Unraveling neuronal dopamine transporter mechanisms with rotating disk electrode voltammetry.
Herein we describe how the rotating disk electrode voltammetric technique can be used to examine the mechanism(s) of the inward transport of dopamine by the neuronal transporter for dopamine (DAT). The usefulness of making measurements kinetically resolving dopamine transport, interpretations of changes in Km and Vmax, approaches to defining pre-steady-state binding of dopamine to DAT, interactions between competing inhibitors, chemical modification of functional groups within DAT, and a presentation of a hypothetical multi-state model of dopamine transport are presented and discussed.
Schenk
James O
JO
Department of Chemistry, Washington State University, Pullman, WA 99164-4630, USA. geni@wsu.edu
Wright
Cortney
C
Bjorklund
Nicole
N
D000818:Animals; D001667:Binding, Competitive / Q000502:physiology; D001692:Biological Transport; D001923:Brain Chemistry / Q000502:physiology*; D004298:Dopamine / Q000737:chemistry / Q000378:metabolism*; D050483:Dopamine Plasma Membrane Transport Proteins; D004563:Electrochemistry; D004566:Electrodes; D006801:Humans; D007700:Kinetics; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism*; D009448:Neurochemistry / Q000295:instrumentation* / Q000379:methods*
D050483:Dopamine Plasma Membrane Transport Proteins; D008562:Membrane Glycoproteins; D026901:Membrane Transport Proteins; D009419:Nerve Tissue Proteins; C493214:SLC6A3 protein, human; D004298:Dopamine