Jan 1, 1976

Stimulation of rat striatal tyrosine hydroxylase by phospholipids and adenosine-3',5'-monophosphate

Arzneimittel-Forschung
J RaeseJ D Barchas

Abstract

Rat striatal tyrosine hydroxylase is stimulated in vitro by various phospholipids. This stimulation was produced by a 3- to 4-fold increase in affinity for pteridine cofactor. No change in the Km for tyrosine was observed, The sedimentation pattern of tyrosine hydroxylase on linear sucrose gradients showed no indication of enzyme dissociation in the presence of lysolecithin at maximal stimulatory concentration. Crude striatal tyrosine hydroxylase is also activated by a combination of ATP, Mg++, EGTA and cAMP. After removing these agents by Sephadex G-25 chromatography, the activated form of the enzyme can be further stimulated by lysolecithin. These results suggest a possible role for phospholipids in the regulation of striatal dopamine synthesis.

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Mentioned in this Paper

Lysolecithin
Adenosine
Sephadex G 25
Chromatography
Lentiform Nucleus Structure
Egtazic Acid
Cyclic AMP, (R)-Isomer
Sedimentation Procedure
Phospholipids
Tyrosine Measurement

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