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

Written2011-05Dimitra Florou, Andreas Scorilas, Dido Vassilacopoulou, Emmanuel G Fragoulis
Department of Biochemistry, Molecular Biology, Faculty of Biology, University of Athens 15701, Panepistimiopolis, Athens, Greece

(Note : for Links provided by Atlas : click)


HGNC Alias symbAADC
HGNC Alias namearomatic L-amino acid decarboxylase
LocusID (NCBI) 1644
Atlas_Id 50590
Location 7p12.1  [Link to chromosome band 7p12]
Location_base_pair Starts at 50492647 and ends at 50561071 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping DDC.png]
Local_order Centromere to telomere.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)


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.


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 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 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.


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Blood Cells Mol Dis. 2009b Jan-Feb;42(1):92-8. Epub 2008 Nov 28.
PMID 19041269
Quantitative expression analysis and prognostic significance of L-DOPA decarboxylase in colorectal adenocarcinoma.
Kontos CK, Papadopoulos IN, Fragoulis EG, Scorilas A.
Br J Cancer. 2010 Apr 27;102(9):1384-90.
PMID 20424616
Identification of a neuron-specific promoter of human aromatic L-amino acid decarboxylase gene.
Le Van Thai A, Coste E, Allen JM, Palmiter RD, Weber MJ.
Brain Res Mol Brain Res. 1993 Mar;17(3-4):227-38.
PMID 8510497
Aromatic L-amino acid decarboxylase deficiency in Taiwan.
Lee HF, Tsai CR, Chi CS, Chang TM, Lee HJ.
Eur J Paediatr Neurol. 2009 Mar;13(2):135-40. Epub 2008 Jun 24.
PMID 18567514
Mechanisms underlying the effects of 5-hydroxytryptamine and 5-hydroxytryptophan in pancreatic islets. A proposed role for L-aromatic amino acid decarboxylase.
Lindstrom P, Sehlin J.
Endocrinology. 1983 Apr;112(4):1524-9.
PMID 6339207
The prognostic and biological significance of cellular heterogeneity in medullary thyroid carcinoma: a study of calcitonin, L-dopa decarboxylase, and histaminase.
Lippman SM, Mendelsohn G, Trump DL, Wells SA Jr, Baylin SB.
J Clin Endocrinol Metab. 1982 Feb;54(2):233-40.
PMID 6798062
Aromatic L-amino acid decarboxylase.
Lovenberg W, Weissbach H, Udenfriend S.
J Biol Chem. 1962 Jan;237:89-93.
PMID 14466899
cDNA cloning of L-dopa decarboxylase from the eclosion stage of the insect Ceratitis capitata. Evolutionary relationship to other species decarboxylases.
Mantzouridis TD, Sideris DC, Fragoulis EG.
Gene. 1997 Dec 19;204(1-2):85-9.
PMID 9434169
Purification and characterization of L-dopa decarboxylase from human kidney.
Mappouras DG, Stiakakis J, Fragoulis EG.
Mol Cell Biochem. 1990 May 10;94(2):147-56.
PMID 2374548
Pig kidney 3,4-dihydroxyphenylalanine (dopa) decarboxylase. Primary structure and relationships to other amino acid decarboxylases.
Maras B, Dominici P, Barra D, Bossa F, Voltattorni CB.
Eur J Biochem. 1991 Oct 15;201(2):385-91.
PMID 1935935
Androgen-regulated genes differentially modulated by the androgen receptor coactivator L-dopa decarboxylase in human prostate cancer cells.
Margiotti K, Wafa LA, Cheng H, Novelli G, Nelson CC, Rennie PS.
Mol Cancer. 2007 Jun 6;6:38.
PMID 17553164
Aromatic L-amino acid decarboxylase activities in human lung tissues: comparison between normal lung and lung carcinomas.
Nagatsu T, Ichinose H, Kojima K, Kameya T, Shimase J, Kodama T, Shimosato Y.
Biochem Med. 1985 Aug;34(1):52-9.
PMID 2996509
The program of androgen-responsive genes in neoplastic prostate epithelium.
Nelson PS, Clegg N, Arnold H, Ferguson C, Bonham M, White J, Hood L, Lin B.
Proc Natl Acad Sci U S A. 2002 Sep 3;99(18):11890-5. Epub 2002 Aug 16.
PMID 12185249
The human aromatic L-amino acid decarboxylase gene can be alternatively spliced to generate unique protein isoforms.
O'Malley KL, Harmon S, Moffat M, Uhland-Smith A, Wong S.
J Neurochem. 1995 Dec;65(6):2409-16.
PMID 7595534
Phenylethanolamine N-methyltransferase-containing neurons in rat retina: immunohistochemistry, immunochemistry, and molecular biology.
Park DH, Teitelman G, Evinger MJ, Woo JI, Ruggiero DA, Albert VR, Baetge EE, Pickel VM, Reis DJ, Joh TH.
J Neurosci. 1986 Apr;6(4):1108-13.
PMID 2871139
Characteristics of cell lines established from human colorectal carcinoma.
Park JG, Oie HK, Sugarbaker PH, Henslee JG, Chen TR, Johnson BE, Gazdar A.
Cancer Res. 1987 Dec 15;47(24 Pt 1):6710-8.
PMID 3479249
The cytochemistry and ultrastructure of polypeptide hormone-producing cells of the APUD series and the embryologic, physiologic and pathologic implications of the concept.
Pearse AG.
J Histochem Cytochem. 1969 May;17(5):303-13. (REVIEW)
PMID 4143745
Aromatic L-amino acid decarboxylase deficiency: clinical features, treatment, and prognosis.
Pons R, Ford B, Chiriboga CA, Clayton PT, Hinton V, Hyland K, Sharma R, De Vivo DC.
Neurology. 2004 Apr 13;62(7):1058-65. (REVIEW)
PMID 15079002
L-DOPA decarboxylase association with membranes in mouse brain.
Poulikakos P, Vassilacopoulou D, Fragoulis EG.
Neurochem Res. 2001 May;26(5):479-85.
PMID 11513473
Aromatic L-amino acid decarboxylase activity in central and peripheral tissues and serum of rats with L-DOPA and L-5-hydroxytryptophan as substrates.
Rahman MK, Nagatsu T, Kato T.
Biochem Pharmacol. 1981 Mar 15;30(6):645-9.
PMID 7271902
Modulation of retinal aromatic L-amino acid decarboxylase via alpha 2 adrenoceptors.
Rossetti Z, Krajnc D, Neff NH, Hadjiconstantinou M.
J Neurochem. 1989 Feb;52(2):647-52.
PMID 2536080
Aromatic L-amino acid decarboxylase is modulated by D1 dopamine receptors in rat retina.
Rossetti ZL, Silvia CP, Krajnc D, Neff NH, Hadjiconstantinou M.
J Neurochem. 1990 Mar;54(3):787-91.
PMID 2137529
Overexpression of dopa decarboxylase in peritoneal dissemination of gastric cancer and its potential as a novel marker for the detection of peritoneal micrometastases with real-time RT-PCR.
Sakakura C, Takemura M, Hagiwara A, Shimomura K, Miyagawa K, Nakashima S, Yoshikawa T, Takagi T, Kin S, Nakase Y, Fujiyama J, Hayasizaki Y, Okazaki Y, Yamagishi H.
Br J Cancer. 2004 Feb 9;90(3):665-71.
PMID 14760382
Human dopa decarboxylase: localization to human chromosome 7p11 and characterization of hepatic cDNAs.
Scherer LJ, McPherson JD, Wasmuth JJ, Marsh JL.
Genomics. 1992 Jun;13(2):469-71.
PMID 1612608
Biphasic effect of androgens on prostate cancer cells and its correlation with androgen receptor coactivator dopa decarboxylase.
Shao C, Wang Y, Yue HH, Zhang YT, Shi CH, Liu F, Bao TY, Yang ZY, Yuan JL, Shao GX.
J Androl. 2007 Nov-Dec;28(6):804-12. Epub 2007 Jun 20.
PMID 17581945
Cloning and expression of human placental L-Dopa decarboxylase.
Siaterli MZ, Vassilacopoulou D, Fragoulis EG.
Neurochem Res. 2003 Jun;28(6):797-803.
PMID 12718431
Activities of 3,4-dihydroxy-L-phenylalanine and 5-hydroxy-L-tryptophan decarboxylases in rat brain: assay characteristics and distribution.
Sims KL, Davis GA, Bloom FE.
J Neurochem. 1973 Feb;20(2):449-64.
PMID 4540567
Neuroendocrine stains and proliferative indices of prostatic adenocarcinomas in transurethral resection samples.
Speights VO Jr, Cohen MK, Riggs MW, Coffield KS, Keegan G, Arber DA.
Br J Urol. 1997 Aug;80(2):281-6.
PMID 9284203
Analysis of the alternative promoters that regulate tissue-specific expression of human aromatic L-amino acid decarboxylase.
Sumi-Ichinose C, Hasegawa S, Ichinose H, Sawada H, Kobayashi K, Sakai M, Fujii T, Nomura H, Nomura T, Nagatsu I, et al.
J Neurochem. 1995 Feb;64(2):514-24.
PMID 7830043
Medullary carcinoma of the thyroid gland. Studies of thyrocalcitonin in plasma and tumor extracts.
Tashjian AH Jr, Melvin EW.
N Engl J Med. 1968 Aug 8;279(6):279-83.
PMID 5660301
Unusually mild phenotype of AADC deficiency in 2 siblings.
Tay SK, Poh KS, Hyland K, Pang YW, Ong HT, Low PS, Goh DL.
Mol Genet Metab. 2007 Aug;91(4):374-8. Epub 2007 May 29.
PMID 17533144
mRNAs of tyrosine hydroxylase and dopa decarboxylase but not of GD2 synthase are specific for neuroblastoma minimal disease and predicts outcome for children with high-risk disease when measured at diagnosis.
Trager C, Vernby A, Kullman A, Ora I, Kogner P, Kagedal B.
Int J Cancer. 2008 Dec 15;123(12):2849-55.
PMID 18814238
Discordance between plasma calcitonin and tumor-cell mass in medullary thyroid carcinoma.
Trump DL, Mendelsohn G, Baylin SB.
N Engl J Med. 1979 Aug 2;301(5):253-5.
PMID 449992
Histidine decarboxylase, DOPA decarboxylase, and vesicular monoamine transporter 2 expression in neuroendocrine tumors: immunohistochemical study and gene expression analysis.
Uccella S, Cerutti R, Vigetti D, Furlan D, Oldrini R, Carnevali I, Pelosi G, La Rosa S, Passi A, Capella C.
J Histochem Cytochem. 2006 Aug;54(8):863-75. Epub 2006 Mar 3.
PMID 16517981
Identification and characterization of a novel form of the human L-dopa decarboxylase mRNA.
Vassilacopoulou D, Sideris DC, Vassiliou AG, Fragoulis EG.
Neurochem Res. 2004 Oct;29(10):1817-23.
PMID 15532536
Detection, purification and identification of an endogenous inhibitor of L-Dopa decarboxylase activity from human placenta.
Vassiliou AG, Fragoulis EG, Vassilacopoulou D.
Neurochem Res. 2009 Jun;34(6):1089-100. Epub 2008 Nov 13.
PMID 19005753
Subunit structure of 3, 4-dihydroxyphenylalanine decarboxylase from pig kidney.
Voltattorni CB, Minelli A, Cirotto C, Barra D, Turano C.
Arch Biochem Biophys. 1982 Aug;217(1):58-64.
PMID 7125679
Isolation and identification of L-dopa decarboxylase as a protein that binds to and enhances transcriptional activity of the androgen receptor using the repressed transactivator yeast two-hybrid system.
Wafa LA, Cheng H, Rao MA, Nelson CC, Cox M, Hirst M, Sadowski I, Rennie PS.
Biochem J. 2003 Oct 15;375(Pt 2):373-83.
PMID 12864730
Comprehensive expression analysis of L-dopa decarboxylase and established neuroendocrine markers in neoadjuvant hormone-treated versus varying Gleason grade prostate tumors.
Wafa LA, Palmer J, Fazli L, Hurtado-Coll A, Bell RH, Nelson CC, Gleave ME, Cox ME, Rennie PS.
Hum Pathol. 2007 Jan;38(1):161-70. Epub 2006 Sep 25.
PMID 16997353
Catecholamines and opioid peptides in human phaeochromocytomas.
Yanase T, Nawata H, Kato K, Ibayashi H.
Acta Endocrinol (Copenh). 1986 Nov;113(3):378-84.
PMID 3788413
Phorbol ester administration transiently increases aromatic L-amino acid decarboxylase activity of the mouse striatum and midbrain.
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J Neurochem. 1994 Aug;63(2):694-7.
PMID 8035193
Intronic variants in the dopa decarboxylase (DDC) gene are associated with smoking behavior in European-Americans and African-Americans.
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Hum Mol Genet. 2006 Jul 15;15(14):2192-9. Epub 2006 Jun 1.
PMID 16740595
Regulation of striatal aromatic L-amino acid decarboxylase: effects of blockade or activation of dopamine receptors.
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Eur J Pharmacol. 1993 Jul 20;238(2-3):157-64.
PMID 8104805


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.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)DDC   2719
Entrez_Gene (NCBI)DDC    dopa decarboxylase
GeneCards (Weizmann)DDC
Ensembl hg19 (Hinxton)ENSG00000132437 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000132437 [Gene_View]  ENSG00000132437 [Sequence]  chr7:50492647-50561071 [Contig_View]  DDC [Vega]
ICGC DataPortalENSG00000132437
TCGA cBioPortalDDC
Genatlas (Paris)DDC
SOURCE (Princeton)DDC
Genetics Home Reference (NIH)DDC
Genomic and cartography
GoldenPath hg38 (UCSC)DDC  -     chr7:50492647-50561071 -  7p12.2-p12.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)DDC  -     7p12.2-p12.1   [Description]    (hg19-Feb_2009)
GoldenPathDDC - 7p12.2-p12.1 [CytoView hg19]  DDC - 7p12.2-p12.1 [CytoView hg38]
Genome Data Viewer NCBIDDC [Mapview hg19]  
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
Consensus coding sequences : CCDS (NCBI)DDC
Gene ExpressionDDC [ NCBI-GEO ]   DDC [ EBI - ARRAY_EXPRESS ]   DDC [ SEEK ]   DDC [ MEM ]
Gene Expression Viewer (FireBrowse)DDC [ Firebrowse - Broad ]
GenevisibleExpression of DDC in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1644
GTEX Portal (Tissue expression)DDC
Human Protein AtlasENSG00000132437-DDC [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP20711   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP20711  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP20711
Catalytic activity : Enzyme4.1.1.28 [ Enzyme-Expasy ] [ IntEnz-EBI ] [ BRENDA ] [ KEGG ]   [ MEROPS ]
Domaine pattern : Prosite (Expaxy)DDC_GAD_HDC_YDC (PS00392)   
Domains : Interpro (EBI)Aromatic_deC    PyrdxlP-dep_de-COase    PyrdxlP-dep_Trfase    PyrdxlP-dep_Trfase_dom1    PyrdxlP-dep_Trfase_major    Pyridoxal-P_BS   
Domain families : Pfam (Sanger)Pyridoxal_deC (PF00282)   
Domain families : Pfam (NCBI)pfam00282   
Conserved Domain (NCBI)DDC
PDB (RSDB)3RBF    3RBL    3RCH   
PDB Europe3RBF    3RBL    3RCH   
PDB (PDBSum)3RBF    3RBL    3RCH   
PDB (IMB)3RBF    3RBL    3RCH   
Structural Biology KnowledgeBase3RBF    3RBL    3RCH   
SCOP (Structural Classification of Proteins)3RBF    3RBL    3RCH   
CATH (Classification of proteins structures)3RBF    3RBL    3RCH   
AlphaFold pdb e-kbP20711   
Human Protein Atlas [tissue]ENSG00000132437-DDC [tissue]
Protein Interaction databases
IntAct (EBI)P20711
Ontologies - Pathways
Ontology : AmiGOaromatic-L-amino-acid decarboxylase activity  aromatic-L-amino-acid decarboxylase activity  protein binding  cytoplasm  cytosol  cellular amino acid metabolic process  catecholamine metabolic process  circadian rhythm  synaptic vesicle  multicellular organism aging  aminergic neurotransmitter loading into synaptic vesicle  amino acid binding  carboxy-lyase activity  enzyme binding  protein domain specific binding  pyridoxal phosphate binding  axon  isoquinoline alkaloid metabolic process  cellular response to drug  5-hydroxy-L-tryptophan decarboxylase activity  L-dopa decarboxylase activity  dopamine biosynthetic process  catecholamine biosynthetic process  serotonin biosynthetic process  neuronal cell body  indolalkylamine biosynthetic process  response to pyrethroid  phytoalexin metabolic process  extracellular 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  cytoplasm  cytosol  cellular amino acid metabolic process  catecholamine metabolic process  circadian rhythm  synaptic vesicle  multicellular organism aging  aminergic neurotransmitter loading into synaptic vesicle  amino acid binding  carboxy-lyase activity  enzyme binding  protein domain specific binding  pyridoxal phosphate binding  axon  isoquinoline alkaloid metabolic process  cellular response to drug  5-hydroxy-L-tryptophan decarboxylase activity  L-dopa decarboxylase activity  dopamine biosynthetic process  catecholamine biosynthetic process  serotonin biosynthetic process  neuronal cell body  indolalkylamine biosynthetic process  response to pyrethroid  phytoalexin metabolic process  extracellular 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 PathwaysR-HSA-209931 [pathway]   
NDEx NetworkDDC
Atlas of Cancer Signalling NetworkDDC
Wikipedia pathwaysDDC
Orthology - Evolution
GeneTree (enSembl)ENSG00000132437
Phylogenetic Trees/Animal Genes : TreeFamDDC
Homologs : HomoloGeneDDC
Homology/Alignments : Family Browser (UCSC)DDC
Gene fusions - Rearrangements
Fusion : FusionGDB4.1.1.28   
Fusion : QuiverDDC
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerDDC [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)DDC
Exome Variant ServerDDC
GNOMAD BrowserENSG00000132437
Varsome BrowserDDC
ACMGDDC variants
Genomic Variants (DGV)DDC [DGVbeta]
DECIPHERDDC [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisDDC 
ICGC Data PortalDDC 
TCGA Data PortalDDC 
Broad Tumor PortalDDC
OASIS PortalDDC [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICDDC  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DDDC
Mutations and Diseases : HGMDDDC
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)DDC
DoCM (Curated mutations)DDC
CIViC (Clinical Interpretations of Variants in Cancer)DDC
NCG (London)DDC
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM107930    608643   
Genetic Testing Registry DDC
NextProtP20711 [Medical]
Target ValidationDDC
Huge Navigator DDC [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDDDC
Pharm GKB GenePA140
Pharm GKB PathwaysPA161749006   PA162355621   PA2030   
Clinical trialDDC
DataMed IndexDDC
PubMed119 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Fri Oct 8 21:15:58 CEST 2021

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