NA-DEPENDENT HIGH-AFFINITY UPTAKE OF CHOLINE INTO CULTURED FIBROBLASTS()

Citation
P. Schloss et al., NA-DEPENDENT HIGH-AFFINITY UPTAKE OF CHOLINE INTO CULTURED FIBROBLASTS(), Biochemical and biophysical research communications, 199(3), 1994, pp. 1320-1325
Citations number
16
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006291X
Volume
199
Issue
3
Year of publication
1994
Pages
1320 - 1325
Database
ISI
SICI code
0006-291X(1994)199:3<1320:NHUOCI>2.0.ZU;2-B
Abstract
The acetylcholine precursor choline is transported into cholinergic ne urons by a high-affinity, sodium-dependent mechanism that is selective ly localized to the cholinergic nerve terminal. In addition, a low-aff inity, sodium-independent choline uptake system is present in choliner gic and non-cholinergic cells which deliver choline for cell membrane anabolism. Here, we show that uptake of [H-3]choline into cultured fib roblast cell lines exhibits high affinity (Km less-than-or-equal-to 10 muM), is sodium-dependent, and is blocked by hemicholinium, a classic al inhibitor of neuronal high-affinity choline uptake. Our data indica te that sodium-dependent high-affinity choline transport systems are a lso present in non-cholinergic cells. (C) 1994 Academic Press, Inc.