ArticleNeurochemical research2009
Detection, purification and identification of an endogenous inhibitor of L-Dopa decarboxylase activity from human placenta.
Article in Neurochemical research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- L-Dopa-Decarboxylase (DDC) Is a Positive Prognosticator for Breast Cancer Patients and Epinephrine Regulates Breast Cancer Cell (MCF7 and T47D) Growth In Vitro According to Their Different Expression ofInternational journal of molecular sciences · 2020Article
- Article
- Dopamine synthesis and dopamine receptor expression are disturbed in recurrent miscarriages.Endocrine connections · 2018Article
- L-DOPA decarboxylase mRNA expression is associated with tumor stage and size in head and neck squamous cell carcinoma: a retrospective cohort study.BMC cancer · 2012Article
- Release of membrane-associated L-dopa decarboxylase from human cells.Neurochemical research · 2011Article
- L-Dopa decarboxylase expression profile in human cancer cells.Molecular biology reports · 2011Article
- Quantitative expression analysis and prognostic significance of L-DOPA decarboxylase in colorectal adenocarcinoma.British journal of cancer · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An endogenous inhibitor of L-Dopa decarboxylase activity was identified and purified from human placenta. The endogenous inhibitor of L-Dopa decarboxylase (Ddc) was localized in the membrane fraction of placental tissue. Treatment of membranes with phosphatidylinositol-specific phospholipase C or proteinase K did not affect membrane-associated Ddc inhibitory activity, suggesting that a population of the inhibitor is embedded within membranes. Purification was achieved by extraction from a nondenaturing polyacrylamide gel. The purification scheme resulted in the isolation of a single 35 kDa band, bearing L-Dopa decarboxylase inhibitory activity. The purified inhibitor was identified as Annexin V. The elucidation of the biological importance of the presence of an L-Dopa decarboxylase activity inhibitor in normal human tissues could provide us with new information leading to the better understanding of the biological pathways that Ddc is involved in.
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Registered trials
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