Atlas of Genetics and Cytogenetics in Oncology and Haematology


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DDC (dopa decarboxylase (aromatic L-amino acid decarboxylase))

Identity

Other namesAADC
HGNC (Hugo) DDC
LocusID (NCBI) 1644
Location 7p12.1
Location_base_pair Starts at 50526134 and ends at 50628768 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order Centromere to telomere.

DNA/RNA

Note The complete nucleotide structure of the human DDC gene has been determined from tissues of neural and non-neural origin (Sumi-Ichinose et al., 1992; Ichinose et al., 1992). The full DDC cDNA sequence has been cloned from human cells, such as pheochromocytoma (Ichinose et al., 1989), liver (Ichinose et al., 1992), hepatoma cells (Scherer et al., 1992), placenta (Siaterli et al., 2003), peripheral leukocytes (Kokkinou et al., 2009b), as well as from several human cell lines, such as, U937 macrophage cells (Kokkinou et al., 2009a), SH-SY5Y, HTB-14 and HeLa cells (Chalatsa et al., 2011).
 
  Table 1. Expression of DDC mRNA transcripts in human tissues, cells and cancer cell lines.
Description The human DDC gene exists as a single-copy in the haploid genome. It is composed of 15 exons and 14 introns, spanning for more than 85 kbs (Sumi-Ichinose et al., 1992). The size of the exons was found to range from 20 to 406 bps (Sumi-Ichinose et al., 1992), whereas the size of the introns ranged from 927 to 24077 bps (Sumi-Ichinose et al., 1992; Yu et al., 2006). The DDC gene is located in close proximity to the epidermal growth factor (EGF) gene (Craig et al., 1992).
Transcription Alternative splicing events are responsible for the production of two distinct DDC mRNAs, termed neural and non-neural, which differ in their 5' untranslated region (UTR). The neural-type transcript includes exon N1 (83 bps) that is located 17.8 kbs upstream of exon two. The non-neural type DDC mRNA bears exon L1 (200 bps), which is located 4.2 kbs upstream to the location of exon N1. The second exon contains the translation start site and is located 22 kbs downstream from the non-neural (L1) exon (Ichinose et al., 1992). The transcription of the gene starts at position -111 (Sumi-Ichinose et al., 1992).
It has been reported that the two alternative DDC transcripts share identical coding regions and that their production is a result of alternative splicing and alternative promoter usage (Ichinose et al., 1992; Sumi-Ichinose et al., 1995). Neural and non-neural promoters have been identified 5' to the flanking region of the respective exon 1 (Le Van Thai et al., 1993; Sumi-Ichinose et al., 1995; Chatelin et al., 2001; Dugast-Darzacq et al., 2004). The generation of the two alternative DDC mRNAs is not a mutually exclusive and tissue-specific event as previously thought (Siaterli et al., 2003; Vassilacopoulou et al., 2004; Kokkinou et al., 2009a; Kokkinou et al., 2009b; Chalatsa et al., 2011).
An alternative splicing event has been described within the coding region of DDC mRNA, leading to the formation of a shorter transcript lacking exon 3 (O'Malley et al., 1995; Chang et al., 1996). It must be noted that the above authors did not specify the nature, neural or non-neural, of this shorter transcript. Recent evidence have revealed the neural nature of this alternative transcript in humans (Kokkinou et al., 2009a; Kokkinou et al., 2009b; Chalatsa et al., 2011).
A novel DDC mRNA coding region splice-variant, resulting in the formation of a truncated DDC mRNA has been also identified. This human DDC mRNA (1.8 kbs), termed as Alt-DDC, lacks exons 10-15 of the full-length transcript, but includes an alternative exon 10 (Vassilacopoulou et al., 2004). The Alt-DDC exon 10 (358 bps) was found within intron 9 of the DDC gene. Although Alt-DDC mRNA was detected in human placenta, high expression levels of this alternative transcript were found in human kidney (Vassilacopoulou et al., 2004).
The notion that transcription of the human DDC gene leads to the production of multiple mRNA isoforms, which are expressed in a non-mutually exclusive and tissue-specific manner, underlines the complexity of the expression patterns of this gene (table 1).
Pseudogene None has been identified yet.

Protein

Note Although, it was initially suggested that the DDC gene encoded for a single protein product (Sumi-Ichinose et al., 1992), evidence that demonstrated the expression of additional DDC protein isoforms in humans, argue against it (O'Malley et al., 1995; Chang et al., 1996; Vassilacopoulou et al., 2004).
Description The DDC enzyme (EC 4.1.1.28) was initially purified and characterized from pig kidney (Christenson et al., 1970) as well as from the insects Calliphora vicina (Fragoulis and Sekeris, 1975) and Ceratitis capitata (Mappouras and Fragoulis, 1988; Bossinakou and Fragoulis, 1996). DDC is a homodimer of 100-110 kDa, with a subunit molecular mass of 50-55 kDa (Voltattorni et al., 1979; Mappouras et al., 1990; Bossinakou and Fragoulis, 1996). The full-length protein molecule consists of 480 amino acids (Ichinose et al., 1989). DDC is a pyridoxal-5-phosphate (PLP)-dependent enzyme possessing a single binding-site for PLP per subunit (Voltattorni et al., 1982; Ichinose et al., 1989; Burkhard et al., 2001).
Expression of the DDC gene, in humans, results in the production of additional protein isoforms (O'Malley et al., 1995; Chang et al., 1996; Vassilacopoulou et al., 2004). O'Malley et al. (1995) identified of a new DDC protein isoform (O'Malley et al., 1995). The truncated DDC protein isoform (Mr; 50 kDa) consists of 442 amino acid residues (DDC442). This isoform was found to be inactive towards the decarboxylation of both L-Dopa to Dopamine and 5-Hydroxytryptophan (5-HTP) to serotonin (O'Malley et al., 1995). As mentioned above, the translation of Alt-DDC mRNA resulted in the synthesis of a truncated 338 amino acid long polypeptide, termed as Alt-DDC (Mr; 37 kDa). This isoform was identical to the full-length DDC protein up to amino acid residue 315. The remaining 23 amino acids of the C-terminal sequence are encoded by the alternative DDC exon 10 and are not incorporated in the full-length DDC protein sequence (Vassilacopoulou et al., 2004).
Although previous data had suggested that DDC was a rather unregulated molecule, several findings have indicated that DDC activity can be modulated by many factors, such as D1, DA receptor antagonists (Rossetti et al., 1990), a2-adrenergic receptor antagonists (Rossetti et al., 1989), D1, D2 receptor antagonists (Zhu et al., 1992; Hadjiconstantinou et al., 1993), DA receptor agonists (Zhu et al., 1993), PK-A and PK-C mediated pathways (Young et al., 1993; Young et al., 1994) and by endogenous inhibitors isolated from human serum (Vassiliou et al., 2005) and placenta (Vassiliou et al., 2009).
Expression DDC has been detected throughout the length of the gastrointestinal tract (Eisenhofer et al., 1997) and in blood plasma (Boomsma et al., 1986). DDC is expressed in normal human kidney and placenta (Mappouras et al., 1990; Siaterli et al., 2003). DDC expression was observed in normal peripheral leukocytes and T-lymphocytes (Kokkinou et al., 2009b). Furthermore, DDC is expressed in the human cancer cell lines U937 (Kokkinou et al., 2009a), SH-SY5Y, HeLa and HTB-14 (Chalatsa et al., 2011). Interestingly, the expression of the alternative DDC isoform (Alt-DDC) was also demonstrated in peripheral leukocytes (Kokkinou et al., 2009b), U937 (Kokkinou et al., 2009a), SH-SY5Y and HeLa cell lines (Chalatsa et al., 2011).
In the central nervous system, increased DDC enzymatic activity is detected in the hypothalamus, epiphysis, striatum, locus ceruleus, olfactory bulb and retina (Park et al., 1986). Elevated enzymatic DDC activity is also detected in peripheral organs such as liver, pancreas, kidney, lungs, spleen, stomach, salivary glands, as well as in the endothelial cells of blood vessels (Lovenberg et al., 1962; Rahman et al., 1981; Lindström and Sehlin, 1983).
Localisation DDC was considered to be a cytosolic molecule (Lovenberg et al., 1962; Sims et al., 1973). Nevertheless, additional experimental findings have demonstrated that a population of enzymatically active DDC molecules is associated with the cellular membrane fraction in the mammalian CNS (Poulikakos et al., 2001). Membrane-associated, enzymatically active DDC subpopulations were detected in the highly hydrophobic fractions of normal human leukocytes and U937 cancer cells (Kokkinou et al., 2009a; Kokkinou et al., 2009b).
Function In terms of substrate specificity, the DDC molecule purified from insects demonstrated a remarkably high affinity towards the decarboxylation of L-Dopa to dopamine (Fragoulis and Sekeris, 1975; Mappouras and Fragoulis, 1988; Bossinakou and Fragoulis, 1996). However, work by Mappouras et al. (1990) in the normal human kidney has suggested that the enzyme is capable of also decarboxylating L-5-Hydroxytryptophan to serotonin, although the decarboxylation activity towards L-5-Hydroxytryptophan was found to be considerably lower than the one observed for L-Dopa (Mappouras et al., 1990). Since DDC expression results in the production of multiple protein isoforms, it is conceivable that these different protein molecules could be responsible for the decarboxylation of other aromatic L-amino acids.
Homology Comparison of the amino acid sequence of DDC from different species, suggested that the enzyme is an evolutionarily conserved molecule. The amino acid sequence around the coenzyme binding lysine is also evolutionarily conserved (Bossa et al., 1977; Ichinose et al., 1989). The conserved amino acids are residues 267-317, which surround the PLP-binding site (Ichinose et al., 1989), as well as, the extended regions of amino acids 64-155 and 182-204, which according to Maras et al. (1991) are important for the enzyme's catalytic function (Maras et al., 1991). Table 2 shows the percentage of human DDC amino acid identity to other species (Maras et al., 1991; Mantzouridis et al., 1997).
 
  Table 2. Human DDC identity.

Mutations

 
  Table 3. The mutations of the DDC gene in the AADC disorder.
Germinal Such mutations have not been identified so far.
Somatic Aromatic L-amino acid decarboxylase (AADC) deficiency, a rare autosomaly-recessive inherited defect, is associated with mutations of the DDC gene. This disorder leads to profound modifications in the homeostasis of central and peripheral nervous system (Hyland et al., 1992). In their majority, such mutations are missense and are listed above (table 3). Other mutations of the human DDC gene that are related to AADC-deficiency are also included (Fiumara et al., 2002; Chang et al., 2004; Pons et al., 2004; Tay et al., 2007; Lee et al., 2009).

Implicated in

Entity Prostate cancer
Note Neuroendocrine differentiation features have been identified in prostatic adenocarcinoma. Aggressiveness of the disease is increased as the cells reach the androgen-independent phase (Speights et al., 1997; Nelson et al., 2002). L-Dopa decarboxylase has been identified as a novel androgen receptor (AR) coactivator protein (Wafa et al., 2003). Recent evidence have shown that the expression of DDC mRNA could serve as a potential novel biomarker in prostate cancer (Avgeris et al., 2008). Wafa et al. (2007) have indicated by immunohistochemistry that DDC was found to be a putative neuroendocrine marker for prostate cancer. In certain NE tumor cells of the prostate gland, DDC was found to be co-expressed with AR. DDC expression was increased after hormone-ablation therapy, as well as, in metastatic tumors that have progressed to the androgen-independent phenotypes (Wafa et al., 2007).
Disease Increased DDC mRNA and/or elevated protein expression levels were detected in the LnCaP cell line following synthetic androgen treatment. DDC protein was found to be enzymatically active in the androgen-treated LnCaP cells as compared to the untreated controls. In treated LnCaP cells, DDC was up-regulated during AR-activation, while DDC expression was down-regulated following AR-inhibition. These findings support a coactivator role for DDC in AR activation (Shao et al., 2007). DDC over-expression affects the gene expression profile of the androgen-dependent prostate cancer cell line, LnCaP, as revealed by microarray analysis (Margiotti et al., 2007).
Prognosis Statistically significant elevated DDC mRNA levels were observed in prostate cancer tissue specimens when compared to benign hyperplasia human samples. Multivariate survival analysis indicated that the expression of the DDC gene could be used as an independent marker for the differential diagnosis between prostate cancer and benign hyperplasia patients, using tissue biopsies. DDC mRNA expression was also shown to be associated with advanced tumor stage and higher Gleason score. This finding suggested an unfavorable prognostic value for DDC expression in patients with tumors in their prostate glands (Avgeris et al., 2008).
  
Entity Colorectal carcinoma
Note High L-Dopa decarboxylase activity has been detected in almost half of the original colorectal carcinomas examined, as well as, in the majority of cultured cell lines, established from human primary and metastatic tumors (Park et al., 1987). Other data have shown that most solid colorectal tumors exhibited DDC activity at lower levels when compared to the enzymatic DDC activity displayed by the NE tumors (Gazdar et al., 1988). DDC mRNA expression was found to be elevated in well-differentiated (grade I) intestinal adenocarcinomas as compared to more aggressive tumors (Kontos et al., 2010).
Prognosis Increased DDC mRNA levels were observed in grade I colorectal adenocarcinomas. Survival analysis revealed a significantly lower risk of disease recurrence and longer overall survival for patients with DDC-positive colorectal neoplasms. These results indicate that DDC mRNA expression might represent a possible future biomarker for the prognosis of colorectal cancer patients (Kontos et al., 2010).
  
Entity Gastric cancer
Note Advanced gastric cancer is characterized by peritoneal dissemination, the most common disease relapse, which is caused by the dispersal of free gastric cancer cells into the peritoneal cavity (Baba et al., 1989; Abe et al., 1995).
Disease It has been proposed that increased DDC mRNA expression could be an accurate tool for the detection of gastric cancer micrometastases in the peritoneal cavity. According to Sakakura et al. (2004), DDC expression levels were equivalent to the degree of dissemination potential of gastric cancer cells.
  
Entity Pheochromocytomas
Note Pheochromocytomas are characterized by over-production of catecholamines (Eisenhofer et al., 2001).
Disease These non-innervated tumors originate, in most cases, from adrenal medullary cells which are capable for catecholamine biosynthesis (Yanase et al., 1986). Catecholamine release by these cells is not initiated by nerve impulses. Elevated DDC mRNA levels have been detected in pheochromocytoma tissues as compared to normal adrenal medullary cells. Isobe et al. (1998) suggested that high DDC expression could lead to the development or growth of pheochromocytomas (Isobe et al., 1998).
  
Entity Neuroblastomas
Note In the neuroblastoma cell line, the SH-SY5Y cells, both neural full-length DDC mRNA and the neural mRNA isoform lacking exon 3, were detected (Chalatsa et al., 2011).
Disease Neuroblastomas, the most common extracranial solid neoplasms in children, originate from sympathetic neural crest cells and their characteristic is the production of catecholamines and their metabolites (Boomsma et al., 1989). Neuroblastomas are categorized as small round-cell tumors of the childhood (Gilbert et al., 1999). In the active untreated state, plasma L-Dopa values and/or DDC enzymatic activity levels have been found to be elevated. Interestingly, following chemotherapy treatment, DDC enzymatic activity levels fall within the physiological range. Elevated levels of plasma L-Dopa and especially DDC enzyme activity are observed during disease relapse (Boomsma et al., 1989).
It is noted that conventional light microscopy cannot clearly differentiate between neuroblastoma and other small round-cell tumors of the childhood. Co-expression of DDC and Tyrosine Hydroxylase (TH) has been used for the differential diagnosis of these types of tumors (Gilbert et al., 1999).
Prognosis Elevated levels of plasma L-Dopa, in neuroblastoma patients, could provide an indication for residual tumor. These findings could be associated with dismal prognosis for neuroblastoma patients. Furthermore, a sharp increase in plasma DDC enzymatic activity could be related to disease reccurence (Boomsma et al., 1989). DDC mRNA was detected in all bone marrow and peripheral blood samples obtained from neuroblastoma patients at relapse. Given these results, Bozzi et al. (2004) have suggested that DDC mRNA expression could represent a specific molecular marker for monitoring bone marrow and peripheral blood neuroblastoma metastases (Bozzi et al., 2004). Furthermore, DDC mRNA levels could be used as a sensitive indicator to predict minimal residual disease as well as the outcome for patients (Träger et al., 2008).
  
Entity Lung carcinomas
Note Elevated DDC enzymatic activity was observed in small-cell lung carcinoma (SCLC) as compared to normal lung epithelia (Nagatsu et al., 1985). The majority of non-SCLC (NSCLC) exhibited low levels or no DDC enzyme activity (Gazdar et al., 1981; Bepler et al., 1988). It is noted that in some NSCLC cases, high DDC activity values have been reported (Baylin et al., 1980), although in these lung lesions the detection of DDC activity was restricted to large-cell carcinomas and adenocarcinomas, while squamous cell carcinomas did not exhibit any enzymatic activity (Gazdar et al., 1988).
Disease DDC activity appears to be a valuable neuroendocrine marker for identifying SCLC tumor cells in culture (Baylin et al., 1980). DDC enzymatic activity is highest during the exponential cellular growth phase and/or when the cells are during the transition from G2 to the M phase of the cell cycle (Francis et al., 1983). DDC activity has been also used as a useful biomarker for the distinction of SCLC from NSCLC. Furthermore, DDC activity has been used for the differentiation between the classical SCLC cell lines (SCLC-C), which express high DDC activity levels, from the variant subtype of the SCLC (SCLC-V), which does not express the enzyme (Carney et al., 1985; Gazdar et al., 1985).
Prognosis The elevated DDC enzymatic activity, which is observed in patients harboring SCLC tumors, seems to be associated with disease differentiation grade. High DDC activity has been associated with better prognosis and patient's outcome (Bepler et al., 1987).
  
Entity Medullary thyroid carcinoma
Note The expression of L-Dopa decarboxylase has been detected in medullary carcinoma of the thyroid gland (Pearse, 1969; Atkins et al., 1973).
Disease Medullary thyroid carcinoma (MTC) originates from the calcitonin (CT)-secreting thyroid C cells and is a unique malignancy of endocrine origin (Tashjian and Melvin, 1968). Malignancy progression could be monitored, in patients with the virulent phenotype of the disease, using the simultaneous increased levels of DDC and histaminase (Trump et al., 1979; Lippman et al., 1982). It has been proposed that increased DDC enzymatic activity might represent an early differentiation marker in the virulent form of this neoplasm (Berger et al., 1984).
  
Entity Neuroendocrine tumors (NETs): bronchial, liver and ileal carcinoids, gastric / pancreatic / pulmonary tumors
Note DDC enzymatic activity constitutes an excellent cellular marker for identifying tumors of the neuroendocrine (NE) origin. The majority of NE tumors tested were found to express relatively high DDC enzymatic activity (Gazdar et al., 1988). DDC expression and/or activity have been reported in NETs, particularly in SCLC. For these reasons, DDC has been considered as a general endocrine marker (Gazdar et al., 1988; Jensen et al., 1990).
Disease Strikingly higher DDC mRNA expression levels were revealed in all bronchial carcinoids and pulmonary NETs when compared to their normal corresponding types of tissues. Immunohistochemical data have confirmed DDC protein expression in all of these tumors. In the gastroenteropancreatic NETs examined, the detected DDC mRNA levels were comparable to those of normal gastric, ileal and pancreatic tissues. Almost half of the pancreatic and stomach NETs and all ileal carcinoids were found to be DDC immunoreactive (Uccella et al., 2006). Interestingly, hepatic carcinoid tumors demonstrated a 20-fold increase in DDC activity as compared with normal surrounding liver tissues (Gilbert et al., 1995).
Hybrid/Mutated Gene Not yet discovered.
  

External links

Nomenclature
HGNC (Hugo)DDC   2719
Cards
AtlasDDCID50590ch7p12
Entrez_Gene (NCBI)DDC  1644  dopa decarboxylase (aromatic L-amino acid decarboxylase)
GeneCards (Weizmann)DDC
Ensembl (Hinxton)ENSG00000132437 [Gene_View]  chr7:50526134-50628768 [Contig_View]  DDC [Vega]
ICGC DataPortalENSG00000132437
AceView (NCBI)DDC
Genatlas (Paris)DDC
WikiGenes1644
SOURCE (Princeton)NM_000790 NM_001082971 NM_001242886 NM_001242887 NM_001242888 NM_001242889 NM_001242890
Genomic and cartography
GoldenPath (UCSC)DDC  -  7p12.1   chr7:50526134-50628768 -  7p12.1   [Description]    (hg19-Feb_2009)
EnsemblDDC - 7p12.1 [CytoView]
Mapping of homologs : NCBIDDC [Mapview]
OMIM107930   608643   
Gene and transcription
Genbank (Entrez)AJ310724 AK298321 AK298392 AU310260 AW772056
RefSeq transcript (Entrez)NM_000790 NM_001082971 NM_001242886 NM_001242887 NM_001242888 NM_001242889 NM_001242890
RefSeq genomic (Entrez)AC_000139 NC_000007 NC_018918 NG_008742 NT_007819 NW_001839007 NW_004929330
Consensus coding sequences : CCDS (NCBI)DDC
Cluster EST : UnigeneHs.359698 [ NCBI ]
CGAP (NCI)Hs.359698
Alternative Splicing : Fast-db (Paris)GSHG0028196
Alternative Splicing GalleryENSG00000132437
Gene ExpressionDDC [ NCBI-GEO ]     DDC [ SEEK ]   DDC [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP20711 (Uniprot)
NextProtP20711  [Medical]
With graphics : InterProP20711
Splice isoforms : SwissVarP20711 (Swissvar)
Catalytic activity : Enzyme4.1.1.28 [ Enzyme-Expasy ]   4.1.1.284.1.1.28 [ IntEnz-EBI ]   4.1.1.28 [ BRENDA ]   4.1.1.28 [ KEGG ]   
Domaine pattern : Prosite (Expaxy)DDC_GAD_HDC_YDC (PS00392)   
Domains : Interpro (EBI)Aromatic_deC    PyrdxlP-dep_de-COase    PyrdxlP-dep_Trfase    PyrdxlP-dep_Trfase_major_sub1    PyrdxlP-dep_Trfase_major_sub2    Pyridoxal-P_BS   
Related proteins : CluSTrP20711
Domain families : Pfam (Sanger)Pyridoxal_deC (PF00282)   
Domain families : Pfam (NCBI)pfam00282   
DMDM Disease mutations1644
Blocks (Seattle)P20711
PDB (SRS)3RBF    3RBL    3RCH   
PDB (PDBSum)3RBF    3RBL    3RCH   
PDB (IMB)3RBF    3RBL    3RCH   
PDB (RSDB)3RBF    3RBL    3RCH   
Human Protein AtlasENSG00000132437
Peptide AtlasP20711
HPRD00145
IPIIPI00025394   IPI00927028   IPI00479686   IPI00926099   IPI00925677   IPI00927223   IPI01014794   IPI00968147   
Protein Interaction databases
DIP (DOE-UCLA)P20711
IntAct (EBI)P20711
FunCoupENSG00000132437
BioGRIDDDC
IntegromeDBDDC
STRING (EMBL)DDC
Ontologies - Pathways
QuickGOP20711
Ontology : AmiGOaromatic-L-amino-acid decarboxylase activity  aromatic-L-amino-acid decarboxylase activity  protein binding  cytosol  cellular amino acid metabolic process  circadian rhythm  synaptic vesicle  multicellular organismal aging  synaptic vesicle amine transport  amino acid binding  protein domain specific binding  pyridoxal phosphate binding  axon  isoquinoline alkaloid metabolic process  cellular nitrogen compound metabolic process  cellular response to drug  dopamine biosynthetic process  catecholamine biosynthetic process  serotonin biosynthetic process  neuronal cell body  small molecule metabolic process  indolalkylamine biosynthetic process  response to pyrethroid  phytoalexin metabolic process  extracellular vesicular exosome  cellular response to alkaloid  cellular response to growth factor stimulus  
Ontology : EGO-EBIaromatic-L-amino-acid decarboxylase activity  aromatic-L-amino-acid decarboxylase activity  protein binding  cytosol  cellular amino acid metabolic process  circadian rhythm  synaptic vesicle  multicellular organismal aging  synaptic vesicle amine transport  amino acid binding  protein domain specific binding  pyridoxal phosphate binding  axon  isoquinoline alkaloid metabolic process  cellular nitrogen compound metabolic process  cellular response to drug  dopamine biosynthetic process  catecholamine biosynthetic process  serotonin biosynthetic process  neuronal cell body  small molecule metabolic process  indolalkylamine biosynthetic process  response to pyrethroid  phytoalexin metabolic process  extracellular vesicular exosome  cellular response to alkaloid  cellular response to growth factor stimulus  
Pathways : KEGGHistidine metabolism    Tyrosine metabolism    Phenylalanine metabolism    Tryptophan metabolism    Serotonergic synapse    Dopaminergic synapse    Cocaine addiction    Amphetamine addiction    Alcoholism   
REACTOMEP20711 [protein]
REACTOME PathwaysREACT_111217 Metabolism [pathway]
Protein Interaction DatabaseDDC
Wikipedia pathwaysDDC
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)DDC
SNP (GeneSNP Utah)DDC
SNP : HGBaseDDC
Genetic variants : HAPMAPDDC
1000_GenomesDDC 
ICGC programENSG00000132437 
CONAN: Copy Number AnalysisDDC 
Somatic Mutations in Cancer : COSMICDDC 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
DECIPHER (Syndromes)7:50526134-50628768
Mutations and Diseases : HGMDDDC
OMIM107930    608643   
MedgenDDC
GENETestsDDC
Disease Genetic AssociationDDC
Huge Navigator DDC [HugePedia]  DDC [HugeCancerGEM]
Genomic VariantsDDC  DDC [DGVbeta]
Exome VariantDDC
dbVarDDC
ClinVarDDC
snp3D : Map Gene to Disease1644
General knowledge
Homologs : HomoloGeneDDC
Homology/Alignments : Family Browser (UCSC)DDC
Phylogenetic Trees/Animal Genes : TreeFamDDC
Chemical/Protein Interactions : CTD1644
Chemical/Pharm GKB GenePA140
Clinical trialDDC
Cancer Resource (Charite)ENSG00000132437
Other databases
Probes
Litterature
PubMed87 Pubmed reference(s) in Entrez
CoreMineDDC
GoPubMedDDC
iHOPDDC

Bibliography

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PMID 436828
 
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Levels of creatine kinase and its BB isoenzyme in lung cancer specimens and cultures.
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PMID 6265067
 
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PMID 7271902
 
The prognostic and biological significance of cellular heterogeneity in medullary thyroid carcinoma: a study of calcitonin, L-dopa decarboxylase, and histaminase.
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J Clin Endocrinol Metab. 1982 Feb;54(2):233-40.
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Written05-2011Dimitra Florou, Andreas Scorilas, Dido Vassilacopoulou, Emmanuel G Fragoulis
Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Athens 15701, Panepistimiopolis, Athens, Greece

Citation

This paper should be referenced as such :
Florou, D ; Scorilas, A ; Vassilacopoulou, D ; Fragoulis, EG
DDC (dopa decarboxylase (aromatic L-amino acid decarboxylase))
Atlas Genet Cytogenet Oncol Haematol. 2011;15(11):942-950.
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