TY - JOUR
T1 - L-DOPA decarboxylase association with membranes in mouse brain
AU - Poulikakos, Poulikos
AU - Vassilacopoulou, Dido
AU - Fragoulis, Emmanuel G.
N1 - Funding Information:
This work was partially supported by a Faculty Research Grant from the National Kapodostrian University of Athens and represents part of the Doctoral thesis of Mr. P. Poulikakos.
PY - 2001
Y1 - 2001
N2 - This work presents evidence on the association of active DDC molecules with membranes in mammalian brain. L-DOPA decarboxylase (DDC) is generally considered to be a cytosolic enzyme, Membrane-associated DDC was detected by immunoblotting and enzymatic assay experiments. DDC activity and immunoreactivity could be partially extracted from mammalian brain membranes by detergent. Fractionation of membranes by temperature-induced phase separation in Triton X-114, resulted in the recovery of membrane-associated DDC in separation phases where integral and hydrophobic membrane proteins separate. Treatment of membranes with phosphatidylinositol-specific phospholipase C or proteinase K, did not elute membrane-associated DDC activity, suggesting that a population of DDC molecules exist embedded within membranes. The elucidation of the functional significance of the enzyme's association with membranes could provide us with new information leading to the better understanding of the biological pathways that DDC is involved in.
AB - This work presents evidence on the association of active DDC molecules with membranes in mammalian brain. L-DOPA decarboxylase (DDC) is generally considered to be a cytosolic enzyme, Membrane-associated DDC was detected by immunoblotting and enzymatic assay experiments. DDC activity and immunoreactivity could be partially extracted from mammalian brain membranes by detergent. Fractionation of membranes by temperature-induced phase separation in Triton X-114, resulted in the recovery of membrane-associated DDC in separation phases where integral and hydrophobic membrane proteins separate. Treatment of membranes with phosphatidylinositol-specific phospholipase C or proteinase K, did not elute membrane-associated DDC activity, suggesting that a population of DDC molecules exist embedded within membranes. The elucidation of the functional significance of the enzyme's association with membranes could provide us with new information leading to the better understanding of the biological pathways that DDC is involved in.
KW - L-DOPA decarboxylase
KW - Membranes
KW - Mouse brain
KW - Phosphatidylinositol-specific phospholipase C
KW - Triton X-114
UR - http://www.scopus.com/inward/record.url?scp=0034885860&partnerID=8YFLogxK
U2 - 10.1023/A:1010952610387
DO - 10.1023/A:1010952610387
M3 - Article
C2 - 11513473
AN - SCOPUS:0034885860
SN - 0364-3190
VL - 26
SP - 479
EP - 485
JO - Neurochemical Research
JF - Neurochemical Research
IS - 5
M1 - 344504
ER -