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Release of membrane-associated L-dopa decarboxylase from human cells.

Authors
  • Chalatsa, Ioanna
  • Fragoulis, Emmanuel G
  • Vassilacopoulou, Dido
Type
Published Article
Journal
Neurochemical Research
Publisher
Springer-Verlag
Publication Date
Aug 01, 2011
Volume
36
Issue
8
Pages
1426–1434
Identifiers
DOI: 10.1007/s11064-011-0468-4
PMID: 21479916
Source
Medline
License
Unknown

Abstract

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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