Journal of Nuclear Medicine, 47, 72P (2006)

 

[11C]-Phenethylguanidines: transport kinetics and binding affinities for the human norepinephrine transporter

 

David Raffel,1 Wei Chen,1 Yong Jung,1 David Gildersleeve,1 Nicholas Cozzi2

 

1Division of Nuclear Medicine, Department of Radiology, University of Michigan, Ann Arbor, MI

2Department of Pharmacology, University of Wisconsin School of Medicine and Public Health, Madison, WI  53706


Abstract

Objectives: [11C]-Phenethylguanidines ([11C]-PG) are a novel class of radiotracers for PET studies of cardiac sympathetic innervation. As analogs of the neurotransmitter norepinephrine, [11C]-PG are transported into sympathetic neurons by the norepinephrine transporter (NET). To better characterize the kinetics of [11C]-PG, their Michaelis-Menten constants Km and Vmax for NET transport were measured in vitro using rat C6 glial cells that stably express the human NET (C6-hNET cells). Binding affinities of PG for hNET (KD) were also measured.

Methods: Five [11C]-PGs were studied: [11C]-para-hydroxy-PG (PHPG); [11C]-meta-hydroxy-PG (MHPG); [11C]-4-fluoro-MHPG (4F-MHPG); [11C]-6-fluoro-MHPG (6F-MHPG); and [11C]-N-[guanyl]-meta-octopamine (GMO). For transport studies, C6-hNET cells were incubated for 5 min at 37°C with varying [11C]-PG concentrations. Km and Vmax were estimated by fitting specific uptake vs. [11C]-PG concentration to a one-site transport model. For competitive binding assays, homogenized and purified C6-hNET cell membranes were incubated with 1.5 nM [3H]mazindol at 22 °C for 3 hr in the absence (control binding) and presence of varying PG concentrations. KD was estimated by fitting % control binding vs. PG concentration to a monophasic inhibition process.

Results: KD, Km and Vmax values are given below, along with Vmax/Km ratios, which reflect each substrate’s NET transport rate. Comparable values for [11C]-meta-hydroxyephedrine (HED), [11C]-epinephrine (EPI), [3H]-norepinephrine (NE) and [3H]-dopamine (DA) are also shown. No correlation was found between KD, Km and Vmax, indicating that each constant is independently influenced by structural changes of NET substrates. C6-hNET transport rates (Vmax/Km) were highly correlated with neuronal transport rates measured previously in isolated rat heart (r = 0.96), suggesting that the measured transport constants Km and Vmax accurately reflect in vivo transport kinetics.

 

 


NET Substrate

KD (uM)

Km (uM)

Vmax

(pmol/min/mg protein)

Vmax/Km

(uL/min/mg protein)

PHPG

1.93 ± 0.20

0.52 ± 0.06

3.31 ± 0.40

6.42±1.12

MHPG

4.87 ± 0.47

0.73 ± 0.20

7.83 ± 1.73

11.2 ± 2.8

4F-MHPG

5.60 ± 0.49

2.57 ± 0.35

7.46± 0.64

2.96 ± 0.54

6F-MHPG

17.7 ± 0.5

2.86 ± 0.43

4.06± 0.66

1.44±0.31

GMO

20.3 ± 2.5

4.43 ± 0.31

5.57± 0.30

1.26±0.13

HED

43.2 ± 1.8

0.49 ± 0.11

5.20 ± 0.90

10.7 ± 0.9

NE

63.9 ± 2.3

0.28 ± 0.03

5.83 ± 0.49

21.3 ± 2.4

EPI

68.4 ± 7.6

3.16 ± 0.78

6.09 ± 1.04

1.97 ± 0.24

DA

8.12 ± 0.47

0.24 ± 0.04

2.91 ± 0.47

12.2 ± 1.8

Values are mean ± SD, N = 5 determinations

 

 

 


 

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