Discrete structural domains and cell-specific expression determine functional selectivity of the dopamine and norepinephrine transporters.

Kari Buck, D. Lorang, S. G. Amara

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The successful generation and functional expression of a series of recombinant chimeric transporters, in which distinct functional properties of NET and DAT are exchanged, have allowed the assignment of a number of important functional properties of MPP+ and antidepressant-sensitive catecholamine transporters to specific domains within their primary structure. These studies are the first comprehensive structure-function analysis of members of the rapidly growing superfamily of Na+/Cl- carriers using chimeric transporters. This represents the first step in identifying the specific structural or regulatory determinants that differentiate NET and DAT. An appreciation of the potentially distinct sites for substrate recognition, translocation, and transport inhibition of NET and DAT may facilitate the development of more selective drugs for the treatment of stimulant addiction, human depression, and other affective disorders.

Original languageEnglish (US)
Pages (from-to)154-175
Number of pages22
JournalNIDA research monograph
Volume161
StatePublished - 1996

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Norepinephrine Plasma Membrane Transport Proteins
Dopamine Plasma Membrane Transport Proteins
Mood Disorders
Antidepressive Agents
Catecholamines
Depression
Pharmaceutical Preparations
Recognition (Psychology)
Inhibition (Psychology)

ASJC Scopus subject areas

  • Medicine (miscellaneous)

Cite this

Discrete structural domains and cell-specific expression determine functional selectivity of the dopamine and norepinephrine transporters. / Buck, Kari; Lorang, D.; Amara, S. G.

In: NIDA research monograph, Vol. 161, 1996, p. 154-175.

Research output: Contribution to journalArticle

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