期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 554, 期 -, 页码 28-35出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2014.05.006
关键词
Amino acid transporter (ATB(0,+)); Organic cation transporter (OCTN2); L-Carnitine; Blood-brain barrier; Protein kinase C
资金
- International PhD Studies in Neurobiology
- International PhD Project Programme of the Foundation for Polish Science
- European Union, Innovative Economy Operational Programme
Carnitine (3-hydroxy-4-trimethylammoniobutyrate) is necessary for transfer of fatty acids through the inner mitochondrial membrane. Carnitine, not synthesized in the brain, is delivered there through the strongly polarized blood-brain barrier (BBB). Expression and presence of two carnitine transporters - organic cation/carnitine transporter (OCTN2) and amino acid transporter B-0,B-+ (ATB(0,+)) have been demonstrated previously in an in vitro model of the BBB. Due to potential protein kinase C (PKC) phosphorylation sites within ATB(0,+) sequence, the present study verified effects of this kinase on transporter function and localization in the BBB. ATB(0,+) can be regulated by estrogen receptor a and up-regulated in vitro, therefore its presence in vivo was verified with the transmission electron microscopy. The analyses of brain slices demonstrated ATB(0,+) luminal localization in brain capillaries, confirmed by biotinylation experiments in an in vitro model of the BBB. Brain capillary endothelial cells were shown to control carnitine gradient. ATB(0,+) was phosphorylated by PKC, what correlated with inhibition of carnitine transport. PKC activation did not change the amount of ATB(0,+) present in the apical membrane of brain endothelial cells, but resulted in transporter exclusion from raft microdomains. ATB inactivation by a lateral movement in plasma membrane after transporter phosphorylation has been postulated. (C) 2014 Elsevier Inc. All rights reserved.
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