in vitro, nor on the antitumor activity of 5-FU or thiotepa in BALB/c mice implanted with P388 leukemia cells [2].

High impact information on Tcfcp2

• Erythroid cell-specific alpha-globin gene regulation by the CP2 transcription factor family [3].
• CP2b has an erythroid cell-specific transcriptional activation domain, which requires the extra exon and can form heteromeric complexes with other CP2 isoforms, but lacks the DNA binding activity found in CP2a and CP2c [3].
• LBP-1a and CP2 are ubiquitously expressed members of the grainyhead transcription factor family, sharing significant sequence homology, a common DNA binding motif, and modulating a range of key regulatory and structural genes [4].
• Here, we show that a grainyhead-related transcription factor, CP2-like 1 (CP2L1), is required for the maturation of the ducts of the salivary gland and kidney [5].
• When murine bone marrow cells were treated with 5-FU plus LSF, release of this inhibitor of CFU-GM proliferation was blocked [2].

Biological context of Tcfcp2

• The deduced amino acid sequence revealed that NF2d9 is 72 and 94% identical to mouse CP2 and human LBP-1a, respectively [1].
• These results define the CP2 factor binding site in more detail and help characterize the activities of the factor in vivo [6].
• Here, we report that this increment of CP2 expression is crucial in erythroid-specific globin gene expression and hemoglobin synthesis [7].
• In an effort to understand how it selects its target genes we carried out a database search, and located several CP2 binding motifs in the promoter region of bone morphogenetic protein-4 (BMP4) [8].
• Competition electrophoretic mobility shift assay and methylation interference analysis revealed that C'BP-2 is a protein closely related, but not identical, to CP2 [9].

Anatomical context of Tcfcp2

• In this report, we exploited our ability to express CP2 in bacteria and eukaryotic cells to further investigate factor activities in vitro and in vivo [6].
• Transcription factor CP2 is involved in activating mBMP4 in mouse mesenchymal stem cells [8].
• In 4 of 5 experiments, LSF significantly accelerated neutrophil recovery (P < or = 0.05, Wilcoxon paired-signed test) [2].
• In addition, platelet, reticulocyte, and CFU-GM regeneration were significantly accelerated in mice treated with LSF compared to control mice (P < or = 0.05) [2].
• LSF had no significant effects on the ability of 5-FU to kill hematopoietic progenitor cells, nor did LSF stimulate or inhibit proliferation of CFU-GM [2].

Associations of Tcfcp2 with chemical compounds

• We tested the effect of LSF (100 mg/kg i.p., b.i.d.) on multilineage regeneration after high-dose 5-FU or thiotepa treatment in BALB/c mice [2].
• METHODS: Based on a median split of sucrose intake during a final 1-h feeding test session, male Wistar rats were designated as either low (LSF) or high sucrose feeders (HSF) [10].
• Lisofylline [(R)-1-(5-hydroxyhexyl)-3,7-dimethylxanthine; LSF] selectively inhibits generation of selected species of PA in P388 cells induced by TNF alpha, IL-1 beta or LPS [11].

Other interactions of Tcfcp2

• We recently cloned human and murine cDNAs that encode CP2, a transcription factor that interacts with the murine alpha-globin promoter [6].

Analytical, diagnostic and therapeutic context of Tcfcp2

• Sequence analysis of the proximal promoter region revealed several potential regulatory elements; these include the recognition elements of Sp1, Nkx, CP2, E2A, SIF (SIS-inducible factor), TFII-I and cAMP-responsive element (CRE), but no TATA sequences [12].
• RESULTS: Data from this experiment revealed augmented responding in HSF compared with LSF during acquisition of amphetamine self-administration [10].
• LSF has a marked protective effect in a variety of acute inflammatory animal models that may be due to inhibition of this shared second messenger pathway involving PA [11].

References