Disease relevance of CDO1

• One cell line, TE 671 (human medulloblastoma) was found to express both a protein of approximately 70 kDa and CDO activity [1].
• The characterization of an in vitro model for CDO expression provides a useful tool for the investigation of this important enzyme, which may have an etiological role in the pathogenesis of Parkinson's disease [1].
• Using PSI-BLAST searches and crystallographic information about the active-site geometry of mammalian CDOs, we identified a total of four proteins from Bacillus subtilis, Bacillus cereus, and Streptomyces coelicolor A3(2) that shared low overall identity to CDO (13 to 21%) but nevertheless conserved important active-site residues [2].
• Phylogenetic analyses of putative bacterial CDO homologs also indicate that CDO is distributed among species within the phyla of Actinobacteria, Firmicutes, and Proteobacteria [2].
• We have examined the effect of this CDO alone and in combination with a range of common chemotherapeutic agents in colorectal cancer cell lines [3].

Psychiatry related information on CDO1

• Similarly, cysteine deoxygenase (CDO) may be involved in the regulation of protein function and antioxidant defense mechanisms by its ability to oxidized cysteine residues [4].

High impact information on CDO1

• The first major step of cysteine catabolism, the oxidation of cysteine to cysteine sulfinic acid, is catalyzed by cysteine dioxygenase (CDO) [5].
• In the present work, we utilize recombinant rat liver CDO and cysteine derivatives to elucidate structural parameters involved in substrate recognition and x-ray absorption spectroscopy to probe the interaction of the active site iron center with cysteine [5].
• Unlike many non-heme iron dioxygenases that employ alpha-keto acids as cofactors, CDO was shown to be the only dioxygenase known to be inhibited by alpha-ketoglutarate [5].
• We determined whether Cu deficiency would decrease taurine status and the hepatic activities of cysteine dioxygenase (CDO) and/or cysteine sulfinic acid decarboxylase (CSAD) in rats [6].
• In metazoa and fungi, the catabolic dissimilation of cysteine begins with its sulfoxidation to cysteine sulfinic acid by the enzyme cysteine dioxygenase (CDO) [2].

Chemical compound and disease context of CDO1

• Cyclophosphamide, pegylated liposomal doxorubicin, vincristine and prednisone (CDOP) plus rituximab is effective and well tolerated in poor performance status elderly patients with non-Hodgkin's lymphoma [7].

Biological context of CDO1

• Detection of human CDO completely correlated with the presence of human chromosome 5 [8].
• A human total genome cosmid library was screened with a PCR product from the coding region of human CDO cDNA and the two positive clones identified were used in fluorescent in situ hybridisation (FISH) analysis on metaphase chromosome spreads [8].
• Treatment of TE 671 cells with cysteine resulted in the upregulation of CDO mRNA, whereas treatment with tumor necrosis factor alpha resulted in the downregulation of CDO mRNA, as evidenced using NPA [1].
• AIM: The elucidation of the structure of the 5' flanking region and the exonic organisation of the human cysteine dioxygenase type I gene [9].
• Human CDO-I clones were identified by screening a liver cDNA library, and inserts were isolated and sequenced [10].

Anatomical context of CDO1

• CDO upregulation in hepatocytes in response to high sulfur amino acids appears clearly as the most spectacular among the regulations of the biosynthetic enzymes [11].
• RESULTS: CDO and SO were expressed in alveolar epithelial cells, which is also the site of expression of cytochrome P450 1B1 [12].

Associations of CDO1 with chemical compounds

• Here we demonstrate the screening and characterization of a cell line that expresses CDO, the primary metabolizing enzyme of cysteine and the regulatory point of sulfate production [1].
• In these organisms, CDO plays an important role in the homeostatic regulation of steady-state cysteine levels and provides important oxidized metabolites of cysteine such as sulfate and taurine [2].
• The ability of these proteins to oxidize cysteine to cysteine sulfinic acid was then compared against recombinant rat CDO [2].
• CDO has a critical role in determining the flux of cysteine between cysteine catabolism/taurine synthesis and glutathione synthesis [13].
• CDO catalyzes the first step in the conversion of cysteine to taurine, as well as the first step in the catabolism of cysteine to pyruvate plus sulfate [14].

Analytical, diagnostic and therapeutic context of CDO1

• Nuclease protection assay (NPA) of mRNA isolated from TE 671 showed the expression of a CDO mRNA [1].
• Simple drug-drug interaction studies showed that combining CDO with chemotherapy resulted in an enhancement of the antiproliferative effects [3].
• METHODS: Antibodies and oligonucleotide probes raised against both CDO and SO were used for immunohistochemistry and in situ hybridisation, respectively, to investigate the expression of CDO and SO in human lung alveoli [12].

References