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Putative cocaine receptor in striatum is a glycoprotein with active thiol function
1Department of Pharmacology and Experimental Therapeutics, University of Maryland School of Medicine, Baltimore 21201.
Membrane Biochemistry
|January 1, 1989
Summary
Dopamine transporters are glycoproteins with crucial thiol groups. Lectins like Concanavalin A alter transporter conformation, affecting dopamine and cocaine binding.
Area of Science:
- Neuroscience
- Biochemistry
Background:
- Dopamine transporters (DATs) are crucial for regulating dopaminergic neurotransmission.
- Understanding DAT structure and function is key to developing targeted therapies.
Purpose of the Study:
- To investigate the molecular characteristics of dopamine transporters.
- To explore the effects of lectins and sulfhydryl reagents on DAT function.
Main Methods:
- Utilized [3H]cocaine binding and [3H]dopamine uptake assays in bovine and rat striata.
- Examined the influence of Concanavalin A, mercury reagents, and various sulfhydryl compounds.
Main Results:
- Lectins, such as Concanavalin A, potentiated DAT activity, suggesting a glycoprotein nature and conformational changes.
- Sulfhydryl reagents differentially affected DAT binding and uptake, indicating the importance of thiol groups.
- Mercury reagents and n-ethylmaleimide showed potent inhibition, while dithio reagents suggested a role for disulfide bonds.
Conclusions:
- Dopamine transporters possess glycoprotein features and critical thiol groups essential for their function.
- Specific chemical modifications can alter DAT conformation and activity, offering insights into transporter regulation.