Authors
Ioanna Kokkinou, Eleftheria Nikolouzou, Alexandros Hatzimanolis, Emmanuel G Fragoulis, Dido Vassilacopoulou
Publication date
2009/1/1
Journal
Blood Cells, Molecules, and Diseases
Volume
42
Issue
1
Pages
92-98
Publisher
Academic Press
Description
L-DOPA decarboxylase (DDC) is a pyridoxal 5-phosphate (PLP)-dependent enzyme that catalyses the decarboxylation of L-DOPA to dopamine. Dopamine (DA) has been found to be a regulating factor of the proliferation and differentiation of different leukocyte subtypes. In the present study, we report the expression of the gene that codes for the L-DOPA decarboxylase in human peripheral leukocytes and in T-lymphocytes, as well as the simultaneous detection of both neural and non-neural type DDC mRNA in the cellular components of this specialized connective tissue type. Furthermore, we have detected the neural type DDC transcript which lacks exon 3 and the alternative 37 kD alt-DDC protein isoform which lacks exons 10–15 but includes an alternative exon 10 in human peripheral leukocytes. Treatment of white blood cells with Triton X-114 resulted in the recovery of DDC in the detergent enriched and …
Total citations
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Scholar articles
I Kokkinou, E Nikolouzou, A Hatzimanolis… - Blood Cells, Molecules, and Diseases, 2009