l-Dopa decarboxylase expression profile in human cancer cells

Chalatsa, Ioanna; Nikolouzou, Eleftheria; Fragoulis, Emmanuel G.; Vassilacopoulou, Dido

doi:10.1007/s11033-010-0196-x

Cited by 16 publications

(15 citation statements)

References 49 publications

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“…1: Panel c). Our work has also shown that HTB-14 cells are inactive towards the decarboxylation of L-Dopa, although they express the enzyme [14]. These data, along with the Triton X-114 separation results, argue against the possibility that the detected membrane-associated molecules are derived from the unspecific attachment of the soluble enzyme with membrane fraction and is in good agreement with the results of Kuhn et al [34] who reported the absence of TH in the aqueous phase in granule membranes after fractionation with Triton X-114.…”

Section: Temperature-induced Phase Separation Of Proteins In Triton Xsupporting

confidence: 64%

Release of Membrane-Associated L-Dopa Decarboxylase from Human Cells

2011

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L-Dopa Decarboxylase is a pyridoxal 5-phosphate (PLP)-dependent enzyme that catalyses the decarboxylation of L-Dopa to dopamine. In this study, we investigated the cellular topology of the active human enzyme. Fractionation of membranes from human cell lines, of neural and non-neural origin, by temperature-induced phase separation in Triton X-114 resulted in the detection of DDC molecules in all separation phases. Solubilization of membrane-associated DDC was observed in a pH and time-dependent manner and was affected by divalent cations and protease inhibitors, suggesting the involvement of a possible release mechanism. The study of the biological properties and function of the solubilization phenomenon described here, as well as, the study of the membrane-associated enzyme could provide us with new information about the participation of the human L-Dopa decarboxylase in physiological and aberrant processes.

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Section: Temperature-induced Phase Separation Of Proteins In Triton Xsupporting

confidence: 64%

Release of Membrane-Associated L-Dopa Decarboxylase from Human Cells

2011

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“…Alternative promoter usage, combined with alternative splicing within the 5′-untranslated region (5′ UTR), gives rise to two different mRNA transcripts, designated neuronal and non-neuronal, but the proteins encoded by these mRNAs are identical [27,28,29,30]. The neuronal type transcript has also been detected in non-neuronal human tissues, such as placenta, kidney, and leukocytes [28,31,32,33] and, more recently, in liver cells [21]. Alternative splicing events have also been reported within the coding region of the gene [34,35].…”

Section: Introductionmentioning

confidence: 99%

Emerging Role of l-Dopa Decarboxylase in Flaviviridae Virus Infections

Frakolaki

Kalliampakou

Kaimou

et al. 2019

Cells

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l-dopa decarboxylase (DDC) that catalyzes the biosynthesis of bioactive amines, such as dopamine and serotonin, is expressed in the nervous system and peripheral tissues, including the liver, where its physiological role remains unknown. Recently, we reported a physical and functional interaction of DDC with the major signaling regulator phosphoinosite-3-kinase (PI3K). Here, we provide compelling evidence for the involvement of DDC in viral infections. Studying dengue (DENV) and hepatitis C (HCV) virus infection in hepatocytes and HCV replication in liver samples of infected patients, we observed a negative association between DDC and viral replication. Specifically, replication of both viruses reduced the levels of DDC mRNA and the ~120 kDa SDS-resistant DDC immunoreactive functional complex, concomitant with a PI3K-dependent accumulation of the ~50 kDa DDC monomer. Moreover, viral infection inhibited PI3K-DDC association, while DDC did not colocalize with viral replication sites. DDC overexpression suppressed DENV and HCV RNA replication, while DDC enzymatic inhibition enhanced viral replication and infectivity and affected DENV-induced cell death. Consistently, we observed an inverse correlation between DDC mRNA and HCV RNA levels in liver biopsies from chronically infected patients. These data reveal a novel relationship between DDC and Flaviviridae replication cycle and the role of PI3K in this process.

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“…These protein isoforms might participate in metabolic processes having alternative functions (Adamopoulos et al, 2019). For example, HeLa and HTB14 (human glioblastoma) coexpress the non-neural full-length DDC mRNA and the alternative neural transcript lacking exon 3, but no enzymatic activity is detectable in the cellular extracts (Chalatsa et al, 2011). Nevertheless, T98G cells do not seem to express the gene coding DDC (Functional Annotation of the Mammalian Genome, 2012).…”

Section: Discussionmentioning

confidence: 99%