Disease relevance of DEC1

• Absent to low expression of a 9q32 candidate tumor suppressor gene (TSG), DEC1 (deleted in esophageal cancer 1), is detected in four Asian ESCC cell lines [1].
• Tumor suppressive role of a 2.4 Mb 9q33-q34 critical region and DEC1 in esophageal squamous cell carcinoma [1].
• Given the reduced expression of the DEC1 gene in esophageal cancer, the high frequency of LOH at 9q32 in esophageal carcinomas, and the fact that the DEC1 cDNA can suppress growth of some cancer cells in vitro, we suggest that the DEC1 gene is a candidate tumor suppressor in 9q32 [2].
• Furthermore, in all evaluated cell lines of human fibroblasts, canine epithelial cells, human carcinoma, human glioblastoma and human melanoma, Bt2cAMP increased the DEC1 mRNA level within 1-3 h [3].
• Thus, immunohistochemical analysis of DEC1 expression is in our hands not suitable for detection of tissue hypoxia in this type of primary brain tumor [4].

High impact information on DEC1

• DEC1 is abundantly expressed in tumors and protects against apoptosis induced by serum starvation [5].
• Tetracycline-induced expression of DEC1 in stable lines proportionally increased the expression of survivin [5].
• The expression of antiapoptotic protein survivin is transcriptionally upregulated by DEC1 primarily through multiple sp1 binding sites in the proximal promoter [5].
• Studies with reporter mutants located, in the survivin promoter, two Sp1 sites that supported DEC1 transactivation [5].
• There is 74% LOH in the DEC1 region of ESCC primary tumors [1].

Biological context of DEC1

• Introduction of DEC1 cDNA into 3 cancer cell lines that lacked expression of DEC1 significantly suppressed cell growth, whereas antisense cDNA or the vector DNA alone did not [2].
• These findings suggest that DEC1 is a novel direct target for cAMP in wide types of cells, and that the bHLH protein is involved in the control of gene expression in cAMP-activated cells [3].
• Differentiated embryo-chondrocyte expressed gene 1 (DEC1) is involved in cell differentiation, proliferation, and apoptosis, and was recently shown to be regulated by hypoxia [6].
• Transcription factors DEC1 and DEC2 also play pivotal roles in multiple signaling pathways impacting various biological processes including development, cell differentiation, cell death, and oncogenesis [7].
• The list of genes includes both circadian regulator genes, such as period 1 and DEC1, and downstream effectors, such as ubiquitin specific protease 30 [8].

Anatomical context of DEC1

• Mutational analysis of this gene by reverse-transcriptase polymerase chain reaction disclosed significantly reduced expression of DEC1 in 8 of 13 (62%) esophageal cancer cell lines and in 16 of 30 (53%) primary squamous cell carcinomas of the esophagus [2].
• In rabbit chondrocyte cultures, PTH or Bt2cAMP increased the DEC1 mRNA level within 1 h [3].
• RESULTS: DEC1 was expressed in tumor cell nuclei, and occasionally in nuclei of endothelial cells, and glial and neuronal cells of surrounding brain tissue [4].
• At 15-72hpf, DEC1 shows a specific and dynamic expression in the developing eyes, somites, pineal gland (epiphysis), heart, brain, spinal cord, notochord, pronephric duct, common cardinal vein and blood cells [9].

Associations of DEC1 with chemical compounds

• Studies with actinomycin D and cycloheximide indicated that the enhancement of DEC1 mRNA by cAMP was not due to mRNA stabilization and did not require new protein synthesis [3].
• In the present study, we examined the effect of parathyroid hormone (PTH), dibutyryl cAMP (Bt2cAMP) and forskolin on the expression of DEC1 in various cells [3].
• Although DEC1 was not related to angiogenesis or to the expression of VEGF and thymidine phosphorylase, a direct association with up-regulated bFGF receptors was noted [6].

Other interactions of DEC1

• MATERIALS AND METHODS: 44 primary and 16 recurrent oligodendroglial neoplasms with 1p-aberrations were investigated immunohistochemically for the expression of DEC1, HIF-1alpha, and CA9 [4].
• PKS1, a polyketide synthase (PKS)-encoding gene at Tox1A, and DEC1, a decarboxylase-encoding gene at Tox1B, are necessary for T-toxin production [10].

Analytical, diagnostic and therapeutic context of DEC1

• Electrophoretic mobility shift assay and chromatin immunoprecipitation detected the presence of DEC1 in the survivin promoter [5].

References