Characterization of a novel brain-specific chloride-dependent glutamic acid transport
The apparent, chloride dependent binding of (/sup 3/H)-glutamate (CGB) to brain membranes has been proposed to label a physiological receptor. However, recent evaluation of the properties of (CBG) has led to the suggestion that it represents transport and sequestration. The purpose of the present work was to determine if CGB represents binding or transport. Our results indicate that CGB is sensitive to detergent and osmotic pertubations. Both association and dissociation of Glu are temperature dependent and the rate of dissociation is dependent on the amount of Glu in the incubation media. All these results indicate that CGB represents transport and sequestration. Synaptosomal chloride dependent Glu transport (CGT) was then characterized. This process has similar pharmacologic and ion stimulation profiles as CGB. It is concluded that these two phenomena represent the identical process. CGT is brain specific. Regional distribution, ontogenetic and lesion studies indicate that CGT is neuronal but is not associated with sodium dependent Glu uptake. These studies also indicate that CGT is either located post synaptically to Glu innervation or is not related to it. Finally, CGT is bidirectional and capable of homoexchange.
- Research Organization:
- Johns Hopkins Univ., Baltimore, MD (USA)
- OSTI ID:
- 5281592
- Resource Relation:
- Other Information: Thesis (Ph. D.)
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
GLUTAMIC ACID
CHEMICAL PROPERTIES
MEMBRANE TRANSPORT
BRAIN
CELL MEMBRANES
CHLORIDES
TEMPERATURE DEPENDENCE
TRACER TECHNIQUES
TRITIUM COMPOUNDS
AMINO ACIDS
BODY
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CENTRAL NERVOUS SYSTEM
CHLORINE COMPOUNDS
HALIDES
HALOGEN COMPOUNDS
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
MEMBRANES
NERVOUS SYSTEM
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANS
550201* - Biochemistry- Tracer Techniques